Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
,
Election/Restrictions
Applicant’s election without traverse of Species A (i.e., a single and specific glycan binding molecule as SEQ ID NO: 17); and Species B (i.e., a single and specific patient population to be treated/prevented as a SARS-CoV-2 infection) in the reply filed on July 9, 2025, is acknowledged.
Status of Claims
Claims 1-21 were originally filed on August 30, 2022.
The amendment received on August, 2022, canceled claims 13 and 18; and amended claims 1-12, 14-17, and 19-21. The amendment received on April 28, 2026, canceled claims 5-6; amended claims 1, 7, 16, 19, and 21; and added new claims 22-24.
Claims 1-4, 7-12, 14-17, and 19-24 are currently pending and claims 1, 8, 16, 19-24 are under consideration as claims 2-4, 7, 9-12, 14-15, and 17 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on July 9, 2025.
Priority
The present application claims status as a 371 (National Stage) of PCT/EP2021/055515 filed March 4, 2021, and claims priority under 119(a)-(d) to British Application Nos. 2003232.2 filed on March 5, 2020; 2004998.7 filed on April 4, 2020; and 2006160.2 file April 27, 2020.
Receipt is acknowledged of papers submitted under 35 U.S.C. 119(a)-(d) for the British applications, which papers have been placed of record in the file. Please note that the British applications are in English and therefore no further action is necessary.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on July 6, 2026, is being considered by the examiner.
Claim Interpretation
For purposes of applying prior art, the claim scope has been interpreted as set forth below per the guidance set forth at MPEP § 2111. If Applicant disputes any interpretation set forth below, Applicant is invited to unambiguously identify any alleged misinterpretations or specialized definitions in the subsequent response to the instant action. Applicant is advised that a specialized definition should be properly supported and specifically identified (see, e.g., MPEP § 2111.01(IV), describing how Applicant may act as their own lexicographer).
Pursuant to MPEP 2111, the pending claims must be "given their broadest reasonable interpretation consistent with the specification." The Federal Circuit’s en banc decision in Phillips v. AWH Corp., 415 F.3d 1303, 1316, 75 USPQ2d 1321, 1329 (Fed. Cir. 2005) expressly recognized that the USPTO employs the "broadest reasonable interpretation" standard:
The Patent and Trademark Office ("PTO") determines the scope of claims in patent applications not solely on the basis of the claim language, but upon giving claims their broadest reasonable construction "in light of the specification as it would be interpreted by one of ordinary skill in the art." In re Am. Acad. of Sci. Tech. Ctr., 367 F.3d 1359, 1364[, 70 USPQ2d 1827, 1830] (Fed. Cir. 2004). Indeed, the rules of the PTO require that application claims must "conform to the invention as set forth in the remainder of the specification and the terms and phrases used in the claims must find clear support or antecedent basis in the description so that the meaning of the terms in the claims may be ascertainable by reference to the description." 37 CFR 1.75(d)(1).
Pursuant to MPEP 2111.01, under a broadest reasonable interpretation, words of the claim must be given their plain meaning, unless such meaning is inconsistent with the specification. The plain meaning of a term means the ordinary and customary meaning given to the term by those of ordinary skill in the art at the time of the invention.
For claims 1, 16, and 21, please note that the instant specification does not define what is meant by “treatment”. However, the instant specification provides examples/embodiments of what is covered by “treatment”. More specifically, the instant specification teaches that “treatment” may embrace a reduction in one or more symptoms associated with a disease/condition caused or contributed to by a Coronavirus infection such as a continuous cough, a fever, change/loss in/of taste/smell (See instant, pg. 4, 1st paragraph). As such, the plain and ordinary meaning of each term applies. “Treat” is defined as to manage a disease by medicinal, surgical, or other measures; to care for a patient medically or surgically (See Medical Dictionary, “Treat”, Medical Dictionary, available online at https://medical-dictionary.thefreedictionary.com/treat, 3 pages (accessed on 2022)).
Also, please note that “Coronavirus” is defined as embracing any virus classed as belonging to the Family Coronaviridiae and embraces the SARS Coronavirus, the MERS Coronavirus, and the SARS-CoV-2 Coronavirus along with all SARS-CoV-2 variants (See instant, pg. 3, 3rd to 4th paragraphs). As such, the Coronavirus infection to be treated or prevented encompasses any Coronavirus.
For claims 22-24, please note that the instant specification does not define what is meant by “prophylactically treating”. As such, the plain and ordinary meaning of each term applies. “Prophylactic” is defined as guarding from or preventing the spread or occurrence of disease or infection (See Merriam-Webster, “Prophylactic”, Merriam Webster Dictionary, available online at https://www.merriam-webster.com/dictionary/prophylactic, 9 pages (last updated August 2, 2026) at pg. 1). Thus, the scope of claims 22-24 encompasses where the administration of a glycan biding molecule guards from or prevents the spread or occurrence of a coronavirus infection and/or a disease or condition caused or contributed by a coronavirus in a subject.
Sequence Interpretation
For claim 20, please note that the Examiner is interpreting the scope as open-ended requiring 100% identity to SEQ ID NO: 17 with any N- and/or C-terminal additions. It is noted that Applicant’s elected SEQ ID NO: 17 is a fusion protein having a general structure of: CBMX1----CBMX2----TD where CBMX1 and CBMX2 are two identical monomers of instant SEQ ID NO: 6 (note: CBM40 derived from Streptococcus pneumoniae NanA sialidase) with three substitutions; namely, V239A, V246G, and A162P, TD is a trimerization domain derived from Pseudomonas aeruginosa sialidase (See GenBank Accession No. WP_411194140.1, 2 pages (2025) at residues 175/176 to 281) with two substitutions; namely, S342D and R403K, the first “----” is a peptide linker of GGGSG (i.e., instant SEQ ID NO: 21), and the second “----" is a peptide linker of GGSLG or GGSL. Moreover, regarding a glycan acid binding fragment of SEQ ID NO: 17, it is noted that there is no limit to the fragment thereby encompassing any fragment ranging from any dipeptide, a single CBM40 monomer, or an amino acid sequence with a deleted residue at the N- and/or C-terminus.
Response to Arguments
Applicant’s arguments, see Response, filed 4/28/26, with respect to the objection to the specification have been fully considered and are persuasive. The objection of specification has been withdrawn.
Applicant’s arguments, see Response, filed 4/28/26, with respect to the obviousness-type double patenting rejection have been fully considered and are persuasive. The rejection of claims 1, 8, 16, and 19-24 as being unpatentable over claims 1-5 of U.S. Patent No. 11,466,059 B2 in view of Matrosovich, et al., Top. Curr. Chem. 367:1-28 (2015), and Coronaviridae Study Group of the Intl. Committee on Taxonomy of Viruses, “The species Severe acute respiratory syndrome-related coronavirus: classifying 2019-nCoV and naming it SARS-CoV-2,” Nat. Microbiol. 5:536-544 (March 2, 2020) (hereinafter referred to as “CSG article”) has been withdrawn.
Applicant’s arguments, see Response, filed 4/28/26, with respect to the obviousness-type double patenting rejection have been fully considered and are persuasive. The rejection of claims 1, 8, 16, and 19-24 as being unpatentable over claims 1-2, 6, 9-13, and 15-17 of copending Application No. 17/929,862 (US Publication No. 2023/0036052 A1) in view Matrosovich, et al., Top. Curr. Chem. 367:1-28 (2015), and Coronaviridae Study Group of the Intl. Committee on Taxonomy of Viruses, “The species Severe acute respiratory syndrome-related coronavirus: classifying 2019-nCoV and naming it SARS-CoV-2,” Nat. Microbiol. 5:536-544 (March 2, 2020) (hereinafter referred to as “CSG article”) has been withdrawn.
New Objections
Specification
The disclosure is objected to because of the following informalities: on page 27, last paragraph to pg. 28, 1st paragraph, discusses amino acid linker sequences without an accompanying SEQ ID NO. Pursuant to MPEP 2422 and 37 CFR 1.821(a), any amino acid sequence at least 4 defined amino acids in length requires a sequence identifier. Additionally, please update the Sequence Listing, if necessary. Appropriate correction is required.
Maintained/Modified Rejections in light of Applicants’ Amendments
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1, 8, 16, and 19-24 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
Independent claim 1 includes a “glycan binding molecule comprising a carbohydrate binding module (CBM) of a Family 40 CBM or a Family 32 CBM”. Independent claim 16 includes a “CBM40”. Independent claim 21 includes a “glycan acid binding molecule” that is Sp2CBM40TD. Dependent claim 19 includes where the “CBM comprises a modified CBM comprising a wild type CBM sequence which has been modified to include one or more mutations”. Dependent claim 20 includes where the modified CBM comprises SEQ ID NO: 17 or a “glycan acid binding fragment thereof.” With respect to the Family 40 CBMs, the instant specification teaches that they encompass molecules of approximately 200 residues and are often found at the N-terminus of GH33 sialidases, but can be found inserted in the beta-propeller of GH33 sialidases (See instant, pg. 11, 3rd paragraph). Although the scope of claims 1 and 16 limit the CBMs to peptide-based CBMs, the structure of the peptide-based CBMs is vast without a common core structure or sequence shared among the species within the Family 40 CBMs needed for the modules to bind to a carbohydrate. Plus, the Family 40 CBM of claim 1 is not limited to full length CBMs, but rather include fragments and modified CBM amino acid sequences as recited in claims 19-20. The specification defines “modified” as referring to molecules which contain one or more mutations relative to a reference sequence (See instant, pg. 21, 6th paragraph) (emphasis added). A “reference sample” can be any wild type CBM sequence (See instant, pg. 21, 7th paragraph). Moreover, the specification teaches that a “mutation” can include any alteration to a wild-type CBM molecule (See instant, pg. 22, last paragraph). As such, a modified CBM40 encompasses where any wild type CBM40 derived from any organism has one or more mutations thereby encompassing any number of substitutions, deletions, insertions and/additions to the wild type CBM40 sequence. Similarly, CBM being a V. cholerae NanH sialidase fragment, a S. pneumoniae nanA sialidase CBM fragment, or a fragment of SEQ ID NO: 17 encompasses any fragment length ranging from a single deleted residue at either termini to any dipeptide. Thus, the Family 40 CBM, modified CBMs, and CBM fragments encompass a vast array of amino acid sequences without a common core structure or sequence shared among species within the claimed genera needed to bind to a carbohydrate, sialic acid, or glycan acid. Therefore, the scope of the claimed inventions encompass a vast array of molecules and modules without a common core structure or sequence in order for the molecule and/or module to function as claimed.
The written description requirement may be met by provided a representative number of species of the genus and/or in light of the state of the art. With regard to the state of the art, Cummings et al. teaches that antibodies, lectins, microbial adhesions, viral agglutinins, and other proteins with CBMs, collectively termed glycan-recognizing probes (GRPs), are widely used in glycan analysis because their specificities enable them to discriminate among a diverse variety of glycan structures (See Cummings et al., “Chapter 48: Glycan-Recognizing Probes as Tools,” Essentials of Glycobiol., Varki et al., eds., 4th Ed., Cold Spring Harbor Laboratory Press, 22 pages (2022) at pg. 1, 1st paragraph). Furthermore, Liu et al. teaches that CBMs are a class of multi-module enzyme proteins with a function to bind to the carbohydrate substrate (See Liu et al., Polymers 14:17 pages (2022) at pg. 1, 1st paragraph). There are over 300,208 CBMs reported in the Carbohydrate Active enZYmes Database by April 2022 (See Liu, pg. 1, 1st paragraph). CBMs are small in size, flexible, stable, strong in identification, with strong plasticity, and they can be fused with enzymes or organisms to improve their functions (See Liu, pg. 2, 2nd paragraph). They are widely distributed in nature and are present in enzymes secreted by bacteria, fungi and archaea (See Liu, pg. 2, 4th paragraph). There are many ways to classify CBMs (See Liu, pg. 2, last paragraph). Based on structural, functional similarities and the different ligand binding sites, CBMs can be divided into three types, namely, surface-binding CBMs (type-A), glycan-chain-binding CBMs (type-B), and small-sugar-binding CBMs (type -C) (See Liu, pg. 2, last paragraph). The type-B CBM structure often contains grooves or cracks of different depths as depicted in Figure 1b (See Liu, pg. 3, last paragraph). Most type-B CBMs are produced by enzymes secreted by bacteria and interact with the free single-chain polysaccharide (See Liu, pg. 3, last paragraph). The typical configurations of type-C CBMs mainly interact with the end of the polysaccharide chain (See Liu, pg. 4, 1st paragraph). Due to steric hinderance, only monosaccharides, disaccharides, trisaccharides, or the terminal sugar group of polysaccharides bind to type-C CBMs (See Liu, pg. 4, 1st paragraph). Lectin was the first known type-C CBM (See Liu, pg. 4, 1st paragraph). As such, the prior art recognizes the vast array of glycan binding molecules and, more specifically, CBMs with varying structures and functions, and fails to identify a core structure or sequence shared among species within the claimed genera necessary for a molecule or module to bind a glycan or carbohydrate including modified CBMs and CBM fragments. Thus, the claims are directed to molecules and modules with a certain function but no correlated structure associated with that function. Without such structure, the specification does not convey possession of the breadth of the claimed genera.
Alternatively, the written description requirement may be met by provided a representative number of species of the genus. In this, the specification does not provide any examples glycan binding molecules other than CBMs, in particular CBM32, 40, 47, 67, or 70 (See instant, pg. 7, 3rd paragraph). The specification only exemplifies one CBM32 amino acid sequence as SEQ ID NO: 1, which is a fragment derived from the full length Clostridium perfringens protein represented by SEQ ID NO: 2 (See instant, pg. 9, 3rd paragraph; pg. 10, 2nd to last paragraph), and can bind, for example, galactose, N-acetylgalactosamine, N-acetylglucosamine, and/or lactose (See instant, pg. 9, last paragraph). Although the specification teaches that a CBM fragment of SEQ ID NO: 1 includes any 5 up to 138 contiguous amino acids from SEQ ID NO: 1 (See instant, pg. 9, 4th paragraph), there is no discussion of a core structure or sequence necessary for a CBM32 fragment of SEQ ID NO: 2 to bind to a carbohydrate. Plus, the specification discusses several microorganisms that contain CBMs such as Cellvibrio mixtus, Clostridium perfringens, and Streptococcus pneumoniae (See instant, pg. 9, 2nd paragraph).
Regarding CBM40, the specification exemplifies two CBM40 amino acid sequences as SEQ ID NO: 4, which is a fragment derived from the full length Vibrio cholerae NanH sialidase protein represented by SEQ ID NO: 3, and as SEQ ID NO: 6, which is a fragment derived from the full length Streptococcus pneumoniae NanA sialidase protein represented by SEQ ID NO: 5 (See instant, pg. 11, 5th to last paragraph; pg. 12, 1st to last paragraph). These CBMs are known to bind to sialic acid (See instant, pg. 11, 3rd paragraph). The specification also teaches that a molecule can comprise from about residue 1 to about residue 150 of SEQ ID NOs: 3-4 (See instant, pg. 13, 2nd paragraph) thereby encompassing a fragment containing a single residue. Additional discussion of CBM40 fragments of SEQ ID NOs: 3 or 5 include any 5 to about any 191 contiguous amino acids (See instant, pg. 13, 4th paragraph; pg. 14, 4th paragraph). Regarding CBM47, the specification exemplifies one amino acid sequence as SEQ ID NO: 7, which is a fragment derived from the full length Streptococcus pneumoniae protein represented by SEQ ID NO: 8, and can bind to L-fucose, fucosyllactose, H-trisaccharide and/or Lewis antigen (See instant, pg. 15, 2nd and 5th to last paragraph). Similar to CBM32 and 40 fragments, the specification teaches that a carbohydrate binding fragment of SEQ ID NO: 7 can comprise anywhere between about 5 to about 144 contiguous amino acids (See instant, pg. 15, 4th paragraph). Regarding CBM67, the specification exemplifies one CBM67 amino acid sequence as SEQ ID NO: 9, which is a fragment derived from the full length Streptomyces avermitilis protein represented by SEQ ID NO: 10 and can bind to L-rhamnose (See instant, pg. 17, 2nd and 5th to last paragraph; pg. 18, 1st to 2nd paragraph). Fragments of SEQ ID NO: 9 include anywhere between about 5 to about 164 contiguous amino acids (See instant, pg. 17, 4th paragraph). Regarding CBM70, the specification exemplifies one CBM70 amino acid sequence as SEQ ID NO: 11, which is a fragment derived from the full length Streptococcus pneumoniae protein represented by SEQ ID NO: 12 and can bind to hyaluronan (See instant, pg. 19, 1st and 3rd to last paragraph; pg. 20, 1st to 2nd paragraph). Fragments of SEQ ID NO: 11 include anywhere between about 5 to about 157 contiguous amino acids (See instant, pg. 19, 2nd paragraph). As such, the specification exemplifies six CBM amino acid sequences with no shared core structure or sequence, and only SEQ ID NOs: 3-6 exhibiting similar carbohydrate binding properties. Notably, there are no examples of any fragments of SEQ ID NOs: 1, 4, 6-7, 9 and 11, which are CBM fragments of a full length protein. Thus, the exemplary CBMs that bind to different carbohydrates do not constitute a representative number of species that an ordinary skilled artisan can extend to the scope of the claimed genera of glycan binding molecules, CBMs, and CBM fragments. Therefore, the specification is not sufficient for the skilled artisan to envisage which molecules or modules will preserve function.
Additionally, regarding modified CBMs, the instant specification teaches 7 general structures, HEX1 to HEX6 and HEX17, to be used to make sialic acid/glycan binding molecules (See instant, pg. 23, last paragraph to pg. 24, 1st paragraph). Each of the 7 HEX structures are a fusion of two CBMs and a modified/mutant trimerization domain (See instant, pg. 23, last paragraph to pg. 24, 1st paragraph). However, it is noted that all CBM components of all 7 HEX structures include two of the same mutations, i.e., V239A and V246G (See instant, pg. 24, 1st paragraph). These two mutations are the only modifications to both CBMs of HEX4 to HEX6 (See instant, pg. 24, 1st paragraph). HEX1 includes three additional mutations of L170T, I286A, and Y292E; HEX2 includes two additional mutations of I286A and Y292E; HEX3 includes one additional mutation of I286A; and HEX17 includes one additional mutation of A162P (See instant, pg. 24, 1st paragraph). As such, the modified CBM sequences are similar requiring the same two mutations with two HEX units containing 3 mutations, one HEX unit containing 4 mutations and one HEX unit containing 5 mutations. Although the 7 HEX structures do not specify an amino acid sequence and encompass any CBM (See instant, pg. 24, 2nd paragraph), the modified CBMs correspond to a specific CBM40 amino acid sequence, i.e., SEQ ID NO: 5. Since the differing CBM sequences do not share a core sequence, the identified mutations for the 7 HEX units cannot be extrapolated to extend to other unrelated CBM sequences. In fact, the identified mutations do not even correspond to the other CBM40 amino acid sequence, SEQ ID NO: 3. As such, the exemplary modified CBMs do not constitute a representative number of species that an ordinary skilled artisan can extend to the scope of the claimed genus. Therefore, the specification is not sufficient for the skilled artisan to envisage other substitutions/deletions/additions/insertions at the other residue sites which preserve function nor to envisage those substitutions other than those claimed with an expectation that function will be preserved.
Vas-Cath Inc. v. Mahurkar, 19USPQ2d 1111, clearly states “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the ‘written description’ inquiry, what is now claimed.” (See page 1117.) The specification does not “clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed.” (See Vas-Cath at page 1116). As discussed above, the skilled artisan cannot envision the detailed chemical structure of the encompassed genus of polypeptides which preserve the required function, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating it. The compound itself is required. See Fiers v. Revel, 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016.
One cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481 at 1483. In Fiddes, claims directed to mammalian FGF’s were found to be unpatentable due to lack of written description for that broad class. The specification provided only the bovine sequence. Therefore, claims 1-2, 5-6, 8, 16, and 19-21 do not meet the written description requirement.
Response to Arguments
Applicant's arguments filed 4/28/26 for claims 1, 8, 16, and 19-24 as failing the written description requirement have been fully considered but they are not persuasive for the following reasons.
In response to Applicants’ arguments, i.e., (1) CBMs being a Family 40 CMB or a Family 32 CBM define a structurally and functionally related class of CBMs that is well known in the art, (2) a “modified CBM” is described in sufficient detail that an ordinary skilled artisan would understand the inventors were in possession of the modified CBMs given that the specification teaches that a modified CBM can comprising a wild type CBM sequence that has been modified to include one or more mutations, (3) CBM fragments require the function of binding to a glycan, and thus, do not encompass any fragment as alleged by the Office Action but only ones that retain binding capability that can be readily tested using any binding assays known in the art, (4) the instant specification demonstrates an anti-viral effect against a coronavirus with specific examples thereby constituting a representative number of examples (See Applicant’s Response received on 4/28/26, pg. 9-11), they are found unpersuasive. MPEP §2163 states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus.
Additionally, the importance of structure/function correlations was highlighted by the court (Abbvie Deutschland v. Janssen Biotech and Centorcor Biologics, App. No. 2013-1338, -1346 (Fed. Cir. 2014)). The Abbvie case involved antibodies and written description. The court stated: “We have held that “a sufficient description of a genus . . . requires the disclosure of either a representative number of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can ‘visualize or recognize’ the members of the genus.” Id. at 1350 (quoting Eli Lilly, 119 F.3d at 1568– 69).”. The courts then further stated: “With the written description of a genus, however, merely drawing a fence around a perceived genus is not a description of the genus. One needs to show that one has truly invented the genus, i.e., that one has conceived and described sufficient representative species encompassing the breadth of the genus. Otherwise, one has only a research plan, leaving it to others to explore the unknown contours of the claimed genus.” (emphasis added) and then state: " Functionally defined genus claims can be inherently vulnerable to invalidity challenge for lack of written description support, especially in technology fields that are highly unpredictable, where it is difficult to establish a correlation between structure and function for the whole genus or to predict what would be covered by the functionally claimed genus. Ariad, 598 F.3d at 1351 (“[T]he level of detail required to satisfy the written description requirement varies depending on the nature and scope of the claims and on the complexity and predictability of the relevant technology.”); see also Centocor Ortho Biotech, Inc. v. Abbott Labs., 636 F.3d 1341, 1352 (Fed. Cir. 2011) (noting the technical challenges in developing fully human antibodies of a known human protein). It is true that functionally defined claims can meet the written description requirement if a reasonable structure-function correlation is established, whether by the inventor as described in the specification or known in the art at the time of the filing date. Enzo Biochem, Inc. v. Gen-Probe Inc., 323 F.3d 956, 964 (Fed. Cir. 2002). However, the record here does not indicate such an established correlation. Instead, Abbvie used a trial and error approach to modify individual amino acids in order to improve the IL-12 binding affinity. Moreover, the ’128 and ’485 patents do not describe any common structural features of the claimed antibodies. The asserted claims attempt to claim every fully human IL-12 antibody that would achieve a desired result, i.e., high binding affinity and neutralizing activity, and cover an antibody as different as Stelara, whereas the patents do not describe representative examples to support the full scope of the claims.”
In the instant case, as an initial matter, it is noted that the scope of the claimed genus of CBM40s are NOT limited to wild-type CBM40s. Pursuant to MPEP 2111, the pending claims must be "given their broadest reasonable interpretation consistent with the specification." The Federal Circuit’s en banc decision in Phillips v. AWH Corp., 415 F.3d 1303, 1316, 75 USPQ2d 1321, 1329 (Fed. Cir. 2005) expressly recognized that the USPTO employs the "broadest reasonable interpretation" standard:
The Patent and Trademark Office ("PTO") determines the scope of claims in patent applications not solely on the basis of the claim language, but upon giving claims their broadest reasonable construction "in light of the specification as it would be interpreted by one of ordinary skill in the art." In re Am. Acad. of Sci. Tech. Ctr., 367 F.3d 1359, 1364[, 70 USPQ2d 1827, 1830] (Fed. Cir. 2004). Indeed, the rules of the PTO require that application claims must "conform to the invention as set forth in the remainder of the specification and the terms and phrases used in the claims must find clear support or antecedent basis in the description so that the meaning of the terms in the claims may be ascertainable by reference to the description." 37 CFR 1.75(d)(1).
As discussed in the rejection supra, the scope of claims 1, 16 and 21 encompass modified CBM40 amino acid sequences, i.e., a CBM40 amino acid sequence comprising one or more mutations, and fragments of wild-type CBM40 amino acid sequences. Such interpretation is supported by the instant specification and claims (See instant, pg. 21, 4th and 6th paragraph to pg. 22, 3rd paragraph; claims 19-20). Thus, the broadest reasonable interpretation of the scope of claimed invention includes administering a wild-type CBM40 amino acid sequence, a modified CBM40 amino acid sequence containing any number of mutations (i.e., substitutions, deletions and/or additions/insertions), or a CBM40 amino acid sequence fragment of any length. Therefore, in light of the broadest reasonable interpretation and the standards to satisfy the written description requirement, the question to answer is whether an ordinary skilled artisan would recognize Applicants were in possession of either a representative number of species falling within the scope of the genus or structural features common to the members of the genus such that a structure/function correlation exists among the members of the claimed genus. The Examiner maintains that the answer is no given the substantial structural diversity of the claimed genus without an established structure/function correlation for either a representative number of species or a core structure/sequence necessary for members of the genus to function as claimed.
Regarding the state of the art, it is acknowledged that all amino acid sequences that constitute a CBM40 share a common lectin β-sandwich fold with two antiparallel β-sheets containing five and six strands. CBM40s specifically recognize glycans containing terminal α-2,3- or α 2,6-linked sialic acids (See Xu et al., Scientific Rep. 6:1-12 (2016) at pg. 2, 1st paragraph; Owen et al., Nat. Commun. 8:1-15 (2017) at pg. 2, col. 2, 4th paragraph). Owens et al. teaches that CBM40s associated with sialidases fall into two subfamilies, the canonical subfamily exemplified by CpCBM40_NanJ, and the Vibrio subfamily exemplified by VcCBM40_NanH (See Owens, pg. 3, col. 2, 2nd paragraph). Owen et al. also teaches that there is considerable sequence divergence between the Vibrio and canonical CBM40 types rendering satisfactory sequence alignments difficult to produce with standard tools (See Owens, pg. 3, col. 2, 2nd paragraph). However, Owens produced an alignment of both types manually, notwithstanding the Vibrio insertion (40 residues) near the N-terminus where the pairwise identities between the canonical representatives range from 21 to 67%, while the maximum canonical vs Vibrio identity is 17% (See Owens, pg. 3, col. 2, 2nd paragraph; Figure 3; Supplemental Figure 4). Owens et al. identifies a tree of 51 non-redundant sequences constructed using a simple distance-based model and neighbor-joining (See Owens, pg. 4, col. 1, 2nd paragraph; Figure 3; Supplemental Figure 4). As such, Family CBM40 includes 18 genera or pseudogenera of the canonical subfamily and 5 genera of the Vibrio subfamily where the sequence identity shared among the members of the CBM40 family is quite low (i.e., 17%) thereby rendering the Family CBM40 members as homologues of each other sharing secondary structural elements (i.e., β-sandwich fold with two antiparallel β-sheets containing five and six strands) and functional elements (i.e., binding to glycans containing terminal α-2,3- or α 2,6-linked sialic acids). However, Owens et al. identifies conserved residues within the canonical subfamily that may be involved in binding affinity and specificity; namely, an arginine dyad that interacts with the sialic acid carboxylic acid group, a glutamic acid that hydrogen bonds to the C4 hydroxyl, and a hydrophobic surface that accommodates the N-acetyl moiety and the hydrophobic face of the glycerol group (See Owens, pg. 3, col. 2, 2nd paragraph to pg. 4, col. 1, 1st paragraph). Thus, although it is acknowledged that an ordinary skilled artisan would be well-aware of the structure/function correlation among wild-type full length CBM40 family amino acid sequences to bind to a glycan molecule in light of the prior art, the scope of the claimed invention is not limited to only wild-type CBM40 family members, but rather encompasses modified CBM40 variants and CBM40 fragments.
With respect CBM32/40 fragments in the instant specification, it is acknowledged that the specification teaches one CBM32 amino acid sequence as SEQ ID NO: 1, which is a fragment derived from the full length Clostridium perfringens protein represented by SEQ ID NO: 2 (See instant, pg. 9, 3rd paragraph; pg. 10, 2nd to last paragraph), and can bind, for example, galactose, N-acetylgalactosamine, N-acetylglucosamine, and/or lactose (See instant, pg. 9, last paragraph); and two CBM40 amino acid sequences as SEQ ID NO: 4, which is a fragment derived from the full length Vibrio cholerae NanH sialidase protein represented by SEQ ID NO: 3, and as SEQ ID NO: 6, which is a fragment derived from the full length Streptococcus pneumoniae NanA sialidase protein represented by SEQ ID NO: 5 (See instant, pg. 11, 5th to last paragraph; pg. 12, 1st to last paragraph). The specification also generally refers to fragments of each of these fragments, i.e., SEQ ID NO: 1, 4, and 6; for example, a CBM fragment of SEQ ID NO: 1 includes any 5 up to 138 contiguous amino acids from SEQ ID NO: 1 (See instant, pg. 9, 4th paragraph) or a molecule can comprise from about residue 1 to about residue 150 of SEQ ID NOs: 3-4 (See instant, pg. 13, 2nd paragraph). However, as discussed in the rejection supra, the specification fails to demonstrate any fragments of SEQ ID NOs: 1-6, that exhibit the claimed function of glycan binding. Thus, the Examiner maintains that the facts of the instant application are analogous to that in Abbvie with respect to CBM32/40 fragments by merely drawing a fence around a perceived genus of CBM32/40 fragments without exemplifying a representative number of CBM32/40 fragments that bind glycans, and instead leave it to others to explore the contours of which CBM32/40 fragments bind to glycans. General discussion of CBM32/40 fragments is insufficient to demonstrate possession of the claimed genus of CBM32/40 fragments given the sequence diversity amino wild-type CBM32/40 family members and given the vast scope of CBM32/40 fragments claimed.
With respect modified CBM32/40s in the instant specification, it is acknowledged that the specification teaches 7 general structures, HEX1 to HEX6 and HEX17, to be used to make sialic acid/glycan binding molecules (See instant, pg. 23, last paragraph to pg. 24, 1st paragraph). However, each of these 7 HEX structures are a specific species of modified CBM that is based on a single wild-type CBM40 amino acid sequence (i.e., SEQ ID NO: 5); namely, a fusion of two CBMs and a modified/mutant trimerization domain where all CBM components of all 7 HEX structures include two of the same mutations, i.e., V239A and V246G (See instant, pg. 23, last paragraph to pg. 24, 1st paragraph). HEX1 includes three additional mutations of L170T, I286A, and Y292E; HEX2 includes two additional mutations of I286A and Y292E; HEX3 includes one additional mutation of I286A; and HEX17 includes one additional mutation of A162P (See instant, pg. 24, 1st paragraph). As discussed in the rejection supra, the specification fails to demonstrate any modified CBM32/40s that exhibit the claimed function of glycan binding. Thus, the Examiner maintains that the facts of the instant application are analogous to that in Abbvie with respect to modified CBM32/40s by merely drawing a fence around a perceived genus of modified CBM32/40s without exemplifying a representative number of modified CBM32/40s that bind glycans, and instead leave it to others to explore the contours of which modified CBM32/40s bind to glycans. General discussion of modified CBM32/40s is insufficient to demonstrate possession of the claimed genus of modified CBM32/40s given the sequence diversity amino wild-type CBM32/40 family members and given the vast scope of modified CBM32/40s claimed.
Furthermore, pursuant to MPEP 2163.05(I)(B), [t]he written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species. A "representative number of species" means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus. (emphasis added). See AbbVie Deutschland GmbH & Co., KG v. Janssen Biotech, Inc., 759 F.3d 1285, 1300, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014) (Claims directed to a functionally defined genus of antibodies were not supported by a disclosure that "only describe[d] one type of structurally similar antibodies" that "are not representative of the full variety or scope of the genus."). The disclosure of only one species encompassed within a genus adequately describes a claim directed to that genus only if the disclosure "indicates that the patentee has invented species sufficient to constitute the gen[us]." See Enzo Biochem, 323 F.3d at 966, 63 USPQ2d at 1615. "A patentee will not be deemed to have invented species sufficient to constitute the genus by virtue of having disclosed a single species when … the evidence indicates ordinary artisans could not predict the operability in the invention of any species other than the one disclosed." In re Curtis, 354 F.3d 1347, 1358, 69 USPQ2d 1274, 1282 (Fed. Cir. 2004) (Claims directed to PTFE dental floss with a friction-enhancing coating were not supported by a disclosure of a microcrystalline wax coating where there was no evidence in the disclosure or anywhere else in the record showing applicant conveyed that any other coating was suitable for a PTFE dental floss.)
In the instant case, although there are situations where a single species adequately supports a genus (See MPEP 2163.05(I)(B), e.g., In re Rasmussen, 650 F.2d 1212, 1214, 211 USPQ 323, 326-27 (CCPA 1981) (disclosure of a single method of adheringly applying one layer to another was sufficient to support a generic claim to "adheringly applying" because one skilled in the art reading the specification would understand that it is unimportant how the layers are adhered, so long as they are adhered), given the breadth of the claimed genus, the limited specific species described in the specification cannot be extrapolated to extend to the full scope of the claimed genus of CBM32/40 fragments and modified CBM32/40s. Although the specification describes for 3 specific species of CBM32/40 fragments (i.e., SEQ ID NOs: 1, 4, and 6), three modified CBM40s (i.e., SEQ ID NOs: 16-17 and VcCBM40TD), and one modified CBM32 (i.e., Cp2CBM32TD), the description of a limited number of species within a vastly broad genus does not constitute a representative number of species. It is noted that HEX1 to HEX6 do not appear to correspond to specific amino acid sequences, although the specification indicates that HEX6 and HEX17 are identical except for an added A162P mutation in HEX17 (See instant, pg. 24, last paragraph). However, as noted supra, the HEX units include two of the same mutations, i.e., V239A and V246G (See instant, pg. 23, last paragraph to pg. 24, 1st paragraph). As such, presuming that the HEX units all share the amino acid sequence of SEQ ID NO: 17, the sequence variability is limited to specific mutations. Plus, the specification demonstrates that Hex17 (i.e., denoted as CBM2 and is a trimeric (hexavalent) form based on S. pneumoniae CBM40) and a CBM3 as a specific CBM32-based (i.e., Cp2CBM32TD and is a trimeric (hexavalent) form based on C. perfringens CBM32) exhibited anti-viral activity (See instant, pg. 39, Points 3.2 and 3.3; Figures 4-5). However, these three species contain specific amino acid and secondary structural framework; namely, trimeric (hexavalent) forms with each containing an oligomerization domain. As such, the exemplary modified CBMs do not constitute a representative number of species that an ordinary skilled artisan can extend to the scope of the claimed genus that includes non-trimeric forms with or without an oligomerization domain and one or more mutations (i.e., any number of substitutions, deletions, insertions). Therefore, even though the specification supports possession of specific species of modified CBM32 (i.e., one species) and of modified CBM40 (i.e., three species), Applicants have not demonstrated a representative number of species within the claimed genus of CBM32/40 fragments and modified CBM32/40s to exhibit the function of glycan binding to constitute possession of the claimed genus.
In response to Applicant’s argument that CBM fragments are limited to those that retain binding capability, which can be readily tested, it is noted that this is the crux of the problem. As discussed in the rejection supra, there is no evidence in the prior art or in the instant specification to demonstrate the core structure/sequence necessary for a CBM32/40 fragment to exhibit the function of glycan binding. Pursuant to MPEP 2164, the enablement requirement of 35 U.S.C. 112(a) or pre-AIA 35 U.S.C. 112, first paragraph, is separate and distinct from the written description requirement. Vas-Cath, Inc. v. Mahurkar, 935 F.2d 1555, 1563, 19 USPQ2d 1111, 1116-17 (Fed. Cir. 1991) ("the purpose of the ‘written description’ requirement is broader than to merely explain how to ‘make and use’"). Here, even though conducting binding assay experiments may be known in the art does not per se establish a structure/function correlation. Rather, as discussed supra, written description requires more than just how to make the CBM32/40 fragments. It requires either a representative number of species within the claimed genus exhibiting the claimed function or establishment of a core structure/sequence necessary for a claimed genus to function as claimed. Therefore, recitation of a functional property and ability to perform experiments to confirm the functional property does not satisfy either of the requirements for written description.
Accordingly, the rejection of claims 1, 8, 16, and 19-24 is maintained as Applicants’ arguments are found unpersuasive.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1, 8, 16, and 19-24 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for the treatment or prophylactic treatment of a SARS-CoV-2 infection by administering a therapeutically effective amount of SEQ ID NO: 17, does not reasonably provide enablement for the treatment or prophylactic treatment of a SARS-CoV-2 infection by administering any glycan acid binding fragments of SEQ ID NO: 17. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to use the invention commensurate in scope with these claims. NOTE: the rejection is limited to examination of elected SEQ ID NO: 17 and fragments thereof.
As stated in MPEP §2164.01(a), “there are many factors to consider when determining whether there is sufficient evidence to support a determination that a disclosure does not satisfy the enablement requirement and whether any experimentation is ‘undue’.” These factors include, but are not limited to:
1. The breadth of the claims;
2. The nature of the invention;
3. The state of the prior art;
4. The level of skill in the art;
5. The level of predictability in the art;
6. The amount of direction provided by the inventor;
7. The presence or absence of working examples;
8. The quantity of experimentation necessary needed to make or use the invention based on the disclosure.
See In re Wands USPQ 2d 1400 (CAFC 1988).
The eight In re Wands factors are applied to Claims 1, 8, 16, and 19-24 as follows:
The Breadth of the Claims and The Nature of the Invention
Although addressing that the subject is suffering from a SARS CoV-2 infection or at risk of suffering from a SARS CoV-2 infection in claims 1, 16, and 21 by administering SEQ ID NO: 17 or a glycan acid binding fragment thereof as a glycan binding molecule comprising a Family 40 CBM with 3 specific mutations, a CBM40, and as a glycan acid binding molecule with the structure of Sp2CBM40TD, respectively, Applicants do not provide any evidence in the specification that any fragment of SEQ ID NO: 17 can treat or prophylactically treat a SARS CoV-2 infection. As discussed in the “Sequence Interpretation” section supra, a glycan acid binding fragment of SEQ ID NO: 17 encompasses any fragment ranging from a fragment having a deleted residue at the N- or C-terminus to any dipeptide of SEQ ID NO: 17. As such, the scope of the glycan acid binding fragments of SEQ ID NO: 17 encompasses a vast array of peptide fragments. Accordingly, claims 1, 8, 16, and 19-24 are unduly broad with respect to treating or prophylactically treating a SARS CoV-2 infection by administering any glycan acid binding fragment of SEQ ID NO: 17.
The State of the Prior Art
It is noted that there is currently no prior art that teaches administering any glycan acid binding fragment of SEQ ID NO: 17 in order to treat or prophylactically treat a SARS CoV-2 infection in a subject.
The Level of Skill in the Art
Practitioners in this art (medical clinicians, pharmacists, doctors and/or pharmaceutical chemists) would presumably be highly skilled in the art for treatment and/or prevention of a SARS CoV-2 infection in a subject.
The Level of Predictability in the Art
The instant claimed invention is highly unpredictable. If one skilled in the art cannot readily anticipate the effect of a change within the subject matter to which that claimed invention pertains (i.e., administering any glycan acid binding fragment of SEQ ID NO: 17 to a subject suffering from a SARS CoV-2 infection), then there is a lack of predictability in the art. Moreover, it is noted that the pharmaceutical art is unpredictable, requiring each embodiment to be individually assessed for physiological activity. The court has indicated that the more unpredictable an area is, the more specific enablement is necessary in order to satisfy the statute. (See In re Fisher, 427 F.2d 833, 166 USPQ 18 (CCPA 1970)). This is because it is not obvious from the disclosure of one species, what other species will work.
In the instant case, Applicants do not demonstrate that any glycan acid binding fragment of SEQ ID NO: 17 administered to a subject suffering from a SARS CoV-2 infection or to a subject who could suffer from a SARS CoV-2 infection is effective to treat or prophylactically treat a SARS CoV-2 infection. Rather, Applicants only demonstrate that 3 specific modified trimeric, hexavalent CBMs (i.e., Vc2BM40TD, which is a trimer of two monomers of instant SEQ ID NO: 3 derived from V. cholerae and a trimerization domain (hereinafter CBM1); Sp2CBM40TD, which is a trimer of two monomers of modified instant SEQ ID NO: 6 with 3 mutations of V239A, V246G and A162P derived from S. pneumoniae and a trimerization domain of instant SEQ ID NO: 14 with 2 mutations of S342D and R403K (hereinafter CBM2); and Cp2CBM32TD, which is a trimer of two monomers of instant SEQ ID NO: 1 derived from C. perfringens and a trimerization domain (hereinafter CBM3)) reduced SARS CoV-2 plaques in vitro, whether administered prior to or after viral exposure at two specific concentrations of 1 mg/ml or 3 mg/ml (See instant, Example 1 at pg. 36-40; Figures 2-6). However, it is noted that the specific amino acid sequences of CBMs1 and 3 are not provided in the specification, in particular, if these two CBMs are modified similar to the CBM2 amino acid sequence and what the amino acid sequence of the trimerization domain is. As such, without clarification, the instant specification only demonstrates a single species, i.e., CBM2 (also referred to in the specification as HEX17 or Neumifil), as effectively treating or prophylactically treating a SARS CoV-2 infection by reducing viral plaque levels in Example 1. Furthermore, the specification describes an in vivo hamster study evaluating the effectiveness of CBM2 on SAR CoV-2 infection symptoms (See instant, Example 3, pg. 41-47; Tables 1-4; Figure 7). The specification concludes that the CBM2 treated hamsters exhibited a generally lower average number of symptoms relative to the control group including fewer instances of labored breathing (Lb) (See instant, pg. 47 Table 4). As such, Example 3 in the specification demonstrates that the CBM2 (i.e., instant SEQ ID NO: 17) is effective in treating a SARS CoV-2 infection. Example 4 demonstrates that CBM2 interacts with the SARS CoV-2 Spike S1 protein from three different strains, i.e., the Wuhan strain, a South African strain, and a UK-Kent strain (See instant, Example 4, pg. 48-49; Figure 8).
Applicants appear to rely on the assumption that by providing evidence that instant SEQ ID NO: 17 treats or prophylactically treats a SARS CoV-2 infection in vitro and in vivo would exhibit similar intended results for the treatment of a SARS CoV-2 infection by any glycan acid binding fragment of instant SEQ ID NO: 17. However, such an assumption cannot be made because there is no indication that any glycan acid binding fragment of SEQ ID NO: 17 would treat or prophylactically treat a SARS CoV-2 infection. Additionally, since the Specification fails to demonstrate any data or evidence that any glycan acid binding fragment of instant SEQ ID NO: 17 treats or prophylactically treats a SARS CoV-2 infection, there would be no way of determining without undue experimentation whether a representative number of glycan acid binding fragments of SEQ ID NO: 17 exhibit such desired results. Without more experimentation demonstrating the efficacy of a representative number of glycan acid binding fragments of SEQ ID NO: 17 that an ordinary skilled artisan can extrapolate to extend to the claimed genera for the treatment and/or prophylactic treatment of a SARS CoV-2 infection, the level of unpredictability remains high. Therefore, it is unpredictable that any glycan acid binding fragment of instant SEQ ID NO: 17 will treat a SARS CoV-2 infection in a subject.
The Amount of Direction Provided by the Inventor.
The Presence or Absence of Working Examples, and
The Quantity of Experimentation Necessary
The specification does not enable any person skilled in the art to which it pertains (i.e. administering any glycan acid binding fragment of SEQ ID NO: 17 to a subject suffering from a SARS CoV-2 infection) to make and/or use the invention commensurate in scope with the claims. There is a lack of adequate guidance from the specification or prior art with regard to the actual treatment or prophylactic treatment of a SARS CoV-2 infection by administering to a subject any glycan acid binding fragment of SEQ ID NO: 17. Applicants fail to provide the guidance and information required to ascertain where the claimed glycan acid binding fragment of SEQ ID NO: 17 treats or prophylactically treats a SARS CoV-2 infection without resorting to undue experimentation. Applicant's limited disclosure is noted but is not sufficient to justify claiming all glycan acid binding fragments of SEQ ID NO: 17 for treating or prophylactically treating a SARS CoV-2 infection.
Absent a reasonable a priori expectation of success for using a representative number of glycan acid binding fragments of SEQ ID NO: 17 to treat or prophylactically treat a SARS CoV-2 infection, one skilled in the art would have to extensively test viral titer levels in vitro and in vivo. Since each prospective embodiment, and indeed future embodiments as the art progresses, would have to be empirically tested, and those which initially failed tested further, an undue amount of experimentation would be required to practice the invention as it is claimed in its current scope, because the specification provides inadequate guidance to do otherwise.
The amount of direction or guidance presented in the specification is limited to specific species for the treatment or prophylactic treatment of a SARS CoV-2 infection and do not provide any direction or guidance for administering any fragment of SEQ ID NO:17 to treat or prophylactically treat a SARS CoV-2 infection. The Specification discloses two working examples, in particular Examples 1 and 3, related to treating a SARS CoV-2 infection. Example 1 demonstrates that 3 specific modified trimeric, hexavalent CBMs (i.e., Vc2BM40TD, which is a trimer of two monomers of instant SEQ ID NO: 3 derived from V. cholerae and a trimerization domain (hereinafter CBM1); Sp2CBM40TD, which is a trimer of two monomers of modified instant SEQ ID NO: 6 with 3 mutations of V239A, V246G and A162P derived from S. pneumoniae and a trimerization domain of instant SEQ ID NO: 14 with 2 mutations of S342D and R403K (hereinafter CBM2); and Cp2CBM32TD, which is a trimer of two monomers of instant SEQ ID NO: 1 derived from C. perfringens and a trimerization domain (hereinafter CBM3)) reduced SARS CoV-2 plaques in vitro, whether administered prior to or after viral exposure at two specific concentrations of 1 mg/ml or 3 mg/ml (See instant, Example 1 at pg. 36-40; Figures 2-6). However, it is noted that the specific amino acid sequences of CBMs 1 and 3 are not provided in the specification, in particular, if these two CBMs are modified similar to the CBM2 amino acid sequence and what the amino acid sequence of the trimerization domain is. As such, without clarification, the instant specification only demonstrates a single species, i.e., CBM2 (also referred to in the specification as HEX17 or Neumifil), as effectively treating or prophylactically treating a SARS CoV-2 infection by reducing viral plaque numbers in Example 1. Example 3 demonstrates that CBM2 when administered to hamsters resulted in the treated hamsters exhibiting a generally lower average number of symptoms relative to the control group including fewer instances of labored breathing (Lb) (See instant, Example 3, pg. 41-47; Tables 1-4; Figure 7). As such, Example 3 in the specification demonstrates that the CBM2 (i.e., instant SEQ ID NO: 17) is effective in treating a SARS CoV-2 infection. However, as noted in “Breadth of the Claims and Nature of the Invention" Section, the scope of the claimed glycan acid binding fragments of SEQ ID NO: 17, encompass a vast array of fragments without a core structure or sequence shared among the species allowing an ordinary skilled artisan to extrapolate the efficacy of a representative number of species to extend to the whole genera. As such, the efficacy of a single CBM40, i.e., CBM2, is insufficient to constitute a representative number of species that an ordinary skilled artisan can extrapolate the efficacy of to extend to other species within the claimed genera. It is further noted that Applicants provide no data, examples, figures, etc. demonstrating that any glycan acid binding fragment of SEQ ID NO: 17 is capable of treating or prophylactically treating a SARS CoV-2 infection. In the absence of such information, a person of ordinary skill in the art would reasonably require an undue quantity of experimentation.
Conclusion of 35 U.S.C. 112(a) (Enablement) Analysis
MPEP §2164.01(a), 4th paragraph, provides that, “A conclusion of lack of enablement means that, based on the evidence regarding each of the above factors, the specification, at the time the application was filed, would not have taught one skilled in the art how to make and/or use the full scope of the claimed invention without undue experimentation. In re Wright, 999 F.2d 1157, 1562; 27 USPQ2d 1510, 1513 (Fed. Cir. 1993).
Genentech Inc. v. Novo Nordisk A/S, 42 USPQ2d 1001, 1005 (CA FC), states that, “[p]atent protection is granted in return for an enabling disclosure of an invention, not for vague intimations of general ideas that may or may not be workable,” citing Brenner v. Manson, 383 U.S. 519, 536 (1966) (stating, in the context of the utility requirement, that “a patent is not a hunting license. It is not a reward for search, but compensation for its successful conclusion”). The Genentech decision continued, “tossing out the mere germ of an idea does not constitute enabling disclosure. While every aspect of a generic claim certainly need not have been carried out by an inventor, or exemplified in the specification, reasonable detail must be provided in order to enable members of the public to understand and carry out the invention.” Id. at p. 1005.
After applying the Wands factors and analysis to Claims 1, 8, 16, and 19-24, in view of the applicant’s entire disclosure, and considering the In re Wright, In re Fisher and Genentech decisions discussed above, it is concluded that the practice of the invention as claimed in Claims 1, 8, 16, and 19-24 would not be enabled by the written disclosure excluding that of treating or prophylactically treating a SARS CoV-2 infection in a subject by administering instant SEQ ID NO: 17 as a glycan binding molecule and/or a glycan acid binding molecule. Therefore, Claims 1, 8, 16, and 19-24, are rejected under 35 U.S.C. §112(a) for failing to disclose sufficient information to enable a person of skill in the art to administer any glycan acid binding fragment of SEQ ID NO: 17 to a subject in order to treat or prophylactically treat a SARS CoV-2 infection.
Response to Arguments
Applicant's arguments filed 4/28/26 for claims 1, 8, 16, and 19-24 as failing the scope of enablement requirement have been fully considered but they are not persuasive for the following reasons.
In response to Applicants’ arguments, i.e., (1) the present application provides an enabling disclosure for the treatment of a SARS-CoV-2 infection by administering fragments of SEQ ID NO: 17 because the fragments must meet defined structural and functional limitations including retaining the ability to bind sialic acid, which can be readily tested by an ordinary skilled artisan without undue experimentation, and (2) the working examples demonstrate that a glycan binding molecule comprising CBM40 or CBM32 has an anti-viral effect against a coronavirus, and thus, enable the full scope of the claims without undue experimentation (See Applicant’s Response received on 4/28/26, pg. 12), they are found unpersuasive. Pursuant to MPEP 2164.01(a), “[t]he determination that “undue experimentation” would have been needed to make and use the claimed invention is not a single, simple factual determination. Rather, it is a conclusion reached by weighing all the above noted factual considerations. There are many factors to consider when determining whether there is sufficient evidence to support a determination that a disclosure does not satisfy the enablement requirement and whether any experimentation is ‘undue’.” In re Wands, 858 F.2d at 737, 8 USPQ2d at 1400, 1404.
MPEP 2164.02 states “[t]o make a valid rejection, one must evaluate all the facts and evidence and state why one would not expect to be able to extrapolate that one example across the entire scope of the claims. For a claimed genus, representative examples together with a statement applicable to the genus as a whole will ordinarily be sufficient if one skilled in the art (in view of level of skill, state of the art and the information in the specification) would expect the claimed genus could be used in that manner without undue experimentation. Proof of enablement will be required for other members of the claimed genus only where adequate reasons are advanced by the examiner to establish that a person skilled in the art could not use the genus as a whole without undue experimentation.” (emphasis added).
In the instant case, as discussed in the rejection supra, the patent office relied on each of the eight Wands factors to support the position that the scope of treatment in a subject suffering from a SARS-CoV-2 infection or of prophylactic treatment in a subject who may suffer from a SARS-CoV-2 infection by administering a fragment of SEQ ID NO: 17 is not fully enabled. First, the breadth and nature of the claimed invention indicate the breadth of the claimed scope of fragments of SEQ ID NO: 17. As discussed supra in the “Sequence Interpretation” section , SEQ ID NO: 17 is a fusion protein with a total of 489 amino acids having a general structure of: CBMX1----CBMX2----TD where CBMX1 and CBMX2 are two identical monomers of instant SEQ ID NO: 6 (note: CBM40 derived from Streptococcus pneumoniae NanA sialidase) with three substitutions; namely, V239A, V246G, and A162P, TD is a trimerization domain derived from Pseudomonas aeruginosa sialidase (See GenBank Accession No. WP_411194140.1, 2 pages (2025) at residues 175/176 to 281) with two substitutions; namely, S342D and R403K, the first “----” is a peptide linker of GGGSG (i.e., instant SEQ ID NO: 21), and the second “----" is a peptide linker of GGSLG or GGSL. Contrary to Applicant’s argument, “fragments” of SEQ ID NO: 17 are NOT defined by any structural limitations. Applicants are invited to point to such structural limitation(s) and/or definitions in the specification. Although the fragments must exhibit the function of glycan acid binding, the recitation of a functional property without any indication of a core structure/sequence necessary for a SEQ ID NO: 17 fragment is insufficient to define which fragments will treat or prophylactically treat a SARS-CoV-2 infection in a subject. Without indication of core structure/sequence necessary for a SEQ ID NO: 17 fragment to treat or prophylactically treat a SARS-CoV-2 infection, the broadest reasonable interpretation of the claimed SEQ ID NO: 17 fragments encompass fragments of any dipeptide of the 489 total amino acids of SEQ ID NO: 17 up to a fragment with one deleted residue at the N- or C-terminus. Second, the state of the art supports the unpredictability with respect to the scope of treatment given that there is no prior art demonstrating efficacy of a SEQ ID NO: 17 fragment against a SARS-CoV-2 infection. Third, the patent office points out that the instant specification only demonstrates SEQ ID NO: 17 itself as effectively treating or prophylactically treating a SARS-CoV-2 infection. The instant specification fails to demonstrate the efficacy of any SEQ ID NO: 17 fragment. Thus, the Examiner maintains that the scope of the claimed invention requires undue experimentation with respect to administering SEQ ID NO: 17 fragment in order to treat or prophylactically treat a SARS-CoV-2 infection in a subject when weighing the evidence as established for each factor including consideration of the broadest reasonable interpretation of what constitutes a SEQ ID NO: 17 fragment, and lack of representative examples demonstrating efficacy as instantly claimed.
Additionally, the Office’s position is supported by the holding in Enzo Biochem, Inc. v. Calgene, Inc., 188 F.3d 1362, 52 USPQ2d 1129 (Fed. Cir. 1999). As discussed in MPEP 2164.06(b)(I)(A), in Enzo Biochem, Inc. v. Calgene, Inc., the court held that two patents with claims directed to genetic antisense technology (which aims to control gene expression in a particular organism), were invalid because the breadth of enablement was not commensurate in scope with the claims. Both specifications disclosed applying antisense technology in regulating three E. coli genes. Despite the limited disclosures, the specifications asserted that the "[t]he practices of this invention are generally applicable with respect to any organism containing genetic material which is capable of being expressed … such as bacteria, yeast, and other cellular organisms." Thus, the court construed the claims to encompass the application of antisense methodology in a broad range of organisms. Ultimately, the court relied on the fact that (1) the amount of direction presented and the number of working examples provided in the specification were very narrow compared to the wide breadth of the claims at issue, (2) antisense gene technology was highly unpredictable, and (3) the amount of experimentation required to adapt the practice of creating antisense DNA from E. coli to other types of cells was quite high, especially in light of the record, which included notable examples of the inventor’s own failures to control the expression of other genes in E. coli and other types of cells. Thus, the teachings set forth in the specification provided no more than a "plan" or "invitation" for those of skill in the art to experiment using the technology in other types of cells.
In the instant case, like in the Calgene case, the amount of direction and the number of working examples provided in the specification were very narrow compared to the wide breadth of the claims at issue, treating or prophylactically treating a SARS-CoV-2 infection is a highly unpredictable technology, and the amount of experimentation required to adapt the practice of treating or prophylactically treating a SARS-CoV-2 infection by administering a fragment of SEQ ID NO: 17 is quite high given the vast array of SEQ ID NO: 17 fragments. Therefore, like in the Calgene case, the teachings set forth in the specification and lack of teachings in the prior art provide no more than a "plan" or "invitation" for those of skill in the art to experiment using the technology for polypeptide fragments that do not have a common core structure, sequence and/or amino acid residues with SEQ ID NO: 17. Applicants are invited to provide additional data demonstrating a representative number of SEQ ID NO: 17 fragments that function as claimed. Without such additional data, the instant disclosure and the state of the art fail enable one or ordinary skill in the art to perform the claimed method without undue experimentation.
Accordingly, the rejection of claims 1, 8, 16, and 19-24 as failing the scope of enablement requirement is maintained as Applicants’ arguments are found unpersuasive.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied for establishing a background for determining obviousness under pre-AIA 35 U.S.C. 103(a) are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims under 35 U.S.C. 103(a), the examiner presumes that the subject matter of the various claims was commonly owned at the time any inventions covered therein were made absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and invention dates of each claim that was not commonly owned at the time a later invention was made in order for the examiner to consider the applicability of 35 U.S.C. 103(c) and potential 35 U.S.C. 102(e), (f) or (g) prior art under 35 U.S.C. 103(a).
103 - KSR Examples of 'Rationales' Supporting a Conclusion of Obviousness(Consistent with the "Functional Approach" of Graham)
Further regarding 35 USC 103(a) rejections, the Supreme Court in KSR International Co. v. Teleflex Inc., 550 U.S. 398, 127 S. Ct. 1727, 82 USPQ2d 1385, 1395-97 (2007) (KSR) identified a number of rationales to support a conclusion of obviousness which are consistent with the proper "functional approach" to the determination of obviousness as laid down in Graham. The key to supporting any rejection under 35 U.S.C. 103 is the clear articulation of the reason(s) why the claimed invention would have been obvious. The Supreme Court in KSR noted that the analysis supporting a rejection under 35 U.S.C. 103 should be made explicit.
Exemplary rationales that may support a conclusion of obviousness include:
(A) Combining prior art elements according to known methods to yield predictable results;
(B) Simple substitution of one known element for another to obtain predictable results;
(C) Use of known technique to improve similar devices (methods, or products) in the same way;
(D) Applying a known technique to a known device (method, or product) ready for improvement to yield predictable results;
(E) "Obvious to try" - choosing from a finite number of identified, predictable solutions, with a reasonable expectation of success;
(F) Known work in one field of endeavor may prompt variations of it for use in either the same field or a different one based on design incentives or other market forces if the variations are predictable to one of ordinary skill in the art;
(G) Some teaching, suggestion, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art reference teachings to arrive at the claimed invention.
Note that the list of rationales provided is not intended to be an all-inclusive list. Other rationales to support a conclusion of obviousness may be relied upon by Office personnel.
Also, a reference is good not only for what it teaches by direct anticipation but also for what one of ordinary skill in the art might reasonably infer from the teachings. (In re Opprecht 12 USPQ 2d 1235, 1236 (Fed Cir. 1989); In re Bode 193 USPQ 12 (CCPA) 1976).
Claims 1, 8, 16, and 21-24 are rejected under 35 U.S.C. 103 as being unpatentable over Taylor et al. US 2017/0007692 A1 published on August 30, 2022 (cited in the IDS received on 8/30/22), in view of Matrosovich, et al., Top. Curr. Chem. 367:1-28 (2015), and Coronaviridae Study Group of the Intl. Committee on Taxonomy of Viruses, “The species Severe acute respiratory syndrome-related coronavirus: classifying 2019-nCoV and naming it SARS-CoV-2,” Nat. Microbiol. 5:536-544 (March 2, 2020) (hereinafter referred to as “CSG article”).
For claims 1, 8, 16, and 21, Taylor et al. claims a method of modulating or priming an immune response in a subject by administering an immunomodulatory amount or quantity of a sialic acid binding molecule to a subject in need thereof (See Taylor, claim 1). The immune response is a protective immune response which protects against an infection caused or contributed to by a pathogen (See Taylor, claim 4) where the pathogen can be a viral pathogen (See Taylor, claim 5). The immune response is protective against a bacterial, fungal, and/or viral infection (See Taylor, claim 22). The subject administered the sialic acid molecule is one that has or is at risk of infection by a pathogen (See Taylor, claim 9) thereby constituting treatment or prophylactic treatment (i.e., at risk of infection). The subject can be symptomatic of an infection and the sialic acid binding molecule is administered to modulate the immune system to facilitate resolution and/or clearance of the infection (See Taylor, claim 14) thereby constituting where administration of the sialic acid binding molecule treats the infection that the subject is suffering from. Thus, the teachings of Taylor et al. satisfy the claim limitation of a method of treating or prophylactically treating an infection as recited in instant claims 1, 16, and 21-24.
Taylor et al. claims that the sialic acid binding molecule comprises a single sialic acid binding molecule or two or more sialic acid binding molecules (See Taylor, claim 17). Taylor et al. also claims where the sialic acid molecule comprises one or more CBMs (See Taylor, claim 18) where the CBM comprises the sialic acid binding domain from S. pneumoniae NanA sialidase (SpCBM) (See Taylor, claim 19). The sialic acid binding molecule can comprise one or more CBMs, a plurality or multiple CBMs, a multivalent CBM, or two or more SpCBMs (See Taylor, claim 21). Moreover, the sialic acid binding molecule can further comprise an oligomerization domain (TD) (See Taylor, claim 23) such as an oligomerization domain derived from P. aeruginosa (See Taylor, claim 24). A specific embodiment of a sialic acid binding molecule is Sp2CBMTD (See Taylor, claim 26). As depicted in Figure 1, Sp2CBMTD contains two identical CBM40s derived from S. pneumoniae NanA sialidase, i.e., two monomers of SEQ ID NO: 4, conjugated to a trimerization domain derived from P. aeruginosa sialidase, i.e., SEQ ID NO: 6, where each of the two CBMs and trimerization domain are separated by a 5-amino acid linker (See Taylor, [0080], [0195]; Figure 1). More specifically, Taylor et al. teaches that the two 5-amino acid linker sequences are GGGSG, which links the first SpCBM to the second SpCBM, and GQALG, which links the second SpCBM to the TD (See Taylor, Table 3). As such, Taylor’ sialic acid binding molecule constitutes the instant Family 40 CBM as recited in instant claim 1, a CBM40 as recited in instant claim 16, and a glycan binding molecule of Sp2CBM40TD comprising of 2 CBMs from S. pneumoniae fuse to a trimerization domain as recited in instant claim 21 (note: Sp2CBM40TD is not limited to instant SEQ ID NO: 17). Thus, when considering the teachings of Taylor as a whole, Taylor suggests a method of modulating or priming an immune response in a subject by administering an immunomodulatory amount or quantity of a sialic acid binding molecule to a subject in need thereof where the immune response is protective against a viral infection and/or the immune response modulate the immune system to facilitate resolution and/or clearance of the infection thereby constituting treatment or prophylactic treatment of the viral infection, and where the sialic acid binding molecule comprises Sp2CBMTD, which comprises 2 CBMs (CBM40s) from S. pneumoniae fused to a trimerization domain.
With respect to where the viral infection is a SARS CoV-2 infection, Taylor et al. teaches that a respiratory disease and/or infection can be caused or contributed to by pathogens such as viruses belonging to the Orthomyxoviridae or Paramyxoviridae families and certain Streptococcus bacteria which utilize cell surface sialic acid containing receptors to bind and/or gain entry to specific cell types (See Taylor, [0026]). The sialic acid binding molecules can be used to modulate an immune response against the respiratory disease and/or infection (See Taylor, [0026], [0029]). A number of pathogens including viral and/or bacterial pathogens can express molecules that exhibit an affinity for sialic acid (See Taylor, [0033]). Pathogens of this type have evolved to exploit cell surface sialic acid moieties as a means to bind to host cells (See Taylor, [0033]). Once bound to a cell via, for example a host cell surface bound sialic acid moiety, a pathogen can colonize the cell surface and/or infect/enter the cell (See Taylor, [0033]). Although Taylor exemplifies that Sp2CBMTD represents a new host-directed class of therapeutics for influenza infections, Taylor suggests that other respiratory pathogens such as some coronaviruses also use sialic acid receptors for pathogenesis thereby implicating a broader application of the Sp2CBMTD in the future (See Taylor, [0225]). However, the teachings of Taylor do not expressly teach that the sialic acid molecules can be used to treat or prophylactically treat a SARS CoV-2 infection in a subject.
Matrosovich, et al. teaches that sialic acid linked to glycoproteins and gangliosides is used by many viruses as a receptor for cell entry (See Matrosovich, abstract) including influenza, parainfluenza, and coronaviruses (See Matrosovich, abstract). Attachment to sialic acid is mediated by receptor binding proteins that are constituents of viral envelopes or exposed at the surface of non-enveloped viruses (See Matrosovich, abstract). The initial step in the viral life cycle is the attachment of virus particles to the cell surface (See Matrosovich, pg. 2, 1st paragraph). Attachment is mediated by binding of the virus to a receptor (See Matrosovich, pg. 2, 1st paragraph). Sialic acid was the first virus receptor identified (See Matrosovich, pg. 2, 2nd paragraph). In particular, it was found that the receptor determinant of influenza virus was sialic acid and that the viral enzyme was a neuraminidase (See Matrosovich, pg. 2, 2nd paragraph). Since then, sialic acid has been found to serve as a receptor of a large spectrum of other viruses (See Matrosovich, pg. 2, 3rd paragraph). These other viruses include coronaviruses, which are divided into four genera: Alpha-, Beta-, Gamma-, and Deltacoronavirus (See Matrosovich, pg. 9, 2nd paragraph). Sialic acid binding activity varies between the four genera (See Matrosovich, pg. 9, 2nd paragraph). Some members of the Betacoronavirus genus recognize O-acetylated sialic acids and contain an acetylesterase that functions as a receptor-destroying enzyme, but some alpha- and gammacoronaviruses have a preference for N-acetyl- or N-glycolylneuraminic acid (See Matrosovich, pg. 9, 2nd paragraph). Betacoronaviruses have an acetylesterase, in particular, a sialate 9-O-acetylesterase that functions as a receptor-destroying enzyme (See Matrosovich, pg. 9, 2nd to last paragraph). The acetylesterase activity was assigned to the HE surface glycoprotein of Betacoronaviruses, and is present only in members of the Betacoronavirus genus (See Matrosovich, pg. 10, 1st paragraph). Matrosovich et al. also teaches that the HE protein has not only acetylesterase activity, but it can also function as a hemagglutinin (See Matrosovich, pg. 10, last paragraph). However, Betacoronaviruses also contain a second surface glycoprotein, the S protein, which has an important function in virus entry by being involved in the attachment of virions to the cell surface and by mediating the subsequent fusion of the viral and the cell membrane (See Matrosovich, pg. 10, last paragraph). The S protein of these viruses is the major hemagglutinin, and thus, the major sialic acid binding protein (See Matrosovich, pg. 11, 1st paragraph). Therefore, Matrosovich et al. teaches that Betacoronaviruses contain two surface glycoproteins that bind to host sialic acid receptors.
The CSG article teaches that the CSG of the Intl. Committee on Taxonomy of Viruses is responsible for developing the classification of viruses and taxon nomenclature of the family Coronaviridae, and has assessed the placement of the human pathogen, tentatively named 2019-nCoV, within the Coronaviridae (See CSG article, abstract). Based on phylogeny, taxonomy and established practice, the viruses (SARS-CoVs) of the species Severe acute respiratory syndrome-related coronavirus, and designates it as SARS-CoV-2 (See CSG article, abstract; pg. 536, col. 1, 3rd paragraph). The CSG further teaches that SARS-CoV-2 is part of the genus Betacoronavirus as depicted in Figures 1 and 2c (See CSG article, abstract; pg. 538, col. 2, last paragraph). It is noted that the disease spectrum and transmission efficiency of SARS-CoV-2 differs from those reported for SARS-CoV (See CSG article, abstract; pg. 539, col. 1, 2nd to last paragraph). Thus, when the teachings of the CSG article are combined with the teachings of Matrosovich, since SARS-CoV-2 is classified as a Betacoronavirus, it would then follow that SARS-CoV-2 contains two surface glycoproteins, the HE protein and the S protein, that bind to host sialic acid receptors.
Therefore, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the instant application to modify the teachings of Taylor and administer a Sp2CBMTD as a sialic acid binding molecule to a subject having or at risk of having a SARS CoV-2 infection in order to treat or prophylactically treat the SARS CoV-2 infection by modulating the immune system to facilitate resolution and/or clearance of the SARS CoV-2 infection. One of ordinary skill in the art at the time the invention was made would have been motivated to do so because betacoronaviruses were known to contain two surface glycoproteins, the HE protein and the S protein, that bind to host sialic acid receptors as taught by Matrosovich; and because SARS CoV-2 was known to be classified under the genus Betacoronavirus as taught by the CSG article. One of ordinary skill in the art at the time the invention was made would have had a reasonable expectation of success given that the Sp2CBMTD of Taylor was known to be administered to a subject in order to treat or prophylactically treat respiratory viral infections that utilize cell surface sialic acid containing receptors for pathogenesis such as coronaviruses by modulating the immune system to facilitate resolution and/or clearance of the viral infection, and therefore, substituting SARS CoV-2 infection as the respiratory viral infection would support the treatment or prophylactic treatment of a SARS CoV-2 infection in a subject by constituting some teaching, suggestion, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art reference teachings to arrive at the claimed invention and/or simple substitution of one known element for another to obtain predictable results pursuant to KSR.
Response to Arguments
Applicant's arguments filed 4/28/26 for claims 1, 8, 16, and 21-24 as being obvious pursuant to 35 USC 103(a) have been fully considered but they are not persuasive for the following reasons.
In response to Applicant’s first argument, i.e., the combination of cited references fail to teach or suggest the methods as recited in instant claims 1, 16, and 21 because Taylor’s reference to coronaviruses is merely a speculative statement that is an invitation to explore a new technology against a number of other respiratory pathogens besides the influenza viruses disclosed in the examples of Taylor (See Applicant’s Response received on 4/28/26, pg. 14), it is found unpersuasive. Pursuant to MPEP 2142, 35 USC 103 authorizes a rejection where, to meet the claim, it is necessary to modify a single reference or to combine it with one or more other references. Since the rejection is based on obviousness, it is unnecessary for every claim limitation to be taught and/or suggested by a single reference. Additionally, the Examiner recognizes that obviousness may be established by combining or modifying the teachings of the prior art to produce the claimed invention where there is some teaching, suggestion, or motivation to do so found either in the references themselves or in the knowledge generally available to one of ordinary skill in the art. See In re Fine, 837 F.2d 1071, 5 USPQ2d 1596 (Fed. Cir. 1988), In re Jones, 958 F.2d 347, 21 USPQ2d 1941 (Fed. Cir. 1992), and KSR International Co. v. Teleflex, Inc., 550 U.S. 398, 82 USPQ2d 1385 (2007). In this case, it is acknowledged that there is not a single reference that teaches and/or suggests every claim limitation recited in independent claims 1, 16, and 21 and the dependent claims. However, Applicants are respectfully reminded that the rejection supra is based on obviousness. As discussed in the rejection supra, Taylor expressly teaches a method of modulating or priming an immune response in a subject by administering an immunomodulatory amount or quantity of a sialic acid binding molecule to a subject in need thereof where the immune response is protective against a viral infection and/or the immune response modulate the immune system to facilitate resolution and/or clearance of the infection thereby constituting treatment or prophylactic treatment of the viral infection, and where the sialic acid binding molecule comprises Sp2CBMTD, which comprises 2 CBMs (CBM40s) from S. pneumoniae fused to a trimerization domain. The question is then whether an ordinary skilled artisan would be motivated with a reasonable expectation of success to administer Taylor’s sialic acid binding molecule comprises Sp2CBMTD, which comprises 2 CBMs (CBM40s) from S. pneumoniae fused to a trimerization domain, to treat or prophylactically treat a SARS-CoV-2 infection. The Examiner maintains that the answer is yes in light of the combination of references.
Pursuant to MPEP 2141, “[a] prior art reference must be considered in its entirety, i.e., as a whole, including portions that would lead away from the claimed invention. W.L. Gore & Assoc., Inc. v. Garlock, Inc., 721 F.2d 1540, 220 USPQ 303 (Fed. Cir. 1983), cert. denied, 469 U.S. 851 (1984). Moreover, pursuant to MPEP 2152.02(b), in order for a prior art document to describe a claimed invention under AIA 35 U.S.C. 102(a)(1) or (a)(2), the prior art document need only describe and enable one skilled in the art to make a single species or embodiment of the claimed invention. See Vas-Cath Inc. v. Mahurkar, 935 F.2d 1555, 1562, 19 USPQ2d 1111, 1115 (Fed. Cir. 1991). As discussed in the rejection supra, Taylor expressly teaches a sialic acid binding molecule comprising Sp2CBMTD, which comprises 2 CBMs (CBM40s) from S. pneumoniae fused to a trimerization domain, which can be administered to treat an infection that express molecules that exhibit an affinity for sialic acid (See Taylor, [0033]). Pathogens of this type have evolved to exploit cell surface sialic acid moieties as a means to bind to host cells (See Taylor, [0033]). Taylor even acknowledges that some coronaviruses use sialic acid receptors for pathogenesis (See Taylor, [0225]). Matrosovich and the CSG article suggest that SARS-CoV-2 pathogenesis utilizes cell surface sialic acid moieties as a means to bind to host cells thereby suggesting that SARS-CoV-2 would be a pathogen sought for treatment as suggested by Taylor. Thus, the fact that Taylor does not reduce-to-practice treatment of a coronavirus does not per se render the claimed methods nonobvious, especially when the combination of cited references demonstrate that SARS-CoV-2 pathogenesis involves sialic acid moieties. Therefore, contrary to Applicant’s argument, when considering the teachings of Taylor as a whole in combination with Matrosovich and CSG, an ordinary skilled artisan would have the requisite motivation to administer Taylor’s sialic acid binding molecule comprising Sp2CBMTD in order to treat or prophylactically treat a SARS-CoV-2 infection.
In response to Applicant’s second argument, i.e., the combination of cited references fail to provide an ordinary skilled artisan with a reasonable expectation of success in arriving at the claimed methods because Taylor merely provides an invitation to explore a new technology against a number of other respiratory pathogens besides influenza, Matrosovick and the CSG article merely informs the ordinary skilled artisan of the characteristics of SARS-CoV-2 without providing any indication as to how a coronavirus infection can be treated (See Applicant’s Response received on 4/28/26, pg. 14-15), it is found unpersuasive. Pursuant to MPEP 2143.02(II), obviousness does not require absolute predictability, however, at least some degree of predictability is required. Evidence showing there was no reasonable expectation of success may support a conclusion of nonobviousness. In re Rinehart, 531 F.2d 1048, 189 USPQ 143 (CCPA 1976). In the instant case, as discussed supra, Taylor expressly suggests administering the instant CBM40 as a sialic acid binding molecule to treat infections caused by pathogens that utilize sialic acid moieties during pathogenesis where some coronaviruses utilize sialic acid moieties during pathogenesis. Matrosovich and CSG suggest SARS-CoV-2 pathogenesis utilizes cell surface sialic acid moieties as a means to bind to host cells thereby suggesting that SARS-CoV-2 would be a pathogen sought for treatment as suggested by Taylor. Applicants have not provided any evidence to support why an ordinary skilled artisan would not have a reasonable (not absolute) expectation of success to administer Taylor’s CBM40 to treat a SARS-CoV-2 infection that is known to utilize cell surface sialic acid moieties as a means to bind to host cells during pathogenesis. Thus, contrary to Applicant’s argument, an ordinary skilled artisan would have the requisite expectation of success to arrive at the claimed methods.
Regarding Applicant’s reliance on In re Kubin, it is noted that the court considered the applicability of the KSR obvious-to-try rationale in rendering a claimed invention obvious. In re Kubin is discussed in MPEP 2143(I)(E) where the court found that there are two classes of situations where ‘obvious to try’ is erroneously equated with obviousness. One of these two classes of situations is when what was "obvious to try" was to explore a new technology or general approach that seemed to be a promising field of experimentation, where the prior art gave only general guidance as to the particular form of the claimed invention or how to achieve it. Id. (citing In re O’Farrell, 853 F.2d 894, 903, 7 USPQ2d 1673, 1681 (Fed. Cir. 1988)). However, the 103 rejection supra does not utilize an obvious to try rationale to render the claimed methods obvious. Rather, the rejection utilizes the KSR rationales of (1) some teaching, suggestion, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art reference teachings to arrive at the claimed invention and/or (2) simple substitution of one known element for another to obtain predictable results. Therefore, the holding in In re Kubin is not applicable to the instant 103 rejection.
Accordingly, the rejection of claims 1, 8, 16, and 21-24 as being obvious pursuant to 35 USC 103(a) is maintained as Applicants’ arguments are found unpersuasive.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1, 8, 16, and 21-24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2, 5-14, 17-27, 30-33, and 41 of U.S. Patent No. 9,066,894 B2 in view of Li et al., J. Med. Virol. 92:552-555 (February 2020), and Taylor et al. US 2017/0007692 A1 published on August 30, 2022 (cited in the IDS received on 8/30/22).
‘894 claims:
PNG
media_image1.png
113
654
media_image1.png
Greyscale
PNG
media_image2.png
61
628
media_image2.png
Greyscale
PNG
media_image3.png
134
627
media_image3.png
Greyscale
PNG
media_image4.png
38
573
media_image4.png
Greyscale
PNG
media_image5.png
28
328
media_image5.png
Greyscale
PNG
media_image6.png
62
638
media_image6.png
Greyscale
PNG
media_image7.png
327
644
media_image7.png
Greyscale
(See ‘894 claims 5-6, 9-10, 12-13, and 27-29 corresponding to issued claims 1-2, 5-8, and 10-12, respectively). As such, the administered CBM40 constitutes a glycan binding molecule comprising a CBM where the CBM is a Family 40 CBM as recited in instant claim 1; and a CBM40 as recited in instant claim 16. However, ‘894 does not claim where the treatment of pneumonia is a disease or condition caused or contributed by SARS CoV-2, and where the two CBM40 V. cholerae monomers are fused to a trimerization domain.
Please see discussion of Taylor et al. supra. Briefly, Taylor et al. teaches that a trimerization domain is fused to a combination of CBM40 monomers derived from V. cholerae. Therefore, an ordinary skilled artisan would be motivated with a reasonable expectation of success to fuse the two CBM40 V. cholerae monomers are fused to a trimerization domain given that a conjugate containing two CBM40 monomers derived from V. cholerae was known to be fused to a trimerization domain.
Li et al. teaches that SARS CoV-2 causes acute, highly lethal pneumonia coronavirus disease 2019 (COVID-19) (See Li, abstract; pg. 552, col. 2, last paragraph). Therefore, an ordinary skilled artisan would be motivated with a reasonable expectation of success to treat pneumonia as a disease or condition caused by SARS CoV-2 by administering ‘894’s SEQ ID NO: 9 given that pneumonia was known to be caused by SARS CoV-2. Therefore, the ‘894 claimed invention is not patentably distinct from the instantly claimed invention.
Response to Arguments
Applicant's arguments filed 4/28/26 for claims 1, 8, 16, and 21-24 as being obvious pursuant to 35 USC 103(a) have been fully considered but they are not persuasive for the following reasons.
In response to Applicant’s argument, i.e., the ‘894 patent is silent as to treating a coronavirus infection or a disease or condition caused by a coronavirus, Taylor merely provides an invitation to explore a new technology against a number of other respiratory pathogens besides influenza, and Li similarly provides a general invitation to explore potential prevention and treatment of the SARS-CoV-2 induced respiratory failure (See Applicant’s Response received on 4/18/26, pg. 15-16), it is found unpersuasive. Regarding Applicant’s argument that Taylor and Li only provide a general invitation to explore potential treatment options, Applicant’s attention is drawn to the “Response to Arguments” section supra for the 103 rejection. The response is incorporated herewith, but will not be reiterated in its entirety.
Furthermore, as discussed in the “Response to Arguments” section for the 103 rejection, it is acknowledged that the ‘894 patent does not claim every instant claim limitation, in particular, treatment or prophylactic treatment of SARS-CoV-2. However, the question to ask is whether an ordinary skilled artisan would be motivated to administer the ‘894 CBM40 to a subject in order to treat or prophylactic treat of SARS-CoV-2 where ‘894’s treatment of pneumonia is a disease or condition caused or contributed by SARS CoV-2. In other words, ‘894 claims a genus method of treatment, but does not specifically claim where the treatment is of a disease or condition caused or contributed by SARS-CoV-2. In light of the combined teachings of Taylor and Li, the Examiner maintains the answer to this question is yes because Taylor teaches the fusion of CBM40 monomers to an oligomerization domain to treat pathogens that utilize sialic acid moieties for pathogenesis and Li demonstrates that pneumonia was known to be caused by SARS CoV-2. Thus, an ordinary skilled artisan would be motivated to administer the ‘894 CBM40 to a subject in order to treat or prophylactic treat pneumonia as a disease or condition caused by SARS CoV-2.
Accordingly, the rejection of claims 1, 8, 16, and 21-24 is maintained as Applicants’ arguments are found unpersuasive.
Claims 1, 8, 16, and 21-24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2 of U.S. Patent No. 10,363,298 B2 in view of Matrosovich, et al., Top. Curr. Chem. 367:1-28 (2015), and Coronaviridae Study Group of the Intl. Committee on Taxonomy of Viruses, “The species Severe acute respiratory syndrome-related coronavirus: classifying 2019-nCoV and naming it SARS-CoV-2,” Nat. Microbiol. 5:536-544 (March 2, 2020) (hereinafter referred to as “CSG article”).
‘298 claims:
PNG
media_image8.png
132
656
media_image8.png
Greyscale
PNG
media_image9.png
82
653
media_image9.png
Greyscale
(‘298 claims 37 and 33 corresponding to issued claims 1-2, respectively). Turning to the specification as a dictionary pursuant to MPEP 804, Sp2CBMTD contains two CBM40 monomers derived from S. pneumoniae fused to a trimerization domain derived from P. aeruginosa (See instant, col. 18, 2nd paragraph). As such, ‘298’s administered Sp2CBMTD constitutes a CBM where the CBM is a Family 40 CBM as recited in instant claim 1; a CBM40 as recited in instant claim 16; and a glycan acid binding molecule that is Sp2CBM40TD comprising 2 CBMs from S. pneumoniae fused to a trimerization domain as recited in instant claim 21. However, ‘298 does not claim where the infection is SARS CoV-2 or a likely infection.
Please see discussion of Matrosovich, et al. and the CDG article supra along with the motivation to combine the ‘298 claimed invention with the prior art. Briefly, an ordinary skilled artisan would be motivated with a reasonable expectation of success to administer ‘298’s Sp2CBMTD to a subject in order to treat SARS CoV-2 as an infection given that SARS CoV-2 is known to be a Betacoronavirus, which are known to contain two surface glycoproteins, the HE protein and the S protein, that bind to host sialic acid receptors. Therefore, the ‘298 claimed invention is not patentably distinct from the instantly claimed invention.
Response to Arguments
Applicant's arguments filed 4/28/26 for claims 1, 8, 16, and 21-24 as being obvious pursuant to 35 USC 103(a) have been fully considered but they are not persuasive for the following reasons. Applicants’ arguments mirror the arguments for the 103 rejection supra. Thus, the response to Applicants’ arguments similarly mirror the response to arguments for the 103 rejection supra. Therefore, the response to Applicants’ arguments are incorporated herewith, but will not be reiterated.
Claims 1, 8, 16, and 19-24 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 8-16 of copending Application No. 17/753,273 (US Publication No. 2023/0054093 A1) in view of Li et al., J. Med. Virol. 92:552-555 (February 2020).
‘273 claims:
PNG
media_image10.png
176
649
media_image10.png
Greyscale
PNG
media_image11.png
91
644
media_image11.png
Greyscale
PNG
media_image12.png
307
638
media_image12.png
Greyscale
PNG
media_image13.png
94
641
media_image13.png
Greyscale
PNG
media_image14.png
403
649
media_image14.png
Greyscale
PNG
media_image15.png
66
624
media_image15.png
Greyscale
(‘273 claims 8-10 and 13-16). It is noted that ‘273’s SEQ ID NO: 9 is 100% identical to instant SEQ ID NO: 17. As such, ‘273 claims a glycan binding molecule comprises a CBM where the CBM is a Family 40 CBM as recited in instant claim 1; a CBM40 as recited in instant claim 16; where the CBM comprises a modified CBM comprising a wild type CBM sequence with one or more mutations, i.e., V239A, V246G, and A162P, as recited in instant claim 19; where the modified CBM comprises instant SEQ ID NO: 17 as recited in instant claim 20; and a glycan acid binding molecule that is Sp2CBM40TD comprising 2 CBMs from S. pneumoniae fused to a trimerization domain as recited in instant claim 21. ‘273 also claims where the sialic acid binding molecule is administered intranasally or mucosally (‘273 claims 11-12). ‘273 claims where the sialic acid binding molecule does not exhibit sialidase activity (‘273 claim 14). These claims are encompassed by the claimed invention. However, ‘273 does not claim where the treatment of pneumonia is a disease or condition caused or contributed by SARS CoV-2.
Li et al. teaches that SARS CoV-2 causes acute, highly lethal pneumonia coronavirus disease 2019 (COVID-19) (See Li, abstract; pg. 552, col. 2, last paragraph). Therefore, an ordinary skilled artisan would be motivated with a reasonable expectation of success to treat pneumonia as a disease or condition caused by SARS CoV-2 by administering ‘273’s SEQ ID NO: 9 given that pneumonia was known to be caused by SARS CoV-2.
This is a provisional nonstatutory double patenting rejection.
Response to Arguments
Applicant's arguments filed 4/28/26 for claims 1, 8, 16, and 19-24 as being obvious pursuant to 35 USC 103(a) have been fully considered but they are not persuasive for the following reasons.
In response to Applicant’s argument, i.e., the ‘273 application is silent as to treating a coronavirus infection or a disease or condition caused by a coronavirus, and Li only provides a general invitation to explore potential prevention and treatment of the SARS-CoV-2 induced respiratory failure (See Applicant’s Response received on 4/28/26, pg. 17), it is found unpersuasive. Regarding Applicant’s argument that Li only provide a general invitation to explore potential treatment options, Applicant’s attention is drawn to the “Response to Arguments” section supra for the 103 rejection. The response is incorporated herewith, but will not be reiterated in its entirety.
Furthermore, as discussed in the “Response to Arguments” section for the 103 rejection, it is acknowledged that the ‘273 application does not claim every instant claim limitation, in particular, treatment or prophylactic treatment of SARS-CoV-2. However, the question to ask is whether an ordinary skilled artisan would be motivated to administer the ‘273 CBM40 to a subject in order to treat or prophylactic treat of SARS-CoV-2 where ‘273’s treatment of pneumonia is a disease or condition caused or contributed by SARS CoV-2. In other words, ‘273 claims a genus method of treatment, but does not specifically claim where the treatment is of a disease or condition caused or contributed by SARS-CoV-2. In light of the teachings of Li, the Examiner maintains the answer to this question is yes because Li demonstrates that pneumonia was known to be caused by SARS CoV-2. Thus, an ordinary skilled artisan would be motivated to administer the ‘894 CBM40 to a subject in order to treat or prophylactic treat pneumonia as a disease or condition caused by SARS CoV-2.
Accordingly, the rejection of claims 1, 8, 16, and 19-24 is maintained as Applicants’ arguments are found unpersuasive.
Examiner Comment
For claims 19-20, notwithstanding the 112 and obviousness-type double patenting rejections, it is noted that the claimed methods of free of the art when instant SEQ ID NO: 17 is administered to a subject. Notably, SEQ ID NO: 17 contains two monomers of modified SEQ ID NO: 6, each with three substitutions: V239A, V426G, and A162P, and a trimerization domain containing modified SEQ ID NO: 14 with two substitutions: S342D and R403K (See instant, pg. 24, HEX17 structure). As such, instant SEQ ID NO: 17 contains the structure: GAM---SEQ ID NO: 6 (V239A, V246G, and A162P)---GGGSG---SEQ ID NO: 6 (V239A, V246G, and A162P)---GGSLG---SEQ ID NO: 14 (S342D, R403K). The GGGSG and GGSLG are 5-amino acid linkers. The closest prior art is: Taylor et al. US 2017/0007692 A1 published on August 30, 2022 (cited in the IDS received on 8/30/22). Taylor teaches that a specific species of sialic acid binding molecule to be administered is Sp2CBMTD (See Taylor, claim 26). As depicted in Figure 1, Sp2CBMTD contains two identical CBM40s derived from S. pneumoniae NanA sialidase, i.e., two monomers of SEQ ID NO: 4, conjugated to a trimerization domain derived from P. aeruginosa sialidase, i.e., SEQ ID NO: 6, where each of the two CBMs and trimerization domain are separated by a 5-amino acid linker (See Taylor, [0080], [0103], [0195]; Figure 1). More specifically, Taylor et al. teaches that the two 5-amino acid linker sequences are GGGSG, which links the first SpCBM to the second SpCBM, and GQALG, which links the second SpCBM to the TD (See Taylor, Table 3). It is noted that SEQ ID NO: 4 spans residues 121-305 of the full length S. pneumoniae nanA sialidase protein (See Taylor, [0039]; [0080]; [0103]). When comparing Taylor’s SEQ ID NO: 4 with instant SEQ ID NO: 6, i.e., the CBM region derived from S. pneumoniae nanA sialidase, there is 100% identity. Moreover, the first 5-amino acid linker sequence, i.e., GGGSG, is identical to the 5-amino acid linker sequence linking the CBMX1 component and CBMX2 component of instant SEQ ID NO: 17. Furthermore, Taylor’s SEQ ID NO: 6 is 100% identical to instant SEQ ID NO: 14 as a trimerization domain. Thus, Taylor’s Sp2CBMTD contains the structure: instant SEQ ID NO: 6---GGGSG---instant SEQ ID NO: 6---GQALG---instant SEQ ID NO: 14. However, Taylor does not expressly teach a Sp2CBMTD amino acid sequence that is 100% identical to instant SEQ ID NO: 17 with the three substitutions, namely, V239A, V426G, and A162P.
Furthermore, it is noted that WO 2019/138222 A2 (cited in the IDS received on 8/30/22) and WO 2019/166802 A2 cannot be used as prior art because both references are excluded under 35 USC 102(b)(1)(A) and/or 35 USC 102(b)(2)(C).
Conclusion
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to THEA D' AMBROSIO whose telephone number is (571)270-1216. The examiner can normally be reached M-F 11:00 to 8:00 pm.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Lianko Garyu can be reached at 571-270-7367. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/THEA D' AMBROSIO/ Primary Examiner, Art Unit 1654
Prosecution Insights