DETAILED ACTION
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 .
Claim Status
Claims 1-19 are pending. Claims 15 and 18 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species, there being no allowable generic or linking claim.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 07/15/2026. Applicant elected the invention of Group I (claims 1-14, 16-17, and 19) and the following species:
Claims 2-3: a fragment of amino acids at positions 53 to 72 (SEQ ID NO: 68) and a fragment of amino acids at positions 135 to 159 (SEQ ID NO: 70);
Claims 4-9: #9104 antibody which comprises heavy chain variable region comprising a heavy chain CDR1 to CDR3 consisting of the amino acid sequence as set forth in SEQ NO ID Nos: 31 (NYYMS), 32 (GIYYGSGNIYYADSVKG), and 33 (DTPGFDY), respectively, and a light chain CDR1 to CDR3 consisting of the amino acid sequence as set forth in SEQ NO ID Nos: 49 (TGSSSNIGNNAVN), 50 (YDSHRPS), and 51 (GAWDYSLSAYV), respectively; and
Claim 11: human ASM protein (SEQ ID NO: 66).
Claims 1-14, 16-17, and 19 are currently under consideration for patentability under 37 CFR 1.104.
Priority
This application is a 371 of PCT/KR2022/095105 (filed on 05/26/2022) which claims benefit of Republic of Korea Application Nos. KR10-2021-0068075 (filed on 05/27/2021) and KR10-2022-0047295 (filed on 04/18/2022). Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged.
Applicant cannot rely upon the certified copies of the foreign priority applications, applicable to KR10-2021-0068075 and KR10-2022-0047295, because translations of said applications have not been made of record in accordance with 37 CFR 1.55. When an English language translation of a non-English language foreign application is required, the translation must be that of the certified copy (of the foreign application as filed) submitted together with a statement that the translation of the certified copy is accurate. See MPEP §§ 215 and 216.
Because an English translation of the certified copy of the foreign priority application has not been made of the record, the examiner cannot establish whether or not what is claimed in the instant application was properly disclosed in the foreign priority application. Therefore, the benefit to the foreign priority application date is not granted.
Claims 1-14, 16-17, and 19 have an effective filing date of 05/26/2022 corresponding to PCT/KR2022/095105.
Information Disclosure Statement
The information disclosure statement(s) filed on 11/27/2023, 09/05/2024, 07/30/2025, and 07/15/2026 has/have been considered. Signed copies are enclosed. All references considered unless marked with strikethrough.
Drawings
The drawings are objected to because Fig. 1 contains sequences that do not appear in the drawings and/or in the Brief Description of the Drawings.
Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
Nucleotide and/or Amino Acid Sequence Disclosures
REQUIREMENTS FOR PATENT APPLICATIONS CONTAINING NUCLEOTIDE AND/OR AMINO ACID SEQUENCE DISCLOSURES
Items 1) and 2) provide general guidance related to requirements for sequence disclosures.
37 CFR 1.821(c) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.821(a) must contain a "Sequence Listing," as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.821 - 1.825. This "Sequence Listing" part of the disclosure may be submitted:
In accordance with 37 CFR 1.821(c)(1) via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter "Legal Framework") as an ASCII text file, together with an incorporation-by-reference of the material in the ASCII text file in a separate paragraph of the specification as required by 37 CFR 1.823(b)(1) identifying:
the name of the ASCII text file;
ii) the date of creation; and
iii) the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(1) on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation-by-reference of the material in the ASCII text file according to 37 CFR 1.52(e)(8) and 37 CFR 1.823(b)(1) in a separate paragraph of the specification identifying:
the name of the ASCII text file;
the date of creation; and
the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(2) via the USPTO patent electronic filing system as a PDF file (not recommended); or
In accordance with 37 CFR 1.821(c)(3) on physical sheets of paper (not recommended).
When a “Sequence Listing” has been submitted as a PDF file as in 1(c) above (37 CFR 1.821(c)(2)) or on physical sheets of paper as in 1(d) above (37 CFR 1.821(c)(3)), 37 CFR 1.821(e)(1) requires a computer readable form (CRF) of the “Sequence Listing” in accordance with the requirements of 37 CFR 1.824.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed via the USPTO patent electronic filing system as a PDF, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the PDF copy and the CRF copy (the ASCII text file copy) are identical.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed on paper or read-only optical disc, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the paper or read-only optical disc copy and the CRF are identical.
Specific deficiencies and the required response to this Office Action are as follows:
Specific deficiency – Nucleotide and/or amino acid sequences appearing in the drawings are not identified by sequence identifiers in accordance with 37 CFR 1.821(d). Sequence identifiers for nucleotide and/or amino acid sequences must appear either in the drawings or in the Brief Description of the Drawings.
Required response – Applicant must provide:
Replacement and annotated drawings in accordance with 37 CFR 1.121(d) inserting the required sequence identifiers;
AND/OR
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required sequence identifiers into the Brief Description of the Drawings, consisting of:
A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
A copy of the amended specification without markings (clean version); and
A statement that the substitute specification contains no new matter.
Specification
Applicant is reminded of the proper language and format for an abstract of the disclosure.
The abstract should be in narrative form and generally limited to a single paragraph on a separate sheet within the range of 50 to 150 words in length. The abstract should describe the disclosure sufficiently to assist readers in deciding whether there is a need for consulting the full patent text for details.
The language should be clear and concise and should not repeat information given in the title. It should avoid using phrases which can be implied, such as, “The disclosure concerns,” “The disclosure defined by this invention,” “The disclosure describes,” etc. In addition, the form and legal phraseology often used in patent claims, such as “means” and “said,” should be avoided.
Claim Objections
Claims 5 and 7 is objected to because of the following informalities:
Claim 5: “consisting of, glycine” is line 4 should read “consisting of glycine”; and
Claim 7: “respectively” should be removed from the groups of amino acids sequences (6 instances).
Appropriate correction is required.
Claim Rejections - 35 USC § 112(a)
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, 10-14, 16-17, and 19 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Instant claim 1 is drawn to “[a]n antibody or antigen-binding fragment thereof that specifically binds to an acid sphingomyelinase (ASM) protein” (lines 1-2). Instant claims 2-3 further specify said antibody or antigen-binding fragment binds distinct epitopes of the ASM protein, delineating either amino acid fragments (instant claim 2) or SEQ ID NOs: 68-73 (instant claim 3) for the epitopes. This functional language encompasses a broad genus of structurally distinct anti-ASM protein antibodies and antigen-binding fragments. In addition, antigen-binding fragments may contain less than 6 CDRs.
Instant claims 4-8 further specify the 6 CDRs of the antibody or antigen-binding fragment. However, 1) instant claims 4-6 recite 23 variable amino acid positions within the CDRs, leading to billions of possible variants and 2) instant claims 7-8 recite CDR combinations, leading to thousands of possible combinations.
The instant specification states “the term ‘antibody’ refers to an immune protein that binds to an antigen to interfere with an action of the antigen or eliminate the antigen” (¶ 0025) and “the antigen-binding fragment may refer to a region except for Fc” (¶ 0027, emphasis added). The use of “may” indicates an optional preference. Therefore, the terms for antibody and antigen-binding fragment are incredibly broad and do not specify the minimum number of CDRs for binding i.e. they can contain less than 6 CDRs.
Antibodies and antigen-binding fragments include but not limited to Fabs, scFvs, VHHs, full-length antibodies, and antibody-drug conjugates, which have distinct structures and functions. For example, Sifniotis et al. (Current Advancements in Addressing Key Challenges of Therapeutic Antibody Design, Manufacture, and Formulation, Antibodies, 2019) state there are numerous formats to address challenges in antibody therapeutics including “bispecific and fragment mAb platforms for tailored engagement and increased bioavailability, and recombinant Fc-fusion proteins for an increased half-life and introduced immunological engagement” (Pg. 14, ¶ 4, lines 4-5). In addition, antibody fragments include “Fabs and single chain variable fragments (scFv)” (Sifniotis et al., Pg. 9, ¶ 4, line 4). These fragments show “better tissue penetration and biodistribution than whole mAb therapeutics; however, a pitfall of smaller peptides lacking an Fc region is a highly reduced in vivo half-life and poor retention times” (Sifniotis et al., Pg. 11, last ¶, lines 1-3). Therefore, antibodies and antigen-binding fragments encompass a variety of species, each with their own advantages and disadvantages (instant claims 1-8).
Sevy and Meiler (Antibodies: computer-aided prediction of structure and design of function, Microbiol Spectrum, 2014) state “antibodies pose formidable challenges for protein structure prediction and design due to their large size and highly flexible loops in the complementarity-determining regions” (Pg. 1, Abstract, lines 6-9). Consequently, an antibody’s structure cannot be predicted from function alone accurately i.e. stating the antibody binds the ASM protein (instant claim 1) or specific epitopes within said protein (instant claims 2-3) is not a sufficient description.
Furthermore, the instant specification does not specify how to create antibody fragments that exhibit the desired biological activity (i.e. retain the ability to bind the ASM protein) nor the minimal number of CDRs required (i.e. the antibody fragment can contain less than 6 CDRs). Wong et al. (Comparative Analysis of the CDR Loops of Antigen Receptors, Front Immunol, 2019) teach “[a]ll six antibody CDRs can be involved in antigen recognition... As the CDRs form the majority of the binding site, their conformations are critical to the binding” (Pg. 2, column 1, ¶ 1, lines 9-15). This teaching indicates all six CDRs can be required for antigen binding (instant claims 1-3).
Even minor changes in the amino acid sequences of the heavy and light variable regions, particularly in the CDRs, may dramatically affect antigen-binding function as evidenced by Rudikoff et al. (Proc. Natl. Acad. Sci. USA, 79(6):1979-1983, March 1982; IDS filed on 07/15/2026, Cite No. 17). Rudikoff et al. teach that the alteration of a single amino acid in the CDR of a phosphocholine-binding myeloma protein resulted in the loss of antigen-binding function. Colman (Research in Immunology, 145:33-36, 1994) teaches that even a very conservative substitution may abolish binding or may have very little effect on the binding affinity (Pg. 35, top of left column; Pg. 33, right column). Taken together, the teachings indicate perturbation to the CDRs of an antibody can have disastrous effects. Therefore, it would not be predictable how CDR mutations or rearrangement would affect binding affinity (instant claims 4-8).
As such, instant claims 1-8 are drawn to a genus of anti-ASM protein antibodies and antigen-binding fragments. The instant application teaches six scFvs comprising heavy chain CDRs 1-3 in Table 3 and light chain CDRs 1-3 in Table 4 (¶ 0071), referred to as #9101, #9102, #9104, #9108, #9113, and #9123. These antibodies have identical CDRs to those recited in instant claim 9.
However, Applicant is claiming a large and structurally diverse genus of anti-ASM protein antibodies and antigen-binding fragments. Absent empirical determination, one skilled in the art would be unable to immediately envision, recognize, or distinguish at least most of the members comprised within the genus claimed, specifically the structures of the antibodies and antigen-binding fragments that bind the ASM protein. Applicant uses the functional language of binding the ASM protein in instant claims 1-3 to define the genus which is not sufficient as it is difficult to predict structure from function (see Sevy and Meiler) and it is generally known in the art that 6 parental CDRs are needed for binding (see Wong et al.). While instant claims 4-8 delineate the 6 CDRs for the antibody or antigen-binding fragment, it is not predictable how CDR mutations or rearrangement would affect its binding affinity (see Rudikoff and Colman).
Accordingly, Applicant’s disclosure is not sufficient to demonstrate possession of the entire claimed genus and Applicant’s disclosure does not satisfy the written description requirement of 35 U.S.C. 112(a).
The MPEP states that the purpose of the written description requirement is to ensure that the inventor had possession, as of the filing date of the application, of the specific subject matter later claimed. The MPEP lists factors that can be used to determine if sufficient evidence of possession has been furnished in the disclosure of the application, including “the level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention” (MPEP 2163[II][A][2]).
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, disclosure of drawings, or by disclosure of relevant identifying characteristics, for example, 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 Applicants were in possession of the claimed genus.
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. As previously indicated, Applicant has disclosed six scFvs within the genus claimed. However, given the large number of species encompassed by the genus claimed as well as the high level of structure variation that would be displayed by members of the claimed genus, the disclosure of a subset of adequately described species is not sufficiently representative of the entire genus.
Furthermore, Applicant has not disclosed relevant, identifying characteristics of CDR amino acid sequences that confer upon an antibody the ability to bind the ASM protein. It is well-known in the art that antibodies generally comprise six parental CDRs. Absent a description of the at least minimal structural features correlating with a functional ability to bind the ASM protein which are shared by members of a genus of antigen-binding fragments, it is submitted that the skilled artisan could not immediately envision, recognize, or distinguish what portion of an antibody (i.e. an antigen-binding fragment comprising CDRs) that confer the ability to bind the ASM protein.
Although screening techniques can be used to find antibodies and antigen-binding fragments that possess the ability to bind the ASM protein, Applicant is reminded that the written description requirement of 35 U.S.C. 112 is severable from the enablement provision. As stated in Vas-Cath Inc. v. Mahurkar (CA FC) 19 USPQ2d 1111, 935 F2d 1555, “The purpose of the ‘written description’ requirement is broader than to merely explain how to ‘make and use’; the applicant must also 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, whatever is now claimed.”
Accordingly, given the difficulty associated with predicting structures of antibodies and antigen-binding fragments that bind the ASM protein and given the lack of particularity with which the genus is described in the specification, it is submitted that the skilled artisan could not immediately envision, recognize, or distinguish at least most of the members of the genus to which the claims are directed, and therefore the instant disclosure fails to demonstrate that Applicant was in possession of the claimed invention at the time the application was filed.
University of California v. Eli Lilly and Co., 43 USPQ2d 1398, 1404. 1405 held that: To fulfill the written description requirement, a patent specification must describe an invention and does so in sufficient detail that one skilled in the art can clearly conclude that "the inventor invented the claimed invention.” Lockwood v. American Airlines Inc., 107 F.3d 1565, 1572, 41 USPQ2d 1961, 1966 (1997); In re Gosteli , 872 F.2d 1008, 1012, 10 USPQ2d 1614, 1618 (Fed. Cir. 1989) ("[T]he description must clearly allow persons of ordinary skill in the art to recognize that [the inventor] invented what is claimed."). Thus, an applicant complies with the written description requirement "by describing the invention, with all its claimed limitations, not that which makes it obvious," and by using "such descriptive means as words, structures, figures, diagrams, formulas, etc., that set forth the claimed invention" Lockwood, 107 F.3d at 1572, 41 USPQ2datl966.
The specification does not reasonably convey possession of the subject matter of instant claims 1-8. Instant claims 1-8 fail to comply with the written description requirement of 35 U.S.C. 112(a) as a person having ordinary skill in the art cannot reasonably conclude that the applicant had possession of the claimed invention at the time the instant application was filed. Instant claims 10-14, 16-17, and 19 are included in this rejection as they incorporate and/or depend on instant claim 1. Instant claim 9 is not included in this rejection as it delineates sequences of the six scFvs as taught by the instant application (Tables 3 and 4).
Claims 4-8 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 scFvs #9101, #9102, #9104, #9108, #9113, and #9123 comprising 6 CDRs as recited in Tables 3-4 that specifically bind the ASM protein, does not reasonably provide enablement for a genus of variants of antibodies and antigen-binding fragments that specifically bind the ASM protein. 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.
As a general rule, enablement must be commensurate with the scope of claim language. MPEP 2164.08 states, “The Federal Circuit has repeatedly held that “the specification must teach those skilled in the art how to make and use the full scope of the claimed invention without undue experimentation’.” In re Wright, 999 F.2d 1557, 1561, 27 USPQ2d 1510, 1513 (Fed. Cir. 1993)” (emphasis added). The “make and use the full scope of the invention without undue experimentation” language was repeated in 2005 in Warner-Lambert Co. v. Teva Pharmaceuticals USA Inc., 75 USPQ2d 1865, and Scripps Research Institute v. Nemerson, 78 USPQ2d 1019 asserts: “A lack of enablement for the full scope of a claim, however, is a legitimate rejection.” The principle was explicitly affirmed most recently in Auto. Tech. Int’l, Inc. v. BMW of N. Am., Inc., 501 F.3d 1274, 84 USPQ2d 1108 (Fed. Cir. 2007), Monsanto Co. v. Syngenta Seeds, Inc., 503 F.3d 1352, 84 U.S.P.Q.2d 1705 (Fed. Cir. 2007), and Sitrick v. Dreamworks, LLC, 516 F.3d 993, 85 USPQ2d 1826 (Fed. Cir. 2008). See also In re Cortright, 49 USPQ2d 1464, 1466 and Bristol-Myers Squibb Co. v. Rhone-Poulenc Rorer Inc., 49 USPQ2d 1370.
The factors to be considered in determining whether a disclosure meets the enablement requirement of 35 U.S.C. 112, first paragraph, have been described in In re Wands, 8 USPQ2d 1400 (Fed. Cir. 1988). Among these factors are: (1) the nature or the invention; (2) the state of the prior art; (3) the relative skill of those in the art; (4) the predictability or unpredictability of the art; (5) the breadth of the claims; (6) the amount of direction or guidance presented; (7) the presence or absence of working examples; and (8) the quantity of experimentation necessary. When the above factors are weighed, it is the examiner’s position that one skilled in the art could not practice the invention without undue experimentation. Some experimentation is not fatal; the issue is whether the amount of experimentation is “undue”; see In re Vaeck, 20 USPQ2d 1438, 1444.
(1) The nature of the invention, (2) the state of the prior art, (3) The relative skill of those in the art, (4) the predictability or unpredictability of the art, and (5) the breadth of the claims
Instant claims 4-8 are drawn to an antibody or antigen-binding fragments that specifically bind the ASM protein comprising 6 CDRs. However, 1) instant claims 4-6 recite 23 variable amino acid positions within the CDRs, leading to billions of possible variants and 2) instant claims 7-8 recite CDR combinations, leading to thousands of possible combinations.
The instant specification states “the term ‘antibody’ refers to an immune protein that binds to an antigen to interfere with an action of the antigen or eliminate the antigen” (¶ 0025) and “the antigen-binding fragment may refer to a region except for Fc” (¶ 0027, emphasis added). The use of “may” indicates an optional preference. Therefore, the terms for antibody and antigen-binding fragment are incredibly broad, including but not limited to Fabs, scFvs, VHHs, full-length antibodies, and antibody-drug conjugates.
Accordingly, instant claims 4-8 are drawn to a genus of variants of antibodies and antigen-binding fragments that specifically bind the ASM protein, the full scope of which is not enabled as instantly claimed (the nature of the invention and the breadth of the claims). It is not clear that a person having ordinary skill in the art would be able to use all species encompassed by the genus to bind the ASM protein.
Sifniotis et al. (Current Advancements in Addressing Key Challenges of Therapeutic Antibody Design, Manufacture, and Formulation, Antibodies, 2019) state there are numerous formats to address challenges in antibody therapeutics including “bispecific and fragment mAb platforms for tailored engagement and increased bioavailability, and recombinant Fc-fusion proteins for an increased half-life and introduced immunological engagement” (Pg. 14, ¶ 4, lines 4-5). In addition, antibody fragments include “Fabs and single chain variable fragments (scFv)” (Sifniotis et al., Pg. 9, ¶ 4, line 4). These fragments show “better tissue penetration and biodistribution than whole mAb therapeutics; however, a pitfall of smaller peptides lacking an Fc region is a highly reduced in vivo half-life and poor retention times” (Sifniotis et al., Pg. 11, last ¶, lines 1-3). Therefore, antibodies and antigen-binding fragments encompass a variety of species, each with their own advantages and disadvantages (the state of the prior art).
Even minor changes in the amino acid sequences of the heavy and light variable regions, particularly in the CDRs, may dramatically affect antigen-binding function as evidenced by Rudikoff et al. (Proc. Natl. Acad. Sci. USA, 79(6):1979-1983, March 1982; IDS filed on 07/15/2026, Cite No. 17). Rudikoff et al. teach that the alteration of a single amino acid in the CDR of a phosphocholine-binding myeloma protein resulted in the loss of antigen-binding function. Colman (Research in Immunology, 145:33-36, 1994) teaches that even a very conservative substitution may abolish binding or may have very little effect on the binding affinity (Pg. 35, top of left column; Pg. 33, right column). Taken together, the teachings indicate perturbation to the CDRs of an antibody can have disastrous effects. Therefore, it would not be predictable how CDR mutations or rearrangement would affect binding affinity (the state of the prior art).
The instant application teaches six scFvs comprising heavy chain CDRs 1-3 in Table 3 and light chain CDRs 1-3 in Table 4 (¶ 0071), referred to as #9101, #9102, #9104, #9108, #9113, and #9123. These antibodies have identical CDRs to those recited in instant claim 9.
However, Applicant is claiming a large and structurally diverse genus of variants of anti-ASM protein antibodies and antigen-binding fragments (the breadth of the claims). This invention is in a class of invention which the CAFC has characterized as "the unpredictable arts such as chemistry and biology". Mycogen Plant Sci., Inc. v. Monsanto Co., 243 F.3d 1316, 1330 (Fed. Cir. 2001). For a person having ordinary skill in the art, i.e. someone with a PhD and/or MD (the relative skill of those in the art), the predictability of using any variant encompassed by the genus of antibodies and antigen-binding fragments that specifically bind the ASM protein would be low (the predictability or unpredictability of the art) given that it is not predictable how CDR mutations or rearrangement would affect its binding affinity to the ASM protein (see Rudikoff and Colman); consequently, this leads to a lack of enablement as a person having ordinary skill in the art would not be able to use all variants of the genus to bind the ASM protein.
Therefore, scFvs #9101, #9102, #9104, #9108, #9113, and #9123 comprising 6 CDRs as recited in Tables 3-4 that specifically bind the ASM protein is supported. A genus of variants of antibodies and antigen-binding fragments that specifically bind the ASM protein as recited in instant claims 4-8 is not supported.
(6) The amount of direction or guidance presented, (7) the presence or absence of working examples, and (8) the quantity of the experimentation
The instant application teaches six scFvs comprising heavy chain CDRs 1-3 in Table 3 and light chain CDRs 1-3 in Table 4 (¶ 0071), referred to as #9101, #9102, #9104, #9108, #9113, and #9123. These antibodies have identical CDRs to those recited in instant claim 9.
The specification does not provide any additional examples or guidance on how to use other variants of antibodies and antigen-binding fragments that specifically bind the ASM protein as recited in instant claims 4-8 other than the six scFvs mentioned above (the amount of direction or guidance presented and the presence or absence of working examples). Given how large and structurally diverse the genus of variants of anti-ASM protein antibodies and antigen-binding fragments is (see the 112(a) written description section for more information), it would require extensive screening and testing to determine which species retain their binding to the ASM protein (i.e. which mutations, which combination of CDRs, and which format of antibody or antigen-binding fragment produce binding to the ASM protein), leading to an unreasonable amount of experimentation. This experimentation is not routine and would therefore require undue experimentation (the quantity of the experimentation, see MPEP 2164.06).
Instant claims 4-8 is not enabled because a person having ordinary skill in the art as of the effective filing date of the application would not be able to use a genus of variants of antibodies and antigen-binding fragments to specifically bind the ASM protein with a predictability of success for the reasons outlined above.
Claim Rejections - 35 USC § 112b
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 2 and 4 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Regarding claim 2, the phrase “epitope selected from the group consisting of a fragment of amino acids at positions 53 to 72, a fragment of amino acids at positions 101 to 123, a fragment of amino acids at positions 135 to 159, a fragment of amino acids at positions 135 to 155, a fragment of amino acid at positions 218 to 228, and a fragment of amino acids at positions 259 to 269 from the N-terminus of the ASM protein" render the claim indefinite because as there is no sequence provided for the recited ASM protein, and one would not reasonably be able to determine the metes and bounds of the claim when the claim references positions in an undisclosed sequence. Examiner notes that the SEQ ID NOs provided in claim 11 further limit the sequence of the ASM protein, but claim 2 does not depend from claim 11. As no ASM sequence is present in the recitation of claim 2, it is indefinite.
For the purposes of claim interpretation, the sequence of the ASM protein will be treated as SEQ ID NOs: 66 or 67.
Regarding claim 4, the use of variable amino acid residues in heavy chain CDRs 1-2 and light chain CDRs 1-2 renders the claim indefinite because the identity of the variable amino acid residues is not clear. As claims need to be complete in themselves (see MPEP 2173), all variable amino acid residues should be defined within the claim itself.
Claims 5 and 6 are not included in this rejection as they define all variable amino acid residues in heavy chain CDRs 1-2 and light chain CDRs 1-2.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1, 10, and 16 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Rousson et al. (Preparation of an anti-acid sphingomyelinase monoclonal antibody for the quantitative determination and polypeptide analysis of lysosomal sphingomyelinase in fibroblasts from normal and Niemann-Pick type A patients, Journal of Immunological Methods, Vol. 160, pp. 199-206, 1993; IDS filed on 11/27/2023, Cite No. 2).
Rousson et al. teach “[a]n anti-acid sphingomyelinase monoclonal antibody” (Pg. 199, Abstract, line 1), reading on an antibody that specifically binds the ASM protein (instant claim 1). Rousson et al. further teach the antibody binds “normal and mutated sphingomyelinase in Niemann-Pick type A patients” (Pg. 199, Abstract, line 5), reading on the ASM protein is derived from a mammal (i.e. a human patient) (instant claim 10). Rousson et al. teach the antibody was used in immunostaining to detect placental ASM protein (Pg. 203, Fig. 2, lanes 1 and 2 stained with the monoclonal antibody with the name MAB 236) wherein said antibody was incubated with the antigen in “10 mM Tris-HCl” (Pg. 203, column 1, ¶ 2, line 4) i.e. a composition, reading on using the antibody in a composition for detecting the ASM protein (instant claim 16).
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
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 for establishing a background for determining obviousness under 35 U.S.C. 103 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.
Claim 11 is rejected under 35 U.S.C. 103 as being unpatentable over Rousson et al. (Preparation of an anti-acid sphingomyelinase monoclonal antibody for the quantitative determination and polypeptide analysis of lysosomal sphingomyelinase in fibroblasts from normal and Niemann-Pick type A patients, Journal of Immunological Methods, Vol. 160, pp. 199-206, 1993; IDS filed on 11/27/2023, Cite No. 2) in view of GenBank Accession No. AAA75009.1 (acid sphingomyelinase [Homo sapiens], NCBI, GenBank Accession No.: AAA75009.1, 1995; IDS filed on 11/27/2023, Cite No. 1) and Zhou et al. (Human acid sphingomyelinase structures provide insight to molecular basis of Niemann–Pick disease, Nat Commun, 7, 13082, 2016; IDS filed on 07/15/2026, Cite No. 22).
As fully described in the 102 rejection section, Rousson et al. teach a monoclonal anti-ASM protein antibody that binds human ASM protein. Rousson et al. do not teach the sequence of the human ASM protein.
GenBank Accession No. AAA75009.1 teaches the sequence of human ASM protein which encompasses SEQ ID NO: 66 (Pg. 1, sequence shown at bottom of page). However, GenBank Accession No. AAA75009.1 has 13 additional amino acids on the N-terminus compared to SEQ ID NO: 66; therefore, it does not teach human ASM consisting of SEQ ID NO: 66 (instant claim 11).
Zhou et al. teach structural features of human ASM protein (Pg. 3, Fig. 1f, shows location of functional domains), indicating N-terminal amino acids (e.g. the first 13 N-terminal amino acids of human ASM protein as taught by GenBank Accession No. AAA75009.1) of the human ASM protein are not a part of functional domains. Zhou et al. teach these N-terminal residues outside of the functional domains are not present in crystal structure (Pg. 3, Fig. 1c), indicating a high degree of disorder and flexibility. This teaching gives motivation for truncating the human ASM protein as the N-terminal amino acids are not required for function or folding.
Zhou et al. do not teach SEQ ID NO: 66.
The sequence of human ASM protein comprising SEQ ID NO: 66 was known and used prior to the effective filing date of the application. In addition, Rousson et al., GenBank Accession No. AAA75009.1, and Zhou et al. are in analogous arts (i.e. human ASM protein). Since Zhou et al. teach the N-terminal amino acids of the human ASM protein are not a part of functional domains or important for protein folding (including the first 13 N-terminal amino acids of human ASM protein as taught by GenBank Accession No. AAA75009.1), there is motivation for truncating the human ASM protein as this fragment is not responsible for function, arriving at the human ASM protein consisting of SEQ ID NO: 66.
MPEP § 2141(III)(G) states a rationale that may support a conclusion of obviousness includes “[s]ome 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.” MPEP § 2143(I)(G) states this rationale should explain why “[a] person of ordinary skill in the art would have been motivated to combine the prior art to achieve the claimed invention and whether there would have been a reasonable expectation of success in doing so." DyStar Textilfarben GmbH & Co. Deutschland KG v. C.H. Patrick Co., 464 F.3d 1356, 1360, 80 USPQ2d 1641, 1645 (Fed. Cir. 2006).
The teaching, suggestion, or motivation in the prior art (i.e. Zhou et al. teach the N-terminal amino acids of the human ASM protein are not a part of functional domains or important for protein folding, applicable to the first 13 N-terminal amino acids of human ASM protein as taught by GenBank Accession No. AAA75009.1) would have led one of ordinary skill to modify the prior art reference (i.e. truncating the human ASM protein as the first 13 N-terminal amino acids of said protein are not responsible for function, arriving at the human ASM protein consisting of SEQ ID NO: 66) to arrive at the claimed invention.
There is a reasonable expectation of success as the sequence of human ASM protein comprising SEQ ID NO: 66 was known and used prior to the effective filing date of the application. A person having ordinary skill in the art would understand truncating non-essential amino acids at the beginning of a protein sequence would not impact antibody binding, as long as the target protein remained folded and the epitope was retained. In addition, Rousson et al., GenBank Accession No. AAA75009.1, and Zhou et al. are in analogous arts (i.e. human ASM protein).
It would have been obvious to a person having ordinary skill in the art prior to the effective filing date of the instant application to truncate the human ASM protein as taught by GenBank Accession No. AAA75009.1 because this fragment is not responsible for function or protein folding as taught by Zhou et al., arriving at the human ASM protein consisting of SEQ ID NO: 66.
Claims 12-14, 17 and 19 are rejected under 35 U.S.C. 103 as being unpatentable over Rousson et al. (Preparation of an anti-acid sphingomyelinase monoclonal antibody for the quantitative determination and polypeptide analysis of lysosomal sphingomyelinase in fibroblasts from normal and Niemann-Pick type A patients, Journal of Immunological Methods, Vol. 160, pp. 199-206, 1993; IDS filed on 11/27/2023, Cite No. 2) in view of US 20190241662 A1 (published 2019-08-08; hereinafter referred to as US ‘662).
As fully described in the 102 rejection section, Rousson et al. teach a monoclonal anti-ASM protein antibody. Rousson et al. do not teach a nucleic acid encoding the antibody (instant claim 12), an expression vector comprising the nucleic acid (instant claim 13), a host cell comprising the nucleic acid (instant claim 14), a kit comprising the antibody (instant claim 17), and a host cell comprising the expression vector (instant claim 19).
US ‘662 teaches methods of making antibodies, specifically:
“an isolated nucleic acid molecule that comprises a nucleotide sequence encoding an amino acid sequence of a binding molecule (e.g., an antibody or activatable antibody)” (¶ 0243; instant claim 12);
“a vector that comprises a nucleic acid molecule… In some embodiments, the vector is an expression vector” (¶ 0251; instant claim 13);
“a host cell containing a nucleic acid molecule” (¶ 0256; instant claim 14);
“a kit comprising a binding molecule (e.g., an antibody or activatable antibody) and/or composition” (¶ 0280; instant claim 17); and
“the expression vector(s) encoding the heavy and light chains is transfected into a host cell” (¶ 0255; instant claim 19).
These teachings read on a nucleic acid encoding the antibody (instant claim 12), an expression vector comprising the nucleic acid (instant claim 13), a host cell comprising the nucleic acid (instant claim 14), a kit comprising the antibody (instant claim 17), and a host cell comprising the expression vector (instant claim 19).
US ’662 further teaches the encoding nucleic acid, expression vector, and host cell can be used “for expression of the antibody” (¶ 0258), giving motivation for utilizing these components US ‘662 further teaches the kit is used “for storing, transferring, administering, or otherwise using the binding molecule” (¶ 0280), giving motivation for packaging the antibody in a kit.
US ‘662 does not teach the monoclonal anti-ASM protein antibody.
Encoding nucleic acids, expression vectors, host cells, and kits of antibody were known and used prior to the effective filing date of the application. In addition, Rousson et al. and US ‘662 are in analogous arts (i.e. antibodies). Since US ‘662 teaches encoding nucleic acids, expression vectors, and host cells can be used for expression of antibodies and kits are useful for storing or transferring antibodies, there is motivation for applying these techniques suitable for antibodies in general to the anti-ASM protein antibody specifically.
MPEP § 2141(III)(G) states a rationale that may support a conclusion of obviousness includes “[s]ome 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.” MPEP § 2143(I)(G) states this rationale should explain why “[a] person of ordinary skill in the art would have been motivated to combine the prior art to achieve the claimed invention and whether there would have been a reasonable expectation of success in doing so." DyStar Textilfarben GmbH & Co. Deutschland KG v. C.H. Patrick Co., 464 F.3d 1356, 1360, 80 USPQ2d 1641, 1645 (Fed. Cir. 2006).
The teaching, suggestion, or motivation in the prior art (i.e. US ‘662 teaches encoding nucleic acids, expression vectors, and host cells can be used for expression of antibodies and kits are useful for storing or transferring antibodies) would have led one of ordinary skill to modify the prior art reference (i.e. applying the techniques suitable for antibodies in general as taught by US ‘662 to the anti-ASM protein antibody as taught by Rousson et al. specifically) to arrive at the claimed invention. There is a reasonable expectation of success as encoding nucleic acids, expression vectors, host cells, and kits of antibody were known and used prior to the effective filing date of the application. In addition, Rousson et al. and US ‘662 are in analogous arts (i.e. antibodies).
It would have been obvious to a person having ordinary skill in the art prior to the effective filing date of the instant application to applying the techniques suitable for antibodies in general as taught by US ‘662 to the anti-ASM protein antibody as taught by Rousson et al.
Double Patenting
A rejection based on double patenting of the “same invention” type finds its support in the language of 35 U.S.C. 101 which states that “whoever invents or discovers any new and useful process... may obtain a patent therefor...” (Emphasis added). Thus, the term “same invention,” in this context, means an invention drawn to identical subject matter. See Miller v. Eagle Mfg. Co., 151 U.S. 186 (1894); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Ockert, 245 F.2d 467, 114 USPQ 330 (CCPA 1957).
A statutory type (35 U.S.C. 101) double patenting rejection can be overcome by canceling or amending the claims that are directed to the same invention so they are no longer coextensive in scope. The filing of a terminal disclaimer cannot overcome a double patenting rejection based upon 35 U.S.C. 101.
Claim 1, 10, 12-14, and 19 is provisionally rejected under 35 U.S.C. 101 as claiming the same invention as that of claims 1-2 and 10-12 of copending Application No. 19/132,042 (reference application; hereinafter referred to as copending ‘042).
This is a provisional statutory double patenting rejection since the claims directed to the same invention have not in fact been patented.
Instant claim 1 and claim 1 of copending ‘042 have identical claim language and recite “An antibody or antigen-binding fragment thereof that specifically binds to an acid sphingomyelinase (ASM) protein” (instant claim 1, lines 1-2; claim 1 of copending ‘042, lines 1-3).
Instant claim 10 and claim 2 of copending ‘042 have identical claim language and recite “The antibody or antigen-binding fragment thereof of claim 1, wherein the ASM protein is derived from a mammal” (instant claim 10, lines 1-2; claim 2 of copending ‘042, lines 1-2).
Instant claim 12 and claim 10 of copending ‘042 have identical claim language and recite “A nucleic acid encoding the antibody or antigen-binding fragment thereof” (instant claim 12, line 1; claim 10 of copending ‘042, lines 1-2).
Instant claim 13 and claim 11 of copending ‘042 have identical claim language and recite “An expression vector comprising the nucleic acid” (instant claim 13, line 1; claim 11 of copending ‘042, line 1).
Instant claims 14 and 19 recite “A host cell comprising the nucleic acid” (instant claim 14, line 1) and “A host cell comprising the expression vector” (instant claim 19, line 1). This claim language is identical to claim 12 of copending ‘042 as it recites “A host cell comprising the nucleic acid… or the expression vector” (lines 1-2).
As instant claim 1, 10, 12-14, and 19 and claims 1-2 and 10-12 of copending ‘042 recite identical limitations as delineated above by the identical claim language, they are directed towards the same invention. Therefore, instant claim 1, 10, 12-14, and 19 are anticipated by claims 1-2 and 10-12 of copending ‘042.
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 4-9 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 3-9 of copending Application No. 19/132,042 (reference application; hereinafter referred to as copending ‘042). Although the claims at issue are not identical, they are not patentably distinct from each other.
Instant claims 4-9 explicitly teach or teach sequences encompassing instant SEQ ID NOs: 31-33 and 49-51 for the 6 CDRs of an anti-ASM protein antibody or antigen-binding fragment. Claim 3 of copending ‘042 teaches an anti-ASM protein antibody or antigen-binding fragment comprising SEQ ID NOs: 89-94 for the 6 CDRs, identical to instant SEQ ID NOs: 31-33 and 49-51 respectively. Claims 3-9 of copending ‘042 teach substitution of 2-5 “or fewer” amino acids in the CDRs; here, the identical sequences as taught in instant claims 4-9 meet those requirements.
As delineated above, claims 3-9 of copending ‘042 teach all limitations of instant claims 4-9 regarding an anti-ASM protein antibody or antigen-binding fragment, rendering the instant claims obvious.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 1-11 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 18-22 of copending Application No. 18/564,378 (reference application; hereinafter referred to as copending ‘378). Although the claims at issue are not identical, they are not patentably distinct from each other.
Instant claim 1 teaches an anti-ASM protein antibody or antigen-binding fragment. Instant claim 2 teaches the anti-ASM protein antibody or antigen-binding fragment binds at least one epitope of the ASM protein, reciting specific amino acid fragments for said epitopes. Instant claim 3 teaches the anti-ASM protein antibody or antigen-binding fragment binds at least one epitope of the ASM protein selected from SEQ ID NOs: 68-73. Instant claims 4-9 explicitly teach or teach sequences encompassing instant SEQ ID NOs: 31-33 and 49-51 for the 6 CDRs of the anti-ASM protein antibody or antigen-binding fragment. Instant claim 10 teaches the ASM protein is derived from a mammal. Instant claim 11 teaches the ASM protein consists of SEQ ID NO: 66 or 67.
Claim 18 of copending ‘378 teaches an anti-ASM protein antibody or antigen-binding fragment (instant claim 1) comprising SEQ ID NOs: 31-33 and 49-51 for the 6 CDRs, identical to instant SEQ ID NOs: 31-33 and 49-51 respectively (instant claims 4-9), in a method of treating a brain disease. Claim 19 of copending ‘378 teaches the anti-ASM protein antibody or antigen-binding fragment binds at least one epitope of the ASM protein, wherein the epitopes are identical to those of instant claim 2. Claim 20 of copending ‘378 teaches the anti-ASM protein antibody or antigen-binding fragment binds at least one epitope of the ASM protein selected from SEQ ID NOs: 68-73, which are identical to instant SEQ ID NOs: 68-73 (instant claim 3). Claim 21 of copending ‘378 teaches the ASM protein is derived from a mammal (instant claim 10). Claim 22 of copending ‘378 teaches the ASM protein consists of SEQ ID NO: 66 or 67 (instant claim 11).
As delineated above, claims 18-22 of copending ‘378 teach all limitations of instant claims 1-11 regarding an anti-ASM protein antibody or antigen-binding fragment, rendering the instant claims obvious. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Art-Free Subject Matter
All species of instant claims 2-3 and 9 were searched, not just the elected species (see Election/Restriction section for more information), as the elected species did not have prior art.
The closest prior art to instant claims 2-3 and 9 is Rousson et al. (Preparation of an anti-acid sphingomyelinase monoclonal antibody for the quantitative determination and polypeptide analysis of lysosomal sphingomyelinase in fibroblasts from normal and Niemann-Pick type A patients, Journal of Immunological Methods, Vol. 160, pp. 199-206, 1993; IDS filed on 11/27/2023, Cite No. 2).
As fully described in the 102 rejection section, Rousson et al. teach a monoclonal anti-ASM protein antibody that binds human ASM protein and its use in detecting human ASM protein. However, Rousson et al. do not teach the epitopes of the antibody as recited in instant claims 2-3 nor the instant SEQ ID NOs comprising said antibody as recited in instant claim 9. It is noted that instant SEQ ID NOs of instant claim 9 were thoroughly searched corresponding to the limitations of the claims and are free of prior art.
Therefore, instant claims 2-3 and 9 are not anticipated by Rousson et al. because the prior art fails to disclose each and every element of the claimed invention. In addition, instant claims 2-3 and 9 are not rendered obvious by Rousson et al. While Rousson et al. teach a monoclonal anti-ASM protein antibody, the prior art does not provide a teaching, suggestion, or motivation to modify the sequences of said antibody to arrive at the claimed invention.
Conclusion
Claims 1-14, 16-17, and 19 are currently under consideration for patentability. Claims 5 and 7 are objected to. Claims 1-14, 16-17, and 19 are rejected. No claims are allowed.
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/J.M.P./Examiner, Art Unit 1642
/SAMIRA J JEAN-LOUIS/ Supervisory Patent Examiner, Art Unit 1642
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