DETAILED ACTION
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Claims 1-24, 31, 32, and 42-50 are pending.
Claims 1 and 42 are independent.
Applicant’s election without traverse of the invention of group I, drawn to anti-glycan antibodies, and the antibody species being those comprising the six CDRs of SEQ ID NOs:1-6 in the reply filed on December 9, 2025 is acknowledged.
Claims 17-21, 32, 42-50 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected inventions, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on December 9, 2025.
Claims 1-16, 22-24, and 31 are under examination as they read upon antibodies that bind the 6-sulfosialyl Lewis X glycan antigen and comprise the six CDRs of SEQ ID NOs:1-6. It should be noted that the species comprising SEQ ID NOs:1-6 is free of the prior art and thus the species search as extended and stopped upon finding art that encompasses more generic embodiments.
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 specification are not identified by sequence identifiers in accordance with 37 CFR 1.821(d). See paragraph [0139] of the instant specification.
Required response – Applicant must provide:
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required sequence identifiers, 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.
It should be noted that paragraph [0139] recites biological linker sequences in the absence of an accompanying SEQ ID number, which is not permitted. It should also be noted that these sequences are present in the sequence listing as subsequences within the longer single chain Fv constructs of SEQ ID NOs:21-24, while the HIS tag in particular does not appear to be disclosed as a separate sequence in the sequence listing as originally filed. Appropriate correction to correct this clerical error is required.
Information Disclosure Statement
The IDS forms received 4/5/2023 and 11/8/2024 are acknowledge and the references cited therein have been considered.
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 1-16, 22-24, and 31 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.
Applicant has broadly claimed antibodies or antigen binding fragments thereof that bind importance in lymphocyte homing. The broadest claims appear to define such antibodies by CDR sequence, but close inspection of the independent claim reveals that such antibodies need only have “at least one” CDR from a list of six, and further that the CDR which is present need only be “80% or more” identical to the recited SEQ ID number or the CDR comprises deletion, substitution, or addition of one or several amino acids as compared the CDR sequence defined by SEQ ID number, with the maximum number of changes permitted by “several” being defined in the specification as being 2 to 10 (see the last sentence of paragraph [0035] on page 26 of the 4/5/2023 specification). It should be noted that of the six CDR sequences defined by SEQ ID number in claim1, only SEQ ID NO:3 which has a length of 11 residues is longer than the 10 changes permitted by “several”. Dependent claims fix the sequence of some CDRs while still allowing for mutations in other CDRs (see for example claim 2) or recite VH and VL domains recited by SEQ ID number which also are typically allowed to comprise mutations via recited percent identity limitations (see for example claims 4 and 8). To support such claims, the working examples disclose the synthesis of the SF1 antibody via hybridoma technology which when sequenced was found to have the six CDR sequences of SEQ ID NOs1-6, VH or SEQ ID NO:13 and a VL of SEQ ID NO:14 (see also Figures 8 and 9). Notably, while the specification discloses making humanized variants of the starting mouse SF1 antibody, such humanized variants do not comprise any CDR mutations (see for example Figure 21).
The guidelines for the Examination of Patent Applications Under the 35 U.S.C. 112, § 1 "Written Description" Requirement make clear that if a claimed genus does not show actual reduction to practice for a representative number of species, then the Requirement may be alternatively met by reduction to drawings, 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 genus. See MPEP 2163. In The Regents of the University of California v. Eli Lilly (43 USPQ2d 1398-1412) 19 F. 3d 1559, the court held that disclosure of a single member of a genus (rat insulin) did not provide adequate written support for the claimed genus (all mammalian insulins). In this same case, the court also noted: “A definition by function, as we have previously indicated, does not suffice to define the genus because it is only an indication of what the gene does, rather than what it is. See Fiers, 984 F.2d at 1169-71, 25 USPQ2d at 1605-06 (discussing Amgen). It is only a definition of a useful result rather than a definition of what achieves that result. Many such genes may achieve that result. The description requirement of the patent statute requires a description of an invention, not an indication of a result that one might achieve if one made that invention. See In re Wilder, 736 F.2d 1516, 1521, 222 USPQ 369, 372-73 (Fed. Cir. 1984) (affirming rejection because the specification does “little more than outlin [e] goals appellants hope the claimed invention achieves and the problems the invention will hopefully ameliorate."). Accordingly, naming a type of material generally known to exist, in the absence of knowledge as to what that material consists of, is not a description of that material.” The court has further stated that “Adequate written description requires a precise definition, such as by structure, formula, chemical name or physical properties, not a mere wish or plan for obtaining the claimed chemical invention.” Id. at 1566, 43 USPQ2d at 1404 (quoting Fiers, 984 F.2d at 1171, 25 USPQ2d at 1606). Also see Enzo-Biochem v. Gen-Probe 01-1230 (CAFC 2002). Recent court cases have emphasized the need for correlation between a well-defined structure and recited functional limitations. For example, the courts have indicated that recitation of an antibody which has specific functional properties in the absence of knowledge of the antibody sequences that give rise to said functional properties do not satisfy the requirements for written description. See for example AbbVie Deutschland GmbH v. Janssen Biotech. Inc. 759 F.3d 1285 (Fed. Cir. 2014). Such cases have indicated that that it is improper to allow patentees to claim antibodies by describing something that is not the invention, i.e. the antigen, as knowledge of the chemical structure of an antigen does not provide information as to what an antibody binding that antigen necessarily looks like (i.e. the primary amino acid structure of the antibody). Applicant is reminded that the courts have long ruled that “Possession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features.” See University of Rochester, 358 F.3d at 927, 69 USPQ2d at 1895. As such, disclosure of a screening assay to test for functional properties of an antibody (such as its ability to bind 6-sulosialyl Lewis X) does not provide evidence of possession of the antibody itself. Further, courts have long ruled that “When a patent claims a genus using functional language to define a desired result, the specification must demonstrate that the applicant has made a generic invention that achieves the claimed result and do so by showing that the applicant has invented species sufficient to support a claim to the functionally-defined genus.” See Capon v. Eshhar, 418 F.3d 1349 (Fed. Cir. 2005). Also, “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.” See AbbVie, 759 F.3d at 1297, reiterating Eli Lilly, 119 F.3d at 1568-69.
It should be pointed out that it is well established in the art that the formation of an intact antigen-binding site requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three different complementarity determining regions, CDR1, 2 and 3, which provide the majority of the contact residues for the binding of the antibody to its target epitope. The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin (Janeway et al., see entire selection). It is also known that single amino acid changes in a CDR can abrogate the antigen binding function of an antibody (see for example Rudikoff et al. and Winkler et al.). Thus, based upon the prior art, skilled artisans would reasonably understand that it is the structure of the CDRs within an antibody which gives rise to the functional property of antigen binding, the epitope to which said CDRs bind is an inherent property which appears to necessarily be present due to conservation of critical structural elements, namely the CDR sequences themselves.
Artisans are well aware that knowledge of a given antigen (for instance 6-sulosialyl Lewis X) provides no information concerning the sequence/structure of antibodies that bind the given antigen. For example, Edwards et al. teach that over 1,000 different antibodies to a single protein can be generated, all with different sequences spanning almost the entire heavy and light chain germline repertoire (42/49 functional heavy chain germlines and 33 of 70 V-lambda and V-kappa light chain germlines, and with extensive diversity in the HCDR3 region sequences (that are generated by VDJ germline segment recombination) as well, see entire document). Similarly, Lloyd et al. teach that a large majority of VH/VL germline gene segments are used in the antibody response to an antigen, even when the antibodies were selected by antigen binding, as their sequencing studies revealed that out of 841 unselected and 5,044 selected antibodies, all but one of the 49 functional VH gene segments was observed (see entire document). Goel et al. disclose the synthesis of three mAbs that bind to the same short (12-mer) peptide and found that the sequences of these antibodies which bound the same epitope exhibited diverse V gene usage indicating their independent germline origin (see entire document). Further, it should be noted that degenerate binding of the same structural motif by antibodies does not require the existence of sequence homology or identity at any of their CDRs or other chemical similarities at the antigen-binding sites; side chain mobility of epitope residues can confer steric and electrostatic complementarity to differently shaped combining sites, allowing functional mimicry to occur (Lescar et al., see entire document, in particular Abstract and Discussion). As such, it does not seem possible to predict the sequence/structure of an antibody that binds a given antigen as there does not appear to be any common or core structure present within all antibodies that gives rise to the function of antigen binding. Further, given data such as that of Edwards et al. indicating the diversity of sequence bound in a population of antibodies that bind to a given antigen, no number of species appears to reasonably representative of the breadth of the genus of antibodies that bind the given antigen. Indeed, Kanyavuz et al. teach that “Theoretically, under physiological conditions, the human immune system can generate BCRs with 1026 distinct sequences, an astronomical number that is far greater than the calculated number of all B cell clones that can be generated during the lifespan of a healthy human (estimated to be 4 × 1014).
As discussed above, applicant made the progenitor SF1 antibody via immunization of a mouse and standard hybridoma technology, with the hybridoma being sequenced prior to humanization. Indeed, applicant’s own humanization working examples took the unmutated CDR sequences of the SF1 clone and placed them into various human frameworks to make humanized variants thereby providing even more evidence of the correlation between CDR structure (sequence) and the function of antigen binding. However, the present claims explicitly seek to alter the very structure known in the art and confirmed by the humanization working examples of the instant specification as being critical for providing antigen binding activity. While applicant has claimed antibodies where only one CDR (or less) worth of sequence needs to be maintained relative to SF1 yet the required antigen binding function is maintained, it is clear that such a level of structure is insufficient for functional activity as demonstrated by White et al. who disclose an antibody which comprises a CDR 100% identical to instant SEQ ID NO:1 yet binds an antigen completely unrelated to 6-sulfosialyl Lewis X (US 2016/0244521, see entire document as well as the enclosed sequence alignments). Thus, the art recognizes that for antigen binding to be maintained, six complete CDR sequences in their proper three-dimensional arrangement (i.e. interspersed with appropriate framework residues such as would be found in an antibody rather than say a fusion protein wherein SEQ ID NOs:1-6 are joined head to tail with no intervening sequence) and applicant has not supplied any data demonstrating that less than this level of structural information is needed to maintain antigen binding activity. It should be noted that many dependent claims recite variable domains by SEQ ID number, but such sequences are either accompanied by percent identity language or encompass truncations such that the sequence of all six CDRs within the claimed antibodies are not fixed.
Therefore, in view of the breadth of the claims artisans would reasonably conclude that while applicant was in possession of antibodies that comprise the six CDRs of the lead SF1 clone (i.e. SEQ ID NOs:1-6) as set forth in the working examples, such an artisans reasonably would also conclude that applicant was not in possession of the full breadth of anti-6-sulfosialyl Lewis X antibodies comprising mutations to the CDR sequences of SEQ ID NOs:1-6 as presently recited at the time the instant application was filed. Amendment of the claims to minimally require that the claimed antibodies comprise the six fully defined CDRs of SEQ ID NOs:1-6 known to collectively be capable of binding 6-sulfosialyl Lewis X glycan when present in an antibody is one possible approach to obviating the issues discussed above.
Claims 1-16, 22-24, and 31 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 enablement requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention.
Applicant has claimed a genus of antibodies that bind the carbohydrate antigen 6-sulfosialyl Lewis X which is often expressed on high endothelial venules and is involved in lymphocyte homing. Such antibodies initially appear to be defined by SEQ ID number for the six CDRs, but a close reading of the independent claim reveals that in reality what is required is a single CDR sequence which has “several” deletions, substitutions, or additions relative to a recited SEQ ID number wherein the specification defines “several” as being 2-10 as per paragraph [0035] spanning pages 25 and 26 of the instant specification. Dependent claims add additional sequence requirements, such as 80% identity to a recited variable domain, but all claims as presently constructed allow for multiple simultaneous changes to the CDR sequences. The specification discloses that applicant made antibodies that bind 6-sulfosialyl Lewis X via immunization of a mouse and recovery of the SF1 lead clone using conventional hybridoma technology (see particularly example 1 beginning on page 43). SF1 was sequenced (see particularly Figures 7-9 as well as example 5), and its CDR sequences were grafted into homologous human frameworks to produce humanized variants of SF1, and it should be pointed out that no changes to the CDR sequences were made as part of the humanization process (see examples 13-14 as well as Figures 22, 24, and 25).
Artisans have long made antibodies via immunization of animals and recovery of clones via hybridoma technology and indeed this is what applicant has done in the working examples to generate the SF1 lead antibody clone. While immunization and hybridoma recovery is quite common, it does not allow artisans any control over the sequence of the recovered antibody. Indeed, replication of the protocol disclosed by applicant to generate the SF1 antibody would almost certainly yield antibodies of wildly different sequence. For example, Edwards et al. teach that over 1,000 different antibodies to a single protein can be generated, all with different sequences spanning almost the entire heavy and light chain germline repertoire (42/49 functional heavy chain germlines and 33 of 70 V-lambda and V-kappa light chain germlines, and with extensive diversity in the HCDR3 region sequences (that are generated by VDJ germline segment recombination) as well, see entire document). Similarly, Lloyd et al. teach that a large majority of VH/VL germline gene segments are used in the antibody response to an antigen, even when the antibodies were selected by antigen binding, as their sequencing studies revealed that out of 841 unselected and 5,044 selected antibodies, all but one of the 49 functional VH gene segments was observed (see entire document). Goel et al. disclose the synthesis of three mAbs that bind to the same short (12-mer) peptide and found that the sequences of these antibodies which bound the same epitope exhibited diverse V gene usage indicating their independent germline origin (see entire document). Thus, repeating the protocols of example 1 of the instant specification is astronomically unlikely to necessarily yield an antibody comprising the six CDRs of SF1 (i.e. SEQ ID NOs:1-6) let alone the entire VH and VL sequences of SF1 (SEQ ID NOs:13 and 14 respectively). Therefore, reproducing applicant’s immunization protocol is unlikely to yield a product that comprises the biological sequences recited in the instant claims.
Given that the claimed products are recited by way of reference to SEQ ID numbers (and thus predetermined and defined biological sequences) artisans would reasonably turn to the tools and techniques of recombinant molecular biology. Recombinant production of antibodies is quite routine in the art, with six CDRs typically being the minimum amount of specific antibody sequence needed by an artisan to recapitulate the desired antigen binding specificity as evidence by the ubiquity of the techniques of antibody humanization which start with six defined CDR sequences (see for example Kipriyanov as well as the working examples of the instant specification discussed above). As such, artisans could readily make and use antibodies which comprise all six CDRs of SEQ ID NOs:1-6. However, close inspection reveals that while antibodies comprising all of SEQ ID NOs:1-6 are encompassed, the actual breadth of the claims is significantly broader such that the claimed antibody essentially has no CDR sequence in common with SEQ ID NOs:1-6. This is because of the recitation of “or comprises at least one or more CDRs, each comprising an amino acid sequence having deletion, substitution, or addition of one or several amino acids in the amino acid sequence of the corresponding CDR” in independent claim 1. Note that as per paragraph [0035] “several” means 2-10 and SEQ ID NOs:1-3, 5 and 6 are all shorter than 10 residues while SEQ ID NO:4 is 11 residues in length. Thus an antibody comprising a CDR that “corresponds” to a recited SEQ ID number but which also comprises “several” mutations effectively has 0% identity with the SEQ ID number in question. The claims also recite alternative embodiments having 80% identity for CDRs, but such percent identity limitations a) need only apply to a single (rather than all six) CDR and b) any changes are random both in the identity and internal location relative to the reference CDR sequence. It is known in the art that even single amino acid changes in a CDR can abrogate the antigen binding function of an antibody (see for example Rudikoff et al. and Winkler et al.) and applicant has provided no guidance or direction concerning CDR mutagenesis, such as in the form of working examples wherein SEQ ID NOs:1-6 were mutated and shown to still provide antigen binding activity. As such it appears that artisans would need to engage in additional unpredictable trial and error basic research and experimentation prior to being able to make and use the full extent of applicant’s antibody products as presently claimed.
Therefore, in view of the breadth of the claimed inventions, the guidance and direction of the working examples and the teachings of the prior art, artisans would not be able to make and use that which has been presently claimed without first performing additional unpredictable research and experimentation. Amendment of the claims to minimally require the six CDRs of SEQ ID NOs:1-6 in all embodiments is likely to significantly advance prosecution and obviate this rejection.
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, 16, and 22 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Uchimura et al. (EP 1726654).
Uchimura et al. disclose and claim antibodies that bind to 6-sulfated sialyl Lewis X but do not bind 6’-sulfated sialyl Lewis X, 6,6’-bis-sulfated sialyl Lewis X, and 6-sulfated Lewis X, and Lewis X (see entire document, particularly the abstract, pages 12-13 and the claims). It is noted that such antibodies are not disclosed by Uchimura as comprising the six CDRs of SEQ ID NOs:1-6 of the instant application. However, as presently recited and as discussed at greater length earlier in this office action in conjunction with 35 USC 112 rejections, the breadth of antibody products encompassed by the instant claims includes those having only one CDR corresponding to SEQ ID NOs:1-6 wherein such CDRs can comprise “several” mutations with the specification indicating that “several” means between 2 and 10. Given that all of SEQ ID NOs:1-6 apart from the CDRL1 of SEQ ID NO:4 are less than 10 residues in length, “at least one CDR encompassing several mutations” reads upon sequences of 0% identity with the CDR sequences recited by SEQ ID number in claim 1 for all heavy chain CDRs and CDRs 2 and 3 of the light chain.
It is further noted that Uchimura et al. do not disclose any dissociation constants for the strength of interaction between their antibodies and the 6-sulfated sialyl Lewis X antigen. However, as per MPEP 2112.01, “"Products of identical chemical composition can not have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present. Id.” Given that as discussed above the antibodies disclosed by Uchimura et al. comprise the same amount of structure as that required by the independent claim and claim 16 recites no additional structural limitations, the antibodies of Uchimura et al. necessarily have the requisite recited binding affinities as there is no difference in structure. Similarly, the “homing inhibitor” claimed in claim 22 is simply the antibody of claim 1, and as discussed above the antibodies disclosed by Uchimura meet the structural and functional limitations of claim 1.
In view of all of the above the anti-6-sulfated sialyl Lewis X antibodies of Uchimura et al. meet the instant claim limitations.
Claims 1, 10, 16, and 22 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Mitsuoka et al. (of record on the 11/4/2025 form 892).
Mitsuoka et al. disclose antibodies G152 and G72 that bind to 6-sulfated sialyl Lewis X (see entire document, particularly the abstract). It is noted that such antibodies are not disclosed by Mitsuoka et al. as comprising the six CDRs of SEQ ID NOs:1-6 of the instant application. However, as presently recited and as discussed at greater length earlier in this office action in conjunction with 35 USC 112 rejections, the breadth of antibody products encompassed by the instant claims includes those having only one CDR corresponding to SEQ ID NOs:1-6 wherein such CDRs can comprise “several” mutations with the specification indicating that “several” means between 2 and 10. Given that all of SEQ ID NOs:1-6 apart from the CDRL1 of SEQ ID NO:4 are less than 10 residues in length, “at least one CDR encompassing several mutations” reads upon sequences of 0% identity with the CDR sequences recited by SEQ ID number in claim 1 for all heavy chain CDRs and CDRs 2 and 3 of the light chain.
It is further noted that Mitsuoka et al. do not disclose any dissociation constants for the strength of interaction between their antibodies and the 6-sulfated sialyl Lewis X antigen. However, as per MPEP 2112.01, “"Products of identical chemical composition can not have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present. Id.” Given that as discussed above the antibodies disclosed by Mitsuoka et al. comprise the same amount of structure as that required by the independent claim and claim 16 recites no additional structural limitations, the antibodies of Mitsuoka et al. necessarily have the requisite recited binding affinities as there is no difference in structure. Similarly, the “homing inhibitor” claimed in claim 22 is simply the antibody of claim 1, and as discussed above the antibodies disclosed by Mitsuoka meet the structural and functional limitations of claim 1.
In view of all of the above the anti-6-sulfated sialyl Lewis X antibodies of Mitsuoka et al. meet the instant claim limitations.
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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 23 and 24 are rejected under 35 U.S.C. 103 as being unpatentable over Uchimura et al. (EP 1726654) and/or Mitsuoka et al. (of record on the 11/4/2025 form 892), in view of Streeter et al. (Reference A3 on the 4/5/2023 IDS).
The teachings of Uchimura et al. and/or Mitsuoka have been discussed above and differ from that which is presently claimed in that neither group explicitly discloses that their anti-6-sulfosialyl Lewis X are present in pharmaceutical compositions for in vivo use.
Streeter et al. disclose the synthesis of MECA-79, and antibody that binds 6-sulfosialyl Lewis X (see particularly the admission by applicant in paragraph [0007] of the instant specification) and its administration as part of a pharmaceutical composition to mice (see entire document, particularly the left column of page 1855, most particularly the section titled “In Vivo Lymphocyte Homing Assay”).
Therefore, it would have been obvious to persons or ordinary skill in the art at the time of filing to place the antibodies of Uchimura et al. and/or Mitsuoka et al. into pharmaceutical compositions in order to gain the advantage of being able to use such antibodies for in vivo purposes such as the assays disclosed by Streeter et al. Artisans would have a more than reasonable expectation of success in doing so as placing antibodies in pharmaceutical compositions is quite routine in the art as can readily be seen in the working examples of Streeter et al.
No claims are allowable.
It should be noted that antibodies that comprise all six CDRs of SEQ ID NOs:1-6 are free of the prior art, and that all claims presently are broader in scope than this.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Michael Szperka whose telephone number is (571)272-2934. The examiner can normally be reached Monday-Friday 8:30-5:00.
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Michael Szperka
Primary Examiner
Art Unit 1641
/MICHAEL SZPERKA/Primary Examiner, Art Unit 1641