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 .
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.
Priority
Acknowledgment is made of the present application as a proper National Stage (371) entry of PCT Application No. PCT/IB2021/056284, filed 07/13/2021, which claims benefit under 35 U.S.C. 119(e) to provisional application No. 63/041,323, filed 07/13/2020.
Status of the Claims
Claims 1, 3, 5, 16-17, 19, 21-23, 25, 27-30 and 33-38 are pending; claims 1, 3, 5, 16-17, 21, 23, 29-30 are amended; claims 2, 4, 6-15, 18, 20, 24, 26 and 31-32 are canceled; no claims are withdrawn. As such, claims 1, 3, 5, 16-17, 19, 21-23, 25, 27-30 and 33-38 are examined below.
Withdrawn Objections/Rejections
The previous objection to the specification (regarding the abstract) is withdrawn in response to Applicant’s amendments to the abstract.
The previous rejection of claim 30 under 35 U.S.C. 102 is withdrawn in response to Applicant’s amendments to the claim.
Specification
The substitute specification filed 11/13/2025 has not been entered because it does not conform to 37 CFR 1.125(b) and (c) because: See specifically, 37 CFR. 1.125(c): A substitute specification submitted under this section must be submitted with markings showing all the changes relative to the immediate prior version of the specification of record. The text of any added subject matter must be shown by underlining the added text. The text of any deleted matter must be shown by strike-through except that double brackets placed before and after the deleted characters may be used to show deletion of five or fewer consecutive characters. The text of any deleted subject matter must be shown by being placed within double brackets if strike-through cannot be easily perceived. An accompanying clean version (without markings) must also be supplied. Numbering the paragraphs of the specification of record is not considered a change that must be shown pursuant to this paragraph.
In the present case, regarding the marked up version of the substitution specification, while some changes are shown (see page 1, showing text that is shown with strike-through), not all changes made relative to the prior version are marked up. For example, text added at page 1 and Table 5 is not shown as lined through. The added text referenced presently, as well as any other changes made by Applicant must be made with markings to show all the changes.
Nucleotide and/or Amino Acid Sequence Disclosures
Specific deficiency - This application fails to comply with the requirements of 37 CFR 1.821 - 1.825 because it does not contain a "Sequence Listing" as a separate part of the disclosure and the CRF of the “Sequence Listing” is defective.
Required response - Applicant must provide:
A "Sequence Listing" part of the disclosure, as described above in item 1); together with
An amendment specifically directing its entry into the application in accordance with 37 CFR 1.825(a)(2);
A statement that the "Sequence Listing" includes no new matter as required by 37 CFR 1.825(a)(4); and
A statement that indicates support for the amendment in the application, as filed, as required by 37 CFR 1.825(a)(3)
If the "Sequence Listing" part of the disclosure is submitted according to item 1) a) or b) above, Applicant must also provide:
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required incorporation-by-reference paragraph, 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.
If the "Sequence Listing" part of the disclosure is submitted according to item 1) c) or d) above, Applicant must also provide:
A CRF in accordance with 37 CFR 1.821(e)(1) or 1.821(e)(2) as required by 37 CFR 1.825(a)(5); and
A statement according to item 2) a) or b) above.
See as indicated 11/17/2025, the sequence listing in computer readable format filed by Applicant 11/13/2025 in response to the previously indicated sequence compliance issues, was indicated to be defective because the application was submitted in a US national phase application with an international filing date of 07/13/2021, as such the listing filed in ST.26 format should have been submitted in ST.25 format.
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, 3, 5, 16-17, 19, 21-23, 25 and 27-30 and 33-38 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.
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. These include: (1) Actual reduction to practice, (2) Disclosure of drawings or structural chemical formulas, (3) Sufficient relevant identifying characteristics (such as: i. Complete structure, ii. Partial structure, iii. Physical and/or chemical properties, iv. Functional characteristics when coupled with a known or disclosed, and correlation between function and structure), (4) Method of making the claimed invention, (5) Level of skill and knowledge in the art, and (6) Predictability in the art. See MPEP 2163.
Independent claim 1 is directed to an anti-HIV-1 antibody or fragment thereof comprising a light chain comprising 3 CDRs (L-CDR1, L-CDR2, L-CDR3) and a heavy chain comprising 3 CDRs (H-CDR1, H-CDR2, H-CDR3), each CDR is one of 3 sequences.
L-CDR1, the sequence consists of any of SEQ ID NOs. 15, 18 or 21, or “a sequence that differs” from anyone of these claimed sequences by one or two substitutions, deletions or additions.
L-CDR2, the sequence consists of any of SEQ ID NOs. 16, 19 or 22, or “a sequence that differs” from anyone these claimed sequences by one or two substitution, deletions or additions.
L-CDR3, the sequence consists of any of SEQ ID Nos. 17, 20 or 23, or “a sequence that differs” from anyone of these claimed sequences by one or two substitutions, deletions or additions.
H-CDR1, the sequence consists of SEQ ID NOs. 24, 27 or 30, or “a sequence that differs” from anyone of these claimed sequences by one or two substitutions, deletions or additions”.
H-CDR2, the sequence consists of SEQ ID NOs. 25, 28 or 31, or “a sequence that differs” from anyone of these claimed sequences by one or two substitutions, deletions or additions.
H-CDR3, the sequence consists of SEQ ID NOs. 26, 29 or 32, or “a sequence that differs” from anyone of these claimed sequences by one or two substitutions, deletions or additions”.
The claims indicated above encompass 6 genera of CDR sequences that must possess certain desired functional characteristics, namely must bind HIV-1 antigen (see at the preamble, the claims are directed to “an anti-HIV-1 antibody or fragment thereof, so must exhibit certain functional requirements) and that may be characterized by substantial variability (differs…by one or two substitutions, deletions or additions, the claims failing to specify which residues must be retained to achieve the required function). For example, the differing sequences are not limited to any particular or distinct sequences (in terms of the one or two substitutions, deletions or additions).
The originally filed specification indicates, regarding the substitutions, deletions or additions are understood to “arise at any amino acid of the range of amino acids defined by CDR X” (page 2). See for example, the specification indicates, “As a non-limiting illustration, L-CDR1 for Antibody #A can be defined as comprising the sequence of amino acids (1)-(11), RASQDISNYLH [as outlined in SEQ ID NO: 15]. Each of positions1, 2, 3, 4, 5, 6, 7, 8, 9, 10, and 11 is to be considered suitable for a substitution, deletion, or addition unless otherwise specified or later refined by amendment.”.
See further claims 3 and 5 reference sequences for the variable region of the heavy chain and light chain, reciting that the sequence has “about 90% homology with the amino acid sequences”, SEQ ID Nos. 7, 8 or 9 for the light chain and SEQ ID Nos. 10, 11, 12 for the heavy chain.
Similarly, as with the genera for each recited CDR, the claims are directed to potential large and variable genera for each of the variable regions for the heavy and light chain sequences, each required to retain the functional requirements of the claim (serve as anti-HIV-1 antibody), the claims lacking any particular identified residues required to be maintained/retained to achieve binding.
Only those sequences meeting the structural and functional requirements of each of the claimed genera are encompassed by the claims. Therefore, the claims encompasses all of the sequences meeting the structural requirements that are also anti-HIV-1 antibodies. Although with the aid of a computer it may be possible to determine the amino acid sequences of the proteins that meet the structural requirements of the claim (i.e. one or two substitutions, deletions or additions relative to the claimed sequences, or sharing 90% homology with the claimed sequences), it is not readily apparent from the claims or the specification which of these sequences are anti-HIV-1 antibodies (bind HIV-1).
Therefore, to meet the written description requirement of 35 U.S.C. § 112(a), the specification must disclose a representative number of species that meet both the structural and functional limitations of the genus or the specification and/or the prior art must identify the structural elements that correlate to the claimed function in a manner that demonstrates to one of ordinary skill in the art that Applicant was in possession of the claimed genus at the time the application was filed. In the instant case, the specification and/or the prior art must establish which of the enormous number of protein sequences that satisfy the structural limitations of the claim are also capable of the recited function (bind HIV-1/serve as an anti-HIV-1 antibody).
As noted previously above, regarding the claimed CDRs, the specification indicates any of the residues in the CDR sequences claimed can be subject to change in terms of substitution, deletion or addition.
The specification refers to 3 specific examples of antibodies at Example 1 referred to as antibodies A, B and D (light and heavy chain sequences provided at Table 1). Applicant references that expression of 3 constructs containing nucleotide sequences for each were generated in a vector containing the heavy and light chain of each antibody, and the antibodies were expressed using CHO cells (Tables 2-3 describing production and purification for each). Antibody clones were obtained for each best banked pool cell lines for antibodies A, B and D.
At Example 2, Applicant indicates a 3D structure model of antibodies A, B and D was built by antibody homology using computation and modeling software, sequences of each of antibodies A, B and D loaded into the software, framework regions and CDRs identified through searching the structures in PDB and selecting a PDB template based on high sequence similarly and structural fitness (Table 5 showing the predicted CDR sequences for the antibodies claimed).
The specification (page 39) indicates, for A, the PDB structure code used for the homology query is 2XKN, for antibody B, 5OPY was used, and for antibody D, 1F3D was used. 2XKN corresponds to the crystal structure for the Fab fragment of the anti-EGFR antibody 7A7, 5OPY corresponds to the crystal structure for anti-alphaVbeta 3 integrin Fab, and 1F3D corresponds to catalytic antibody 4B2 in complex with its amidinium hapten.
2XKN is shown in PDB to meet the structural requirements of the claim (for example claim 1), however is reported as an anti-EGFR antibody. It is not readily predictable whether or not this anti-EGFR antibody fragment would be capable of the claimed required function of binding HIV-1. Therefore, although the specification suggests any positions can be substituted, added, deleted, it is the case that at the least the changes that correspond to 2XKN don’t support the functional requirements (as 2XKN is an anti-EGFR antibody).
At Example 3 the specification describe epitope mapping for mAb D only, using HIV-p24 peptide microarrays containing 232 different linear peptides printed in duplicate (464 spots) framed by additional HA (38 spots) and c-Myc (38 spots) control peptides. Applicant reports for mAb D, epitope mapping against HIV-p24 highlighted a conserved 7 residue motif (SEQ ID NO. 33). Further at Example 4 (page 41), Applicant’s specification supports that molecular docking and western blot evaluation of antibodies A, B and D suggested recognition of linear epitopes at regions 1, 4 and 7 of HIV-1 p24 protein, Applicant performing tandem epitope binning assay to confirm (using Biolayer interferometry). It is noted however, the specification does not clearly identify what portions/structures are those that Applicant refers to as regions 1, 4 and 7. The originally filed specification reports that the results showed that when antibody A binds, antibodies B and D add an increase in signal response, demonstrating that B and D bind to distinct epitopes when compared to antibody A, and that similarly, when A and D are used as suturing antibodies, the remainder do not show competition for epitopes. However, see as indicated above, regarding epitope mapping, only mapping was reported for antibody D (as binding SEQ ID NO. 33). Applicant’s reported results appear to suggest each of Antibodies A, B and D binding different epitopes, it reported that D binds SEQ ID NO. 33.
Examples 5 and demonstrate affinity results of antibodies A, B and D compared to a commercial antibody, as well as binding capacity, however the Examples fails to identify what commercial antibody the claimed antibodies are being compared to.
None of these examples indicate any particular necessarily retained structural features that correlate with the required function.
While the specification supports Applicant was in possession of 3 specific antibodies, namely antibody A having light chain CDR sequences consisting of SEQ ID Nos. 15, 16 and 17, and heavy chain CDR sequences consisting of SEQ ID Nos. 24, 25 and 26, antibody B having light chain CDR sequences consisting of SEQ ID Nos. 18, 29 and 20 and heavy chain CDR sequences consisting of SEQ ID Nos. 27, 28 and 29, and antibody D having light chain CDR sequences consisting of SEQ ID Nos. 21, 22 and 23 and heavy chain CDR sequences consisting of SEQ ID Nos. 30, 31 and 32, the specification does not support any other combinations of these CDR sequences nor any combinations of any of these CDR sequences which differ by one or two substitutions, deletions or additions. The specification, including actual reduction to practice, includes no examples or supportive evidence of any possible variations of these sequences binding to HIV-1 antigen such that would convey Applicant was in possession of the entirety of each recited genus.
The specification does not disclose any specific correlation between structure and function. For example, there is no clear or specific indication what residues must be conserved in order to retain the claimed functionality, and there is no clear description as to what positions can tolerate variation in terms of substations, deletions or additions and still retain functionality.
It is well known in the art that even small changes in sequence structure can profoundly affect antibody-antigen interactions. It is not within the skill of the art to predict any and all substitutions, additions or deletions that would result in products that retain the claimed binding properties of a parent antibody. The art supports that structure is not necessarily a reliable indicator of function.
The teachings of Harlow et al. (Antibodies, A Laboratory Manual, Cold Spring Harbor laboratory, 1988, pages 25-26 and 37-59, cited herewith) which describe how the steps of the humoral immune response to an immunogen are dependent on APC, T-cell and B-cell recognition and processing of the immunogen in ways well known in the art to be highly unpredictable and heavily influenced by the particular immunogen and the specifics of the immunization protocol. Harlow et al. teach that even small changes in structure, such as loss of a single hydrogen bond, can profoundly affect antibody-antigen interaction (p. 25, last paragraph to page 26, second paragraph).
The principles laid out in Harlow are further illustrated in the teachings of Edwards et al. ("The remarkable flexibility of the human antibody repertoire; isolation of over one thousand different antibodies to a single protein, BLyS" J. Mol. Biol. (2003) 334, 103–118, DOI: 10.1016/j.jmb.2003.09.054), which shows the immense combinatorial flexibility and capacity of the human antibody repertoire to generate binding sites to an individual protein antigen, the B-lymphocyte growth factor known as “BLyS” (see entire document). Edwards describes in detail how the breadth of antibody structures against a given immunogen can be influenced by the immunization and/or selection methods (see Discussion Section).
As another example see Meyer et al. (“New Insights in Type I and II CD20 Antibody Mechanisms-Of-Action With a Panel of Novel CD20 Antibodies”, British Journal of Haematology, 2018, 180, 808–820, |https://doi.org/10.1111/bjh.15132) which supports the potential scope of the genus of antibodies encompassed by the instant claims, Meyer describes the core binding region of the well-known anti-CD20 antibody rituximab corresponds to amino acid residues 170ANPS173, wherein N171 is the key residue for binding. By contrast, the OBZ and B1 anti-CD20 antibodies share an overlapping epitope with rituximab (170ANPSEKNSP178); however, in contrast to rituximab residues at positions 176–178 contribute the most to binding (see page 809, left col., 2nd full paragraph).
Meyer also described the production and characterization of a panel of new anti-CD20 antibodies which were shown to bind epitopes contained within or nearby the rituximab 170ANPS173 epitope but to bind to different residues than rituximab binds in this region (see page 811, “New CD20 mAbs with overlapping, but distinct epitopes,” see also page 815-16 bridging paragraph).
More particularly, Meyer teaches the newly created anti-CD20 mAbs m1 and m2 were found to bind within but also in the vicinity of the rituximab binding site (m1 and m2) and elsewhere (m2):
“detailed epitope mapping was performed for both mIgG2c-CD20 mAbs m1 and m2, by using PepScan technology. We identified the critical residues of m1 to be 168EPANPSEK175 by using linear (Figure S2A) and circular (Fig 2C, left) peptides with a positional amino acid scan covering the larger extracellular loop. Also, for m2, a signal decrease below the WT binding signal occurred within the 168EPANPSEK175 sequence motif but the binding signal to the linear (Figure S2B) and circular (Fig 2C, right) peptide was rather low. This suggests that the epitope of both mAbs is located on the larger loop in the same region, however their binding characteristics are different. The data suggests that m1 binds a linear epitope, whereas m2 binds to a conformational epitope.” Regarding Meyers, while these antibodies bind within or nearby the rituximab 170ANPS173 epitope they do so with heavy and light chain CDRs non-homologous to those of rituximab.
Thus, even if multiple antibodies bind epitopes within the same small region of a given polypeptide it is not uncommon for said antibodies to bind to different amino acids even within said small region and for said antibodies to have structurally dissimilar CDRs.
As further illustration of the unpredictability in the art, Brown et al. (“Tolerance of single, but not multiple, amino acid replacements in antibody VH CDR 2: a means of minimizing B cell wastage from somatic hypermutation?”, J Immunol. 1996 May;156(9):3285-91), describes how a one amino acid change in the VHCDR2 of a particular antibody was tolerated whereas, the antibody lost binding upon introduction of two amino changes in the same region (at 3290 and Tables 1 and 2).
Vajdos et al. (“Comprehensive functional maps of the antigen-binding site of an anti-ErbB2 antibody obtained with shotgun scanning mutagenesis” J Mol Biol. 2002 Jul 5;320(2):415-28, DOI: 10.1016/S0022-2836(02)00264-4) teach that amino acid sequence and conformation 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 (see especially at 416). Aside from the CDRs, the Fv also contains more highly conserved framework segments which connect the CDRs and are mainly involved in supporting the CDR loop conformations, although in some cases, framework residues also contact antigen.
The evidence cited in detail above supports that it is not possible to visualize or recognize the identities of the members of each of the claimed genera that exhibit the required functional property. Applicant was not considered to be in possession of all antibodies encompassed by the extremely large and potentially variable claimed language. There is no disclosure of partial structure or other common features, common to all members of each genus, which would be responsible for the recited binding ability/function.
The specification discloses a limited 3 species of antibodies that meet both the structural and functional requirements of the claims. For all the reasons discussed in detail above, claims 1-9, 16, 17, 19, 21, 23, 27-29 are rejected under 35 U.S.C. 112(a) as Applicant was not in possession of all other species encompassed by the claimed genera indicated above (with respect to claims 1 and further 2).
Regarding claim 25, Applicant further recites a nucleotide sequence encoding the anti-HIV-1 antibody according to claim 1. As indicated in detail above for the reasons as noted, Applicant is not considered in possession of the entirety of the invention as claimed. Even further, regarding nucleic acid sequences encoding a particular antibody, one having ordinary skill in the art could not readily predict a nucleotide sequence for an antibody of an unknown structure. For a given amino acid sequence there are potentially many different possible nucleotide sequences that would translate to the same sequence (since several amino acid residues are encoded by more than one codon). For this reason, one having ordinary skill cannot readily visualize what nucleic acid sequence would encode an antibody as claimed (for example, an antibody comprising one or two unspecified substitutions, additions or deletions). As a result, claims 25 is further rejected under 35 U.S.C. 112(a), as Applicant is not in possession of all nucleic acid sequences encompasses the antibodies encompassed by the recited genera as indicated in detail above.
Claim 30 is further directed to “an anti-HIV-1 antibody which specifically binds to an epitope of HIV-1 p24 protein consisting of an amino acid sequence of SEQ ID NO. 33, wherein the anti-HIV-1 antibody comprises…” the CDRs as claimed (see claim 30 recites CDRs consistent with claim 1 discussed in detail previously above). Regarding the language at claim 30, “binds to an epitope of HIV-p24 protein consisting of an amino acid sequence of SEQ ID NO. 33” limits the claim to an antibody that binds an epitope (any epitope) that is found within the sequence consisting of (limited to) the sequence SEQ ID NO. 33- the claim does not, for example require or limit to the an epitope that is SEQ ID NO. 33 (i.e., the epitope is not limited to SEQ ID NO. 33), and further merely requires the protein SEQ ID NO. 33 (see recites “of HIV-p24 protein consisting of the amino acid sequence of SEQ ID NO. 33”). The limitations of claim 30 further are describing the product by what it does in terms of desired binding property (binds to an epitope of HIV-p24 protein consisting of an amino acid sequence of SEQ ID NO. 33), rather than by the structure of the antibody itself.
The claim still encompasses an extremely large genus of products that may be characterized by substantial variability (basically any antibody that exhibits the desired functional ability),whereas the scope of the description is much narrower. The further limitations directed to what the antibody binds does nothing to further describe the structure of the antibody itself, and as such is not sufficient to show applicant was in possession of the entirety of the claimed subject matter.
See as discussed in detail previously above, the originally filed specification is limited to 3 specific antibodies, and these 3 fail to suggest or provide structure that would correlate with the desired function in a way that would allow one to readily visualize all the species encompassed by the claimed genus.
Recent court cases 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 AbbVie Deutschland GmbH v. Janssen Biotech. Inc. as well as Amgen v. Sanofi, as discussed above. Indeed, in Amgen the court indicates 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 give the required kind of structure-identifying information about the corresponding antibodies, with the antibody-antigen relationship be analogized as a search for a key on a ring with a million keys on it.
Regarding predictability as it relates to antigen/antibody binding is as discussed above. As noted above, even if multiple antibodies bind epitopes within the same small region of a given polypeptide it is not uncommon for said antibodies to bind to different amino acids even within said small region and for said antibodies to have structurally dissimilar CDRs (see Meyer et al. discussed above).
For all of the reasons as indicated, claim 30 is similarly rejected under 35 U.S.C. 112(a), as the specification does not support Applicant was in possession of the antibody as claimed at claim 30.
New claim 33 as presented limits the light chain variable region to particular sequences (no substitutions, deletions or additions). However, the issues raised above regarding the heavy chain CDRs sequences is still an issue for the reasons discussed in detail above. This is similarly the case regarding new claim 34, which limits the heavy chain sequence only.
Further, newly recited claims 35-38 fail to provide any further written description such to satisfy requirements under 35 U.S.C. 112(a) for the claimed antibody.
Consistent with the reasons as indicated above the claims are rejected under 35 U.S.C. 112(a) for in sufficient written description, as the originally filed specification does not convey evidence that Applicant was in possession of each of the recited genera encompassed by the claims. One having ordinary skill in the art cannot readily visualize what species of variants that differ by one or two substitutions, deletions or additions would retain the desired functional ability (the required binding, as claimed).
Response to Arguments
Applicant's arguments filed 11/13/2025 have been fully considered but they are not persuasive for the following reasons.
Regarding remarks page 10, the previous objection to the specification is withdrawn in response to Applicant’s amendments to the claims (abstract is amended, 11/13/2025).
Regarding the issues raised under sequence compliance (referenced at remarks page 10 by Applicant), see for the reasons indicated above, the sequence listing provided is defective.
Regarding the rejection of claims under 35 U.S.C. 112(a), for insufficient written description, at remarks page 10-12 applicant refers to the amino acid sequences of anti-HIV-1 antibodies referenced in the specification as A, B and D. At remarks pages 12-13 Applicant indicates the claims are amended to recite the sequences shown in the foregoing table. However, this argument is not persuasive because although the claim scope encompasses these antibodies, the scope is also broader as it includes antibodies limited to the claimed sequences and also those having one or to substitutions, deletions or additions.
Applicant further argues, regarding this additionally recited language that extends the scope of the claimed antibodies beyond merely those limited to A, B, and D, that the claimed SEQ ID Nos. are very short, and so the language “by one or two substitutions, deletions or additions” does not change the scope much. However, this is not persuasive, particularly for the reasons and evidence discussed in the detailed rejection previously and above. Specifically, even one single change in residue can have major effects on binding/function of an antibody. The argument that the sequences are short and exhibit only one or two changes each is not persuasive given even such a small change could have a large impact on binding. This is also the case given that the recited potential changes are recited to be at the CDR sequences. For example, the claims are not limited to sequences that retain the specific CDRs, and merely have variations at other regions of the sequence. While the claims do have literal support, and as such the claim language is not new matter, the issue that the claims do not support Applicant was in possession of all possible species encompassed by this extremely large and variable claim language. One cannot readily visualize what species, encompassed by the large and variable claimed genus, would still be capable of and exhibit the required functional ability. As such, the claimed language is rejected under 35 U.S.C. 112(a) for the reasons as indicated in detail above.
Regarding remarks at page 13, the previous rejection of claim 30 under 35 U.S.C. 102(a)(1) is withdrawn in response to Applicant’s amendments to the claim.
For all of these reasons, Applicant’s remarks are not persuasive.
Conclusion
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Correspondence
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ELLEN J MARCSISIN whose telephone number is (571)272-6001. The examiner can normally be reached M-F 8:00am-4:30pm.
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/ELLEN J MARCSISIN/Primary Examiner, Art Unit 1677