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 .
Claims Status
The remarks filed on 06/26/2025 are acknowledged.
Claims 1-26, 33, 36, 38, 43-59 and 61 are cancelled.
Claims 27-32, 34-35, 37, 39-42, and 60 are pending and under examination.
Withdrawn
The rejections of claims 27-32, 34-35, 39-42, and 60-61 under 35 U.S.C. 112(a) written description are withdrawn. Applicant has amended claim 27 to overcome the rejections.
The rejections of claims 39 and 40 under 35 U.S.C. 112(a) enablement are withdrawn. Applicant has amended the claims to overcome the rejections.
The double patenting rejections of claims 27-32, 34-35, 37, 39-42, and 60-61 over U.S. Patent No. 10,717,778 are withdrawn in light of the terminal disclaimer filed 06/26/2025.
Terminal Disclaimer
The terminal disclaimer filed on 06/26/2025 disclaiming the terminal portion of
any patent granted on this application which would extend beyond the expiration date of
U.S. Patent No. 10,717,778 has been reviewed and is accepted. The terminal disclaimer has been recorded.
Claim Interpretation
In view of the 112(b) rejections and 112(a) new matter rejections below, the Examiner is interpreting claim 27 as including, at a minimum, the substitutions listed (i.e. L48I in the VL and T30S, L48V, A49S and/or F49Y in the VH) and not as being limited to only these substitutions, as the “consisting” language would imply, since dependent claims 28, 37, and 60 add limitations that require more substitutions in the VL and VH domains than those listed in claim 27. Thus, it seems Applicant still desires to claim the narrower of the VL and VH domains comprising more substitutions than only those listed in claim 27, and did not intend for the “consist(s)” of language in claim 27 to be limiting.
New Grounds of Rejections Necessitated by Amendment
Claim Rejections - 35 USC § 112(b)
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 27-32, 34-35, 37, 39-42, and 60 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.
Claim 27 recites the limitation “…ii) said VH Domain consists of the amino acid sequence of SEQ ID NO:56, modified to consist of one or more amino acid substitution(s) in the framework regions of said VH Domain selected from T30S, L48V, A49S, or F79Y…”. The language of “consist of one or more amino acid substitution(s)… selected from T30S, L48V, A49S, or F79Y” makes it unclear if the list of amino acid substitutions is an open or closed list and if the VH can only comprise these amino acid substitutions or may comprise other amino acid substitutions. Additionally, dependent claims 28, 37, and 60 add limitations that require more substitutions in the VL and VH domains than those listed in claim 27, further making the limitations of claim 27 unclear. Therefore, the scope of this claim is indefinite.
Claims 28-32, 34-35, 37, 39-42, and 60, which depend from claim 27, are therefore indefinite for the same reasons.
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 27-32, 34-35, 37, 39-42, and 60 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. This is a new matter rejection.
Claim 27 requires that the VL domain consists of the amino acid sequence of SEQ ID NO: 55 modified with the amino acid substitution L48I and the VH domain consists of the amino acid sequence of SEQ ID NO: 56, modified to consist of one or more amino acid substitution(s) in the framework region of said VH domain selected from T30S, L48V, A49S, or F49Y. The original disclosure does not provide support for a VL and VH domain consisting of only these specific substitutions, as required by the claim. The specification does support VL and VH domains comprising these substitutions, but there is no mention of VL and VH domains with only these substitutions and no others.
Claim Rejections - 35 USC § 112(d)
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 28, 37, and 60 are rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. Claim 27, from which claims 28, 37, and 60 depend thereof, recites the limitation “i) said VL Domain consists of the amino acid sequence of SEQ ID NO:55, modified with the amino acid substitution L48I; and ii) said VH Domain consists of the amino acid sequence of SEQ ID NO:56, modified to consist of one or more amino acid substitution(s) in the framework regions of said VH Domain selected from T30S, L48V, A49S, or F79Y; and wherein said numbering is the Kabat numbering.” The “consists of” language would imply that SEQ ID NOs: 55 and 56 would only have the specified amino acid substitutions and would not have any other amino acid substitutions. However, the sequences recited in claim 28 and 37 (i.e. 57, 58, 110-115), and the recited substitutions in claim 60 would expand the scope of claim 27 because they comprise substitutions beyond L48I in the VL and T30S, L48V, A49S, or F79Y in the VH. Therefore, these claims do not further limit claim 27. Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Note: While these claims expand the scope of claim 27, they still recite limitations which are taught in the art as addressed in the rejections under 35 U.S.C. 103 below.
Maintained Rejections
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.
Claims 27-32, 34-35, 39-42, and 60 are rejected under 35 U.S.C. 103 as being unpatentable over Haynes (WO 2016054101; 10/16/2023 PTO-892) in view of Schwabe (WO 2017062672; 10/16/2023 PTO-892), Vasquez (WO 2009036379; 10/16/2023 PTO-892), and Creative Biolabs, 2017 (10/16/2023 PTO-892).
Regarding claims 27-29, 30, and 60, Haynes teaches bispecific molecules, which are covalently linked polypeptide chains to form antibodies (bispecific antibody), for their use in the treatment of HIV-1 and that the bispecific molecules can bind to two different targets or epitopes on two different cells [0007]. Haynes further teaches that 7B2 are targeting arms that recognize HIV-1 gp41 [0048] and that the bispecific molecules comprise an arm with the binding specificity of 7B2 [0007]. Haynes also teaches that SEQ ID NO: 55 is the VL region of 7B2 and that SEQ ID NO: 56 is the VH region of 7B2 [see Figure 9, page 110]. Haynes further teaches that the antibodies include humanized antibodies [0107] and that the sequences of non-human antibodies may be humanized [0071].
SEQ ID NO: 55 has 100% sequence identity to SEQ ID NO: 55 of the instant application and SEQ ID NO: 56 has 100% sequence identity to SEQ ID NO: 56 of the instant application.
However, Haynes does not teach that the VL domain is modified to comprise one or more amino acid substitution(s) in the framework regions of said VL Domain selected from P15L, H22N, R39K, L48I, N76S, N77S, 185V, H100Q, or R103K or that the VH domain is modified to comprise one or more amino acid substitution(s) in the framework regions of said VH Domain selected from Q6E, V11L, Fl2V, E23A, T30S, V37I, L48V, A49S, V78L, F79Y, L82M, D82aN, R82Bs, S83R, D85E, A107T, or R108L.
Schwabe teaches SEQ ID NO: 364, a humanized antibody named 9G3V4-1 [page 237, see Table].
SEQ ID NO: 364 of Schwabe has framework regions with 100% sequence identity to SEQ ID NO: 57 of the instant application. Further, SEQ ID NO: 57 of the instant application contains the framework regions of SEQ ID NO: 123 of the instant application for frameworks 1-3 and SEQ ID NO: 124 of the instant application for framework 4. SEQ ID NO: 57 of instant claim 28 when aligned to SEQ ID NO: 55 of instant claim 27 comprises the following mutations: H22N, R39K, L48I, N76S, I85V, H100Q, and R103K. Thus, this also meets the limitations of instant claim 60.
Vasquez teaches polynucleotides that encode one or more heavy chain chassis (framework) amino acid sequences that are N-terminal to the CDRH3 amino acid sequences, and that the heavy chain chassis sequence can be IGHV3-11 [page 10, lines 19-26] and that the polynucleotides further encode one or more FRM4 (framework) amino acid sequences that are C-terminal to the CDRH3 amino acid sequences, and that the FRM4 amino acid sequence can be IGHJ4 [page 11, lines 1-4]. Vasquez also teaches that antibodies can contain CDR length and sequence diversity, and framework diversity, representative of naturally-occurring human antibodies [page 2, lines 25-27]. Vasquez further teaches that the chassis sequences are based on the human IGHV germline repertoire and correspond to all functionally expressed human IGHV germline sequences [page 43, lines 22-26]. Thus, the heavy chain chassis sequences of Vasquez would be known framework regions to humanize antibodies. Vasquez also teaches that there is a need for antibodies that are non-immunogenic (i.e. more human) and that have desired properties (e.g., the ability to recognize a broad variety of antigens) [page 2, lines 8-11].
The first through third framework regions are within IGHV3-11, as taught by Vasquez, and which have 100% sequence identity to the first through third framework regions of SEQ ID NO: 58 as evidence in the specification [see Figure 7B]. The IGHJ4-1 sequence is shown in Table 20 [see page 123] and has 100% sequence identity to the fourth framework of SEQ ID NO: 58. Further, SEQ ID NO: 58 contains the framework regions of SEQ ID NO: 125 for frameworks 1-3 and SEQ ID NO: 126 for framework 4. SEQ ID NO: 58 of instant claim 28 when aligned to SEQ ID NO: 56 of instant claim 27 comprises the following mutations: Q6E, V11L, F12V, E23A, T30S, V37I, L48V, A49S, V78L, F79Y, L82M, D82aN, R82bS, S83R, D85E, A107T, and R108L. Thus, this also meets the limitations of instant claim 60.
Creative Biolabs teaches that antibody humanization is important for reducing the immunogenicity of monoclonal antibodies derived from xenogeneic sources and for improving their activation of the human immune system [page 2, first paragraph].
It would have been obvious to someone of ordinary skill in the art before the effective filing date of the claimed invention to have modified the frameworks of the VL and VH regions of the antibody taught by Haynes, to specifically be the framework regions as taught by Schwabe and Vasquez, thereby arriving at SEQ ID NO: 57 for the VL domain and SEQ ID NO: 58 for the VH region, because Schwabe and Vasquez teach that these are known framework regions to humanize antibodies. One would have been motivated to humanize the antibody because Haynes teaches that the antibodies include humanized antibodies [0107] and that the sequences of non-human antibodies may be humanized [0071], and Creative Biolabs teaches that antibody humanization is important for reducing the immunogenicity of the antibodies and for improving their activation of the human immune system.
Claim 31 is included in this rejection because Haynes teaches that the bispecific antibodies can include an Fc region [0094] and that the Fc region may be a variant Fc region that increases serum half-life compared to non-FC variants [0096].
Claims 32, 34, and 35 are included in this rejection because Haynes teaches that the bispecific molecules can bind to two different cells, wherein the bispecific molecule comprises an arm (epitope-binding site) with binding specificity of 7B2, which arm binds to the HIV-1 envelope expressed on the first cells (specifically gp41 as taught above), and a second arm (epitope-binding site) with the binding specificity for an epitope expressed on a different cell type than the first cell, such that the bispecific molecules ca bring the two cells together and that the second cell is an effector cell which expresses CD3 or CD16 [0007].
Claim 39 is included in this rejection because Haynes teaches that the antibody can be formulated as a composition (pharmaceutical composition) where the antibody is dissolved or dispersed in a pharmaceutically acceptable carrier [0132]. Haynes further teaches that the antibodies can be used in a method of treating and preventing HIV-1 infection in an individual, comprising administering to the individual a therapeutically effective amount of a composition comprising the antibodies in a pharmaceutically acceptable form [0108] which would have made obvious including a therapeutically effective amount in the composition.
Claim 40 is included in this rejection because Haynes teaches that the antibodies can be used in a method of treating and preventing HIV-1 infection in an individual, comprising administering to the individual a therapeutically effective amount of a composition comprising the antibodies in a pharmaceutically acceptable form [0108].
Claim 41 is included in this rejection because Haynes teaches that the antibodies can be administered in combination with latency activating agents [0134].
Claim 42 is included in this rejection because Haynes teaches that the latency activating agent can be HDAC inhibitors, e,g, vorinostat, romidepsin, panobinostat, disulfiram, JQ1, bryostatin, PMA, inonomycin, or any combination thereof [0134].
Claim 37 is rejected under 35 U.S.C. 103 as being unpatentable over Haynes (WO 2016054101; 10/16/2023 PTO-892), Schwabe (WO 2017062672; 10/16/2023 PTO-892), Vasquez (WO 2009036379; 10/16/2023 PTO-892), and Creative Biolabs, 2017 (10/16/2023 PTO-892), as applied to claims 27-32, 34-35, 39-42, and 60 above, and further in view of Johnson (WO2015184203 (‘203); 10/16/2023 PTO-892) and Johnson (WO2015021089 (‘089); 10/16/2023 PTO-892).
The teachings of Haynes, Schwabe, Vasquez, and Creative Biolabs are above. Further, Haynes teaches that the bispecific molecules can comprise a first polypeptide chain, a second polypeptide chain, and a third polypeptide chain [0010].
However, Haynes, Schwabe, Vasquez, and Creative Biolabs do not specifically teach that the gp41-binding molecule comprises a first polypeptide chain, a second polypeptide chain, and a third polypeptide chain, wherein (III) (a) said first polypeptide chain comprises the amino acid sequence of SEQ ID NO:110; (b) said second polypeptide chain comprises the ammo acid sequence of SEQ ID NO: 111; and (c) said third polypeptide chain comprises the amino acid sequence of SEQ ID NO: 112.
Johnson (‘203) teaches an HIV mab 1/CD3 mab 2/ CD8 mab 1 tri-specific binding molecule that is composed of four polypeptide chains [00353]. Johnson further teaches SEQ ID NO: 91, which is the amino acid sequence of the first polypeptide chain [00354] and the structure of this first polypeptide chain is VL(HIV mAb 1)-VH(CD3 mAb 2)-E-Coil-(CH2-CH3) [00353].
SEQ ID NO: 91 has 98.8% sequence identity to SEQ ID NO: 113 of the instant application. The differences between the two sequences are the framework substitutions as disclosed in SEQ ID NO: 57. Applicant discloses that residues 1-113 of the first polypeptide correspond to the VL domain of 7B2GL (SEQ ID NO: 57) [see paragraph 00250 of the instant specification].
Johnson (‘203) also teaches SEQ ID NO: 92, which is the amino acid sequence of the second polypeptide chain [00355] and the structure of this second polypeptide chain is VL(CD3 mAb 2)-VH(HIV mAb 1)-K-Coil [00353].
SEQ ID NO: 92 has 95.4% sequence identity to SEQ ID NO: 114 of the instant application. The differences between the two sequences are the framework substitutions as disclosed in SEQ ID NO: 58. Applicant discloses that residues 119-244 of the second polypeptide chain correspond to the VH domain of 7B2GL (SEQ ID NO: 58).
Johnson further teaches that an HIV mAb 1 may be a gp41 antibody such as 7B2 [00180].
Johnson (‘089) teaches bi-specific monovalent diabodies that are composed of three polypeptide chains [0049]. Johnson further teaches SEQ ID NO: 17, which is a preferred sequence for the third polypeptide chain [0073]. SEQ ID NO: 17 is disclosed as residues 1-10 are peptide 1 (linker) and amino acid residues 11-227 are the CH2 and CH3 domains of an IgG antibody Fc region [0074].
SEQ ID NO: 17 has 100% sequence identity to SEQ ID NO: 112 of the instant application.
It would have been obvious to someone of ordinary skill in the art before the effective filing date of the claimed invention to have modified the first and second polypeptide chains, as taught by Johnson (‘203), to contain the gp41-binding VL domain of SEQ ID NO: 57 and the gp41-binding VH domain of SEQ ID NO: 58, as taught by Haynes, Schwabe, Vasquez, and Creative Biolabs because the VL and VH domains of the polypeptide chains of Johnson (‘203) are disclosed as HIV mAb VL and VH domains, respectively, where the HIV mAb may be a gp41 antibody because it is prima facie obvious to substitute equivalents known for the same purpose (see MPEP 2144.06 (II)). Further, as Haynes teaches that the bispecific molecules can comprise a first polypeptide chain, a second polypeptide chain, and a third polypeptide chain, it would have been obvious to have chosen the specific sequence of the third polypeptide chain of Johnson (‘089) to be the third polypeptide chain because this is a known sequence in the art, and Johnson teaches that it is a preferred sequence for the third polypeptide chain in bispecific diabodies.
Response to Declarant’s Arguments
The declaration under 37 CFR 1.132 filed 06/26/2025 is insufficient to overcome the rejections of claims 27-32, 34-35, 37, 39-42, and 60 based upon the teachings of Haynes, Schwabe, Vasquez, and Creative Biolabs applied under 35 U.S.C. 103. Points 1-14 did not set forth any arguments. The Examiner acknowledges Declarant’s credentials and the nature of the invention claimed. It is noted that Declarant is an inventor of the pending application and is highly interested in the outcome of prosecution. In point 15, Declarant argues that when engineering HIV antibodies claimed in the present invention, it was common practice to identify and use framework regions derived from other HIV antibodies as a starting point for engineering our HIV antibodies of interest. This is not found persuasive because Declarant provides no objective evidence. Declarant’s statement is not an indication that this is the only method of engineering HIV antibodies and does not directly criticize any motivation in the rejection itself. A statement that other methods of engineering HIV antibodies is not dispositive of the rejection. In point 16, Declarant argues that they would not look to the framework region sequences of antibodies from other receptors or disease targets because that was not the standard practice nor were the framework sequences from non-HIV sources believed to be useful or functional to create HIV antibodies. This is not found persuasive because Declarant cannot make statements about what others would and would not do because Declarant is not in possession of that fact. The rejection sets out why one would have looked to other framework regions and that an antibody with these framework regions would have reasonably been expected to function. Declarant does not cite any objective evidence about non-useful or non-functional framework regions and the rejection clearly states that these were known framework regions to engineer antibodies. In points 17-18, Declarant argues that one of skill in the art at the time the Application was filed would not have considered looking for framework region sequences in antibodies from other receptors or disease targets, like those disclosed in Schwabe or Vasquez, because the skilled artisan would have questioned the operability of an HIV antibody constructed using non-HIV framework regions and that it was not common practice for one of ordinary skill in the HIV vaccine art to consider antibodies to targets outside the HIV art, like as taught in Schwabe or Vasquez, for constructing new HIV antibodies because of the specific and unique structure of HIV envelope. This is not found persuasive because while Declarant repeatedly refers to common practice, this is the opinion of Declarant, and Declarant has not filed any objective evidence that others wouldn’t use non-HIV framework regions or wouldn’t have a reasonable expectation of success in using non-HIV framework regions given the rationale outlined in the rejection.
In point 19, Declarant argues that there would have been no motivation, let alone suggestion, to identify and combine the teachings of Schwabe or Vasquez to arrive at the HIV framework regions claimed in the present invention. Declarant offers a legal opinion about motivation, and this is not persuasive because a clear motivation is provided in the rejection. Declaration is not entitled to any legal opinion, and saying that there is no motivation to combine is a legal determination. Further, Declarant does not provide any specific criticism of any specific fact in the rejection. In points 20, 21, and 22, Declarant states that creating an HIV vaccine has been a goal of the scientific community around the world for over 40 years, but that there has been no real success with such development and the failure to successfully create a HIV vaccine is due to many factors, including the rapidly evolving virus as well as variability in the immune responses in and within species, and because of this, there is a very high level of unpredictability when engineering HIV vaccines. This is not found persuasive because while Declarant argues some factors preventing the development of an HIV vaccine, there have certainly been factors other than technical reasons, and further, Declarant does not point to any particular deficiency in the rejection itself. Additionally, Declarant seems to be stating that the claimed subject matter solved a problem that was long standing in the art. However, there is no showing that others of ordinary skill in the art were working on the problem and if so, for how long. In addition, there is no evidence that if persons skilled in the art who were presumably working on the problem knew of the teachings of the above cited references, they would still be unable to solve the problem. See MPEP § 716.04. Further, the argument that there is a high level of unpredictability is not persuasive because Declarant provides no objective evidence supporting this statement. However, to the extent that this is given any weight, the rejections set forth why there would be a reasonable expectation of success in combining the references to arrive at the claimed antibody and Declarant does not point to any particular deficiency in the rejection itself. In point 23, Declarant argues that the skilled artisan at the time of filing would not have expected that a functional antibody could be engineered to have a sufficient and effective binding affinity using known framework regions from various other antibody targets or using some known CDR sequences due to the unpredictability of antibody engineering. This is not found persuasive because Declarant does not provide any evidence that using non-HIV framework regions would be unpredictable. In point 24, Declarant argues that one of ordinary skill in the art at the time the Application was filed would not necessarily expect incorporating amino acid mutations that were known to be used for the humanization of antibodies could generate an HIV antibody with a sufficient and effective binding affinity. This is not found persuasive because, again, Declarant does not provide any objective evidence supporting this statement. In points 25, 26, and 27, Declarant argues that one of ordinary skill would have no expectation that the HIV antibodies engineered might actually bind HIV with sufficient affinity without actually testing them, that the mutations claimed are located in the Vernier zone of the HIV antibodies engineered, which were known to affect the binding affinity for HIV, and therefore, one of skill in the art would not have had a reasonable expectation that the HIV antibodies harboring those mutations, would bind just as efficiently and effectively as the original antibodies taught in Haynes without actually testing them. This is not found persuasive because absolute predictability is not required and is not the legal bar. The Examiner clearly articulated why there would be a reasonable expectation of success in combining the references in the rejection to arrive at the claimed antibody and Declarant does not provide any objective evidence to support otherwise. To conclude, Declarant presents many arguments about the predictability of the art, and while the declaration is given all due weight, Declarant is highly interested in the outcome of prosecution, and does not support the arguments with any objective evidence.
Response to Applicant’s Arguments
The rejections of claims 27-32, 34-35, 37, 39-42, and 60 under 35 U.S.C. 103 over Haynes, in view of Schwabe, Vasquez, Creative Biolabs, Johnson (‘203), and Johnson (‘089), are maintained. Applicant states on claim 8 of the remarks that they have amended the claim language to recite the “Vernier zone” and “consisting of” language, as suggested by the Examiner in the Office Action mailed 03/12/2024. The Examiner never suggested to amend the claims to recite these limitations. Rather, the Examiner stated that Applicant’s previous arguments that the references fail to show certain features of the invention, it was noted that the features application relies (i.e. the vernier zone should be unchanged) are not recited in the rejected claim(s). Additionally, the Examiner stated that the term “comprise” means that the sequence could have any number of additional substitutions, meaning that Applicant’s argument that the vernier zone should be unchanged is not even a claimed feature. See pages 32-33 of the Office Action mailed 03/12/2024. Further, the claim amendment of “the amino acids in the Vernier zones of the VL and VH domains are unchanged, with the proviso…” still does not require that the Vernier zones remain unchanged because the VL and VH domains require specific substitutions in these zones.
Further, on pages 8-10 of the remarks, Applicant argues the rejections of the instant claims as rejected under 35 U.S.C. 103 by reiterating what was stated in the declaration. The arguments set forth in the declaration are addressed above and will not be reiterated and are incorporated herein. Applicant further argues on page 10 of the remarks that there was no motivation to combine the cited references of Haynes, Schwabe, Vasquez, and Creative Labs, and that this combination of references would not have provided a reasonable expectation of success to arrive at the claimed invention. This is not found persuasive because the Examiner has clearly articulated why one would have been motivated to combine these references to arrive at the claimed antibody with a reasonable expectation of success. See rejections above. Applicant also argues that the teachings of Johnson (‘203) and Johnson (‘089) do not cure the deficiencies of Haynes, Schwabe, Vasquez, and Creative Biolabs. This is not found persuasive because no such deficiency exists.
Conclusion
No claims are allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Brittney E Donoghue whose telephone number is (571)272-9883. The examiner can normally be reached Mon - Fri 7:30 - 3:30.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Jeffrey Stucker can be reached at (571) 272-0911. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/B.E.D./Examiner, Art Unit 1675
/JEFFREY STUCKER/Supervisory Patent Examiner, Art Unit 1675