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 .
Claims 1-19 are pending and will be examined on the merits.
Claim Rejections - 35 USC § 112
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.
Claim 3, 5, 8 and 13-19 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.
Claims 3, 5, 8, 14 16 and 17
Regarding claims 3, 5, 8, 14, 16 and 17, each instance of the phrase "preferably" (recited 3x in claim 3; 1x in 5, 8, 14, 16 and 17) renders the claim indefinite because it is unclear whether the limitation(s) following the phrase are part of the claimed invention. See MPEP § 2173.05(d).
Note: All of claims 3, 5, 8, 14, 16 and 17 will be examined as if the limitation(s) following “preferably” did not occur.
Claim 13
Regarding claim 13, the phrase "such as" renders the claim indefinite because it is unclear whether the limitations following the phrase are part of the claimed invention. See MPEP § 2173.05(d).
Note: claim 13 will be examined as if the limitations following “such as” did not occur.
Claims 15, 18 and 19
All of claims 15, 18 and 19 are method claims directed to “methods of using” a composition claimed elsewhere in the claim set in: (i) prophylactic or therapeutic treatment of a neurodegenerative tauopathy in a subject or (ii) monitoring the progression of a neurodegenerative tauopathy in a subject.
None of claims 15, 18 or 19 recite any active method steps regarding how the method of using the claimed composition(s) are performed. Attempts to claim a process without setting forth any steps involved in the process generally raises an issue of indefiniteness under 35 U.S.C. 112(b) or pre-AIA 35 U.S.C. 112, second paragraph. For example, a claim which read: "[a] process for using monoclonal antibodies of claim 4 to isolate and purify human fibroblast interferon" was held to be indefinite because it merely recites a use without any active, positive steps delimiting how this use is actually practiced. Ex parte Erlich, 3 USPQ2d 1011 (Bd. Pat. App. & Inter. 1986). (See MPEP § 2173.05(q)).
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 and 3-19 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention. This is a written description rejection.
Note: This written description rejection is directed towards embodiments of the claimed invention that are dependent on claim 1.
Note: claims 15, 18 and 19 were indicated as indefinite above for failing to recite any active method steps. These claims are subject to this written description rejection solely on the basis of referring to a composition lacks written description.
Scope of the claimed antibodies
Instant claims 1, and 4-19
Instant claims 1 and 4-19 are directed toward human-derived recombinant anti-tau antibody or fragment thereof (as well as nucleic acids encoding such antibodies, vectors comprising such nucleic acids encoding such antibodies and host cells comprising vectors comprising nucleic acid encoding such antibodies) that is capable of: i) binding pathological hyperphosphorylated tau filaments in dystrophic neurites, neurofibrillary tangles and neuropil threads in an IHC assay of brain tissue from patients with Alzheimer’s disease (AD), progressive supranuclear palsy (PSP) and/or Pick’s Disease (PiD), with the antibodies binding specific epitopes recited later in claim 1 (either the epitope comprising SEQ ID NOs: 31 and 32, epitope pS202/pT205 (SEQ ID NO: 33) or epitope pT212/pS214 (SEQ ID NO: 34)) and ii) capturing tau and AD-associated Tau in an immunoprecipitation assay with AD brain extracts.
With respect to the claimed antibody’s required biochemical functions and structure required to perform these, claims 1 and 4-19 are directed to three genera—
Genus 1- Genus 1 is directed to antibodies recognizing an epitope comprising SEQ ID NO: 31 and SEQ ID NO: 32. Genus 1 is directed to antibodies having VH CDRs 1, 2 and 3 of SEQ ID NOs: 3, 4 and 5, respectively and VL CDRs 1,2 and 3 of SEQ ID NOs: 8, 9 and 10, respectively. Genus 1 also permits up to two amino acid substitutions in each of the six VH and VL CDR sequences with no limitations regarding which CDR residues may be substituted or which amino acid residues the substituted CDR residues are permitted to be replaced with.
Genus 2- Genus 2 is directed to antibodies recognizing an epitope of phosphorylated tau peptide pS202/pT205 (SEQ ID NO: 33). Genus 2 is directed to antibodies having VH CDRs 1, 2 and 3 of SEQ ID NOs: 13, 14 and 15, respectively and VL CDRs 1,2 and 3 of SEQ ID NOs: 18, 19 and 20, respectively. Genus 2 also permits up to two amino acid substitutions in each of the six VH and VL CDR sequences with no limitations regarding which CDR residues may be substituted or which amino acid residues the substituted CDR residues are permitted to be replaced with.
Genus 3- Genus 3 is directed to antibodies recognizing an epitope of phosphorylated tau peptide pS212/pS214 (SEQ ID NO: 34). Genus 3 is directed to antibodies having VH CDRs 1, 2 and 3 of SEQ ID NOs: 23, 24 and 25, respectively and VL CDRs 1,2 and 3 of SEQ ID NOs: 28, 29 and 30, respectively. Genus 3 also permits up to two amino acid substitutions in each of the six VH and VL CDR sequences with no limitations regarding which CDR residues may be substituted or which amino acid residues the substituted CDR residues are permitted to be replaced with.
Instant claim 3
Instant claim 3 is dependent on instant claim 1 and further limits claim 1 by specifying the antibody comprises VH and VL pairings of: 1) SEQ ID NOs: 2 and 7, respectively, 2) SEQ ID NOs: 12 and 17, respectively and 3) SEQ ID NOs: 22 and 27, respectively. Additionally, each VH and VL sequence of each recited VH/VL pairing is permitted to comprise one or more amino acid substitutions, with there being no restrictions or limitations regarding where these residue substitutions are permitted to occur or which residues the substituted residues are permitted to be replaced with. Please note that, with respect to the binding-critical CDR sequences, claim 3 is directed to the same CDR combinations as claim 1 (including the up to two amino acid substitutions per CDR recited in claim 1).
In order to demonstrate the astronomically large number of variant antibodies the instant claims are directed to, the CDRs associated with VH of SEQ ID NO: 22 and VL of SEQ ID NO: 27 found on p 31 on of the instant Specification will be used as an example. The table below shows the length of each of the VH and VL CDRs. The combination function from statistics (nCr = n!/r!(n-r)!) was applied to each of the CDRs with n = the total number of residues within that CDR and r = the 2 amino acids to be picked from each CDR for substitution:
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The results of the nCr function depict the number of possible ways of selecting two amino acids for substitution. Note that there are over 2.1 billion different ways simply to select the two residues from each of the CDR to be substituted. Each residue substituted must then be replaced with one of the 19 remaining amino acids and this must be done independently for each of the 2.1 billion ways one may select two amino acids from each CDR for substitution, resulting in the claims being directed to an unfathomably large number of variant CDR combinations. As such, instant claim 3 encompasses the genus of all is astronomically large genus of antibodies defined by partial structure, provided that the antibody(ies) are capable of performing the required function of binding one of: the epitope comprising SEQ ID NOs: 31 and 32, epitope pS202/pT205 (SEQ ID NO: 33) or epitope pT212/pS214 (SEQ ID NO: 34))
Description pf Claimed Antibodies in specification
The instant Specification discloses a total of 16 anti-tau antibodies and their binding properties at Table I, which is found on p 3 of the instant Specification. However, with respect to antibodies capable of performing the required function of binding one of the three specific epitopes recited in instant claim 1, Table I of the instant disclosure discloses three antibodies: 1) antibody NI-502.4P3, which is capable of binding the tau epitope comprising SEQ ID NOs 31 and 31, 2) antibody NI-502.31B6, which is capable of binding the tau epitope pS202/pT205 (SEQ ID NO: 33) and antibody NI-502.8H1, which is capable of binding the tau epitope pT212/pS2114 (SEQ ID NO: 34) (Specification, p 3, line 1).
The instant disclosure discloses that antibody NI-502.4P3 comprises a VH of SEQ ID NO: 2 (comprises VHCDR 1, 2 and 3 of SEQ ID NOs: 3, 4 and 5, respectively) and a VL of SEQ ID NO: 7 (comprises VLCDR 1, 2 and 3 of SEQ ID NOs: 8, 9 and 10, respectively). The instant disclosure discloses that antibody NI-502.31B6 comprises a VH of SEQ ID NO: 12 (comprises VHCDR 1, 2 and 3 of SEQ ID NOs: 13, 14 and 15, respectively) and a VL of SEQ ID NO: 17 (comprises VLCDR 1, 2 and 3 of SEQ ID NOs: 18, 19 and 20, respectively). The instant disclosure discloses that antibody NI-502.8H1 comprises a VH of SEQ ID NO: 22 (comprises VHCDR 1, 2 and 3 of SEQ ID NOs: 23, 24 and 25, respectively) and a VL of SEQ ID NO: 27 (comprises VLCDR 1, 2 and 3 of SEQ ID NOs: 28, 29 and 30, respectively) (Specification, Table III, p 30-31).
The instant disclosure does not disclose any variants of antibodies NI-502.4P3, NI-502.31B6 or NI-502.8H1 wherein up to two amino acid substitutions are made to one or more of the CDR sequences of the parental antibody to form a variant antibody that retains the parental antibody’s ability to bind its respective tau epitope. As such, for each of the three tau epitopes recited in claim 1, the instant disclosure discloses one species of antibody comprising six known and distinct CDRs capable of performing the required function of binding that epitope.
State of the Relevant Art
As was well-known in the antibody art, antibodies as a class share an overall structure generally comprising two heavy chain polypeptides that each comprises a heavy chain variable region (VH) and a heavy chain constant region made up of several domain (CH1, hinge, CH2, CH3, and for some antibodies, a CH4). Each of the heavy chains pairs with a light chain polypeptide that comprises a light chain variable region (VL) and a constant region. Sela-Culang (Sela-Culang, et al., Front in Immunol. 2013; Vol. 4; Article 302) teaches on the subject of the structural basis of antibody-antigen recognition (Sela-Culang, Abstract). Sela-Culang teaches that there is a lack of intrinsic properties linking epitopic vs non-epitopic residues based on features present in said residues suggests that epitopes depend, to a great extent, on the antibody that recognizes them (Sela-Culang, p 2, ¶ 7). Sela-Culang teaches that antibodies fold in such a manner such that six hypervariable loops of the light and heavy domains of an antibody (three loops on the HC and three on the LC) are folded together and form the antigen binding site (Sela-Culang, p 3, ¶ 2). Sela-Culang teaches that the complimentary determining regions (CDRs) are amino acid sequences within this hypervariable region and that amino acids that define the CDR regions are typically defined based on numbering schemes (e.g., Kabat, Chothia, IMGT) derived from empirical studies of the boundaries between the framework and binding residues of the antibodies (Sela-Culang), p 3, ¶ 3). Sela-Culang teaches that identification of paratopes (the portion of an antibody which binds an antigen) is done through the identification of CDRs but CDRs, as identified by methods such as Kabat, Chothia and IMGT may miss ~20% of antigen binding residues (Sela-Culang, 4, ¶ 1-2). Sela-Culang teaches that each CDR has its own unique amino acid composition (i.e., different from the other CDRs) and each CDR has a unique set of contact preferences (Sela-Culang, p 5, ¶ 1).
Absent the conserved structure provided by all six CDRs of a parental antibody in the context of appropriate VH and VL framework sequences, the skilled artisan generally would not be able to visualize or otherwise predict what an antibody with a particular set of functional properties would look like structurally. As discussed above, neither an epitope nor a paratope can be calculated a priori based on properties of the component amino acids. Furthermore, each and every CDR sequence is unique and distinct and, as such, a CDR sequence cannot be predicted, either from the epitope sequence of from the CDR sequences of the antibody, if known.
In addition to the importance of the CDR regions, Sela-Culang also teaches that framework residues are also play an important role in antigen binding (Sela-Culang, P 7, ¶ 3). These framework residues can be divided into two types. The first are framework residues that actually contact the antigen and therefore are part of the binding site (Sela-Culang, p 7 ¶ 4). The second type of framework residues that affect antigen binding are framework residues that do not directly contact the antigen but affect binding indirectly (Sela-Culang, p 7, ¶ 5). Some of the framework residues are in close proximity to the CDR regions, providing structural support that allows the CDRs to adopt the right conformation to form the antigen binding site (Sela-Culang, p 7, ¶ 5). The other type of framework residues that indirectly affect antigen binding are further from the CDR regions and affect the relative orientation of the VH and VL regions, and thus the orientation of the CDRs relative to each other (Sela-Culang, p 7, ¶ 6). Sela-Culang also teaches that the effect of framework residues on antigen binding is impossible to predict a priori. For example, Sela-Culang teaches that positions in FR-3 of the heavy chain affects the orientation of CDRH1 relative to CDRH2, however this is not always the case, as it has been shown that mutating a Lys in this region for either a Val, Ala or Arg resulted in affinity differences but no structural changes (Sela-Culang, p 7, ¶ 5).
Additionally, at the time of filing, numerous anti-tau antibodies were known in the art Weinreb (Weinreb, et al., US 2017/0369560A1; Published 12/28/2017; priority to 12/21/2012 via US 61/745,410) discloses numerous conventional antibodies, all of which comprise six distinct CDRs (Weinreb, claim 43).
Are the disclosed species representative of the claimed genus?
MPEP § 2163 states that a “representative number of species” means that the species that are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
As stated and articulated above, for each of the three recited tau epitopes of claim 1, the instant disclosure discloses one species of antibody with six known and distinct CDR sequences capable of performing the required function of binding that epitope.
The VH and VL CDR pairing of VHCDR 1, 2 and 3 of SEQ ID NOs: 3, 4 and 5, respectively and VLCDR 1, 2 and 3 of SEQ ID NOs: 8, 9 and 10, respectively is disclosed as being capable of binding the tau epitope comprising instant SEQ ID NOs 31 and 32. The VH and VL CDR pairing of VHCDR 1, 2 and 3 of SEQ ID NOs: 13, 14 and 15, respectively and VLCDR 1, 2 and 3 of SEQ ID NOs: 18, 19 and 20, respectively is disclosed as being capable of binding the tau epitope pS202/pT205 (SEQ ID NO: 33). The VH and VL CDR pairing of VHCDR 1, 2 and 3 of SEQ ID NOs: 23, 24 and 25, respectively and VLCDR 1, 2 and 3 of SEQ ID NOs: 28, 29 and 30, respectively is disclosed as being capable of binding the tau epitope pT212/pS214 (SEQ ID NO: 34).
However, as discussed above, the fact that the claims permit up to two amino acid substitutions per CDR with no further limitations or restrictions on such substitutions results in the claims encompassing an astronomically large number of variant antibodies per parental antibody. A disclosure of a single antibody capable of performing the required function of binding one of the tau epitopes of claim 1 is simply insufficient to be representative of the astronomically large genus of variant antibodies also encompassed by the claims.
Identifying characteristics and structure/function correlation
In the absence of a representative number of species, the written description requirement for a claimed genus may be satisfied by disclosure of relevant, identifying characteristics; i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus.
As noted above, the art generally accepted that the combination of the CDRs within the VH and VL pair of an antibody was the minimum structure essential for binding specificity and the framework residues also play a role in antigen binding and a disclosure of an antigen or epitope does not permit a skilled artisan to envision the structure an antibody would need to have to bind that antigen or epitope, even if the amino acid sequence of that epitope is known.
The teachings of Sela-Culang make very clear that a structure-function relationship between an antibody’s CDRs and the epitope it binds is not understood well enough to permit a skilled artisan to analyze an epitopic sequence and envision, a priori, the required CDR structure required to form a functional antibody capable of binding that epitope. Sela-Culang teaches that CDRs are independent structurally and each possess independent binding preferences. There is nothing in the present disclosure nor the prior art that would lead one of skill in the art to believe that the disclosure contains any new discoveries that would supplant these notions.
Because the species disclosed are insufficient to be considered representative of either the unfathomably large number of possible variations to the binding-critical CDR regions, coupled with the lack of established structure/function correlation, the claims lack written description and Applicant was not in possession of the invention as claimed.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 15, 18 and 19 are rejected under 35 U.S.C. 101 because the claimed invention is directed to non-statutory subject matter. The claims do not fall within at least one of the four categories of patent eligible subject matter because the claims are directed to the “use” of the anti-tau antibodies, nucleic acids encoding such antibodies, and vectors comprising nucleic acids encoding such antibodies.
The claims are not directed toward a: 1) composition of matter; 2) machine; 3)manufacture; or 4) process, but rather a “method of using” of the claimed anti-tau antibodies (or associated nucleic acids/vectors), wherein no active, positive method steps are present to suggest a process is being claimed. "Use" claims that do not purport to claim a process, machine, manufacture, or composition of matter fail to comply with 35 U.S.C.§ 101 MPEP 2173.05(q).
Subject Matter Free of Prior Art
The following antibodies are free of prior art:
An anti-tau antibody that recognizes an epitope comprising instant SEQ ID NOs: 31 and 32, wherein the antibody comprises VH CDR 1, 2 and 3 of SEQ ID NOs: 3, 4 and 5, respectively and VL CDR 1, 2, and 3 of SEQ ID NOs: 8, 9 and 10, respectively.
An anti-tau antibody that recognizes an epitope of phosphorylated tau peptide pS202/pT205 (SEQ ID NO: 33), wherein the antibody comprises VH CDR 1, 2 and 3 of SEQ ID NOs: 13, 14 and 15, respectively and VL CDR 1, 2, and 3 of SEQ ID NOs: 18, 19 and 20, respectively.
An anti-tau antibody that recognizes an epitope of phosphorylated tau peptide pT212/pS215 (SEQ ID NO: 34), wherein the antibody comprises VH CDR 1, 2 and 3 of SEQ ID NOs: 23, 24 and 25, respectively and VL CDR 1, 2, and 3 of SEQ ID NOs: 28, 29 and 30, respectively.
A multi-database, fused CDR search was performed on each of the VH and VL CDR triplets of the instant claimed anti-tau antibodies. No complete matches were found that would qualify as prior art and the table below depicts the next nearest prior art for each of the VH and VL CDR triplets:
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All of the next nearest prior art sequences identified were from antibodies but none of the next nearest prior art sequences originated from an anti-tau antibody binding any epitope on tau. As such, one of ordinary skill in the art would not be motivated to start with any of the next nearest prior art sequences originating from non-tau binding antibodies and modify the amino acid sequence(s) to form any antibody binding any epitope on tau. As such, the anti-tau antibodies described above are free of prior art.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claim 1-14 and 16-17 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of copending Application No. 18/259,734 (Published as US 20240309076-A1 on 9/19/2024).
Although the claims at issue are not identical, they are not patentably distinct from each other because the copending claims are directed to AAV genomes comprising expression cassettes encoding the same anti-tau antibodies as the instant application. These AAV expression cassettes would therefore inherently produce the same anti-tau antibodies as the instant application when the adeno associated virus infects a cell.
Regarding instant claims 1-3, 7, 9, 12, 14 and 16-17, the copending claims are directed to AAV expression vectors that encode (and would inherently produce) an anti-tau antibody that recognizes the phosphorylated tau peptide pS202/pT205 of copending SEQ ID NO: 122 (same as instant SEQ ID NO: 33) (copending claim 1), wherein said anti-tau antibody comprises VH CDR 1, 2 and 3 of copending SEQ ID NOs: 160, 161 and 162, respectively (same as instant SEQ ID NOs: 13, 14 and 15, respectively) and VL CDR 1, 2 and 3 of copending SEQ ID NOs: 163, 164 and 165, respectively (same as instant SEQ ID NOs: 18, 19 and 20, respectively) (copending claim 2) and wherein the anti-tau antibody comprises VH and VL sequences of copending SEQ ID NOs: 99 and 100, respectively (same as instant SEQ ID NOs: 12 and 17, respectively) (copending claim 3. Regarding instant claim 4, the antibody described in the previous sentence comprises VH and VL sequences identical to instant claimed antibody NI-502.31B6, which, as evidenced by the instant Specification, would inherently bind tau peptide pS202/pT205 with an EC50 of 2.0 nm (Specification, p 4, lines 1-6). Regarding instant claim 5, copending claim 4 is directed to anti-tau antibodies further comprising heavy and light chain constant regions. Regarding instant claim 6, copending claim 6 is directed to anti-tau scFvs. Regarding instant claim 8, copending claim 1 is directed to polynucleotide sequences operably linked to heterologous expression control sequences. Regarding instant claims 10-11, copending claims 14-15 are directed to host cell comprising the copending AAV polynucleotides as well as methods of producing AAVs that would inherently produce antibodies identical to the instant claimed anti-tau antibodies comprising culturing said host cells followed by isolation of AAVs. Regarding instant claim 13, copending claim 12 is directed to AAV expression vectors that are contained in a vehicle that is an AAV capsid.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
Claims 1-19 are rejected.
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Sydney Van Druff whose telephone number is (571)272-2085. The examiner can normally be reached 10 am - 6 pm.
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/SYDNEY VAN DRUFF/ Examiner, Art Unit 1643
/JULIE WU/ Supervisory Patent Examiner, Art Unit 1643