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 .
Election/Restrictions
Claim 1 recites the following structures:
VH1-CHa (species A)-Fc1 (species B)
VL1-CLb (species C)
VH2-CH1-Fc2 (species D), and
VL2-CL (see claim 1 lines 2-3).
In the Restriction mailed 23 February 2026, Applicant was to elect the structures in bold. Applicant’s response to the Restriction received 22 April 2026 (referred to herein as Remarks) is hereby acknowledged and addressed below. Applicant has elected the following:
VH1-IgG CH3 (S354C/T366S/L368A/Y407V), disulfide bond (Seq ID No: 13)-Linker (Seq ID No: 27)-IgG CH1 (Seq ID No: 5)-IgG CH2-IgG CH3 (Y349C/T366S/L368A/Y407V), disulfide bond (Seq ID No: 11) (see Remarks pg. 3, last 2 para),
VL1-CH3 (Y349C/T366W), disulfide bond (Seq ID NO: 12)-Linker (Seq ID No: 27)-CL1 (Seq ID NO: 15) (see Remarks pg. 4, 1st para), and
VH2-CH1-IgG CH2-IgG CH3 (S354C/T366W), disulfide bond (Seq ID No: 10) (see Remarks pg. 4, 2nd para).
It is noted that Applicant has also elected Structure Q-SBL9 (see specification figure 15; see Remarks pg. 3, top). However, this structure is at odds with Applicant’s election. For example, figure 15 has VH2-CH3-linker-CH1 while Applicant has elected this particular embodiment for VH1. Therefore, in the interest of compact prosecution Examiner will used the elections set forth above as the election of Species A-D while using Structure Q-SBL9 as a guide (i.e., not the election of Species) for searching the prior art. During the course of examination the Examiner found 35 USC 102(a)(1) art regarding the specific embodiment wherein Species A and C are IgM CH3 domains. Therefore, regarding this particular embodiment (wherein the CH3 domain of the CHa and CLb domain comprises IgM) is hereby rejoined.
Priority
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
Status of the Claims
Claims 1-28 were originally filed 26 June 2023. The preliminary amendment filed the same day has been entered. Election was made without traverse in the reply filed on 22 April 2026.
Claims 1-3, 5, 6, 8-12, 14-16, 18, 20-22, 24, 25, and 27 are currently pending and under consideration.
Specification
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code. Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01. For example, see specification pg. 25 top.
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 1-3, 6, 9-12, 14-16, 18, 20-22, 24, 25, and 27 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 1 and 14 are drawn to a bispecific antibody comprising “a first arm binding” and “a second arm binding” in lines 2 and 3. The scope of the first and second arm is unclear. For example, the first arm comprises VH1-CHa-Fc1. It is unclear if this is a generic name for a structure, the order of domains on a polypeptide, or alternatively a formula with attachment sites. It is unclear if VH1-CHa-Fc1 and VL1-CLb are meant to be separate structures as and would suggest or separate regions on a single polypeptide. The scope of the second arm is unclear of the same reasons. In addition, the claim is drawn to VH1, VH2, VL1, and VL2. It is unclear if VH1 and VL1 are a pair as convention would suggest or is the claim encompass wherein both VH1 and VL1 bind the same target but have separate variable region pairings given the claim says VH1 and VH2 can bind separate targets and similarly VL1 and VL2. Furthermore, the preamble recites “a bispecific antibody” in the preamble while also reciting the VH1 and VH2 or VL1 and VL2 can bind the same antigen. It is unclear how the antibody can be a “bispecific antibody” and bind the same target (see also claim 14). Furthermore, claims 1 and 14 are drawn to “same or different antigen binding regions”. It is unclear if the claims are drawn to variable regions with the same CDRs or alternatively the entire variable region sequence (e.g., VH) is the same. It is unclear if both antigen binding domains have the same CDRs but different framework sequences are these antigen binding domains within the scope of “same” or alternatively “different”.
In addition, the scope of the CHa domain in claim 1 is unclear regarding the CH1 domain. For example, is the CHa domain drawn to comprising an IgG heavy chain constant region (i.e., CH1, CH2, or CH3) or alternatively comprising an IgG CH1 domain given the following clause is linked by “or” and describes a CH1 domain.
In addition, claim 1 and 14 are drawn to “the CLb comprises i) a CL1 including an IgG light chain constant region” in line 10. It is unclear if “including” an IgG light chain constant region is an example of a CL1 or in addition to a CL1. The same ambiguity regarding “including” is present in claims 1 and 14 regarding the VH and VL regions.
Claim 1 and 14 recite the limitation "the CH1" in line 13 or 12, respectively. There is insufficient antecedent basis for this limitation in the claim. For example, in claim 1 is “the CH1” referring to the CH1 recited in line 3, 8, or line 11. In the case of line 8, it is unclear how the CHa can comprise an IgD CH1 region.
In addition, claim 1 is drawn to “CL is an IgG light-chain constant region CL”. It is unclear how a CL can be defined by itself.
Claims 3, 6, 11, 12, 18, and 21 are drawn to particular substitutions in the Fc region of the antibody. It is unclear if the substitutions are identified relative to a particular Seq ID No. or according to a particular numbering scheme.
Claim 6 is drawn to a light chain constant region (CL1) comprising IgG 1-4, IgD, or IgM. The light chain constant region typically comprises a λ or κ chain and therefore it is unclear how the CL1 can comprise IgG 1-4, IgD, or IgM.
Claim 10 is drawn to wherein the CHa and CLb each comprise CH3. It is unclear if this the CH3 recited in claim 1 or in addition to the CH3 recited in claim 1.
Claim 11 recites the limitation "the dimers" in line 1, “the CH3 dimers” in line 6, and “the Fc” in line 6. There is insufficient antecedent basis for these limitations in the claim. Claim 1 refers to multiple CH3 domains and it is unclear which CH3 domain claim 11 refers to (e.g., an IgG CH3 or IgM CH3). In addition, claim 1 recites an Fc1 and an Fc2.
Claims 11 and 18 are drawn to “one of the dimers formed by bonding CH3” in line 1 or 2, respectively. The language is unclear. For example, is the claim drawn to two CH3 domains which have dimerized, or alternatively, is the claim drawn to the bonds between individual amino acids in a single CH3 domain. Claim 11 also recites two lists of substitutions in the first paragraph (see lines 3-5). It is unclear if ½ of a dimer must have at least one substitution from both lists, or alternatively, is the first list associated with a first half of the dimer and the second list associated with the second half of the dimer.
Claim 12 is drawn to “any one of CH3 of CHa and CH3 of CLb” in lines 2 and 4. It is unclear if the claim is drawn to any one of CH3 of CHa or CH3 of CLb, or alternatively, to wherein both the CH3 of CHa and the CH3 of CLb comprise the recited substitutions.
Claim 16 is drawn to a CL3 domain. The scope of the CL3 domain is unclear given the independent claim is drawn to a CH1 and CL1 pairing.
Claim 22 is drawn to “Cha” in line 1. It is unclear what Cha is referring to or if Applicant meant CHa.
Claim 22 is drawn to wherein the CH3 and CH1 of CHa and CH3 and CL1 of CLb are linked via a linker. It is unclear if the claim is drawn to a linker between each of the domains (e.g., CH3-linker-CH1-linker-CH3-linker-CL1), or alternatively, a single linker, or alternatively 2 linkers.
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.
Claim 2, 3, 6, 15, and 24 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 2 and 15 are drawn to wherein the CHa and CLb domains comprise IgG1-4, IgD, or IgM. Claim 1 (from which claim 2 depends) and claim 14 (from which claim 15 depends) are drawn to either a CLb comprising IgG and IgM domains and a CHa domain comprising IgG, IgD, or IgM (see claim 1) while claim 14 is drawn to wherein the CHa and CLb comprise IgG domains. Therefore, claim 2 does not further limit claim 1 while claim 15 expands the scope of claim 14.
It is also noted, in regards to claim 2 and the CLb domain it is unclear if claim 2 expands the scope given claim 1 which limits the CLb domain to IgG and IgM.
Claim 3 is drawn to CHa domains comprising a CH1 and CH3 domain (see claim 1 i))wherein the CH1 and CH3 domains are an IgG1-4, IgD, or IgM. Claim 1 limits the constant regions, specifically the CH1 to IgG and IgD and limits the associated CH3 domains to IgG. Therefore, claim 3 expands the scope of the CH1 and CH3 domains recited in claim 1.
Claim 6 is drawn to wherein CLb comprises a CL1 and CH3 domains (see claim 1 second i)) comprising IgG 1-4, IgD, or IgM. Claim 1 limits CLb regions comprising CL1 to IgG κ or λ and CH3 domains to IgG; therefore, claim 6 expands the scope of the CL1 and CH3 regions.
Claim 24 is drawn to wherein the bispecific antibody either has a disulfide bond in the CH3 domain or does not have a disulfide bond. Claim 24 does not further limit the structure of claims 14 and 22.
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.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1-3, 5, 6, 8, 10, and 11 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Wozniak (see US PG Publication 2018/0016354 A1, as cited on the IDS received 06/23/2023).
Wozniak broadly discloses domain exchange antibodies (see Wozniak abstract). Bispecific antibodies depends heavily on dimerization of heavy chains mediated by homodimer association of CH3 domains (Wozniak pg. 2 para [0014]). Wozniak discloses several bispecific structures wherein one antigen binding domain comprises paired CH3 domains (see Wozniak figures 1A 1-8, 1B 1-4, 7, and 8, 1C 1-4, 7, and 8, 21 1-5). For example, Wozniak discloses one particular embodiment:
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(see Wozniak figure 1B-2).
Wozniak discloses the following regarding the structures:
“Alternatively, the CH3HET domain is anto of a human or humainized IgG2, IgG3, IgG4, IgA, IgM, IgE, or IgD antibody, or a functional variant of such CH3 domain” (see Wozniak pg. 4 para [0072]).
Regarding the knob-in-holes substitutions and disulfide bridges:
“one or more knob or hole mutations, preferably any of T366Y/Y407′T, F405A/T394′W, T366Y:F405A/T394′W:Y407′T, T366W/Y407′A and S354C:T366W/Y349′C:T366′S:L368′A:Y407′V” (see Wozniak pg. 5 para [0089], emphasis added; see also pg. 15 para (0274-0279]), and
“ a cysteine residue that is covalently linked to a cysteine residue of the other cognate CH3 domain, thereby introducing an interdomain disulfide bridge, preferably linking the c-terminus of both CH 3 domains” (see Wozniak pg. 5 para [0090]).
This is pertinent to instant claims 1-3, 5, 6, 8, 10, and 11.
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 text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1-3, 6, 9-12, 14-16, 18, 21, 22, 24, 25, and 27 are rejected under 35 U.S.C. 103 as being unpatentable over Wozniak (see US PG Publication 2018/0016354 A1, as cited on the IDS received 06/23/2023) and Taylor (see US PG Publication 2014/0341906).
Wozniak broadly discloses domain exchange antibodies (see Wozniak abstract). Bispecific antibodies depends heavily on dimerization of heavy chains mediated by homodimer association of CH3 domains (Wozniak pg. 2 para [0014]). Wozniak discloses several bispecific structures wherein one antigen binding domain comprises paired CH3 domains (see Wozniak figures 1A 1-8, 1B 1-4, 7, and 8, 1C 1-4, 7, and 8, 21 1-5). For example, Wozniak discloses one particular embodiment:
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(see Wozniak figure 1B-2).
Wozniak discloses the following regarding the structures:
“Specifically, any or each of the CH3 domains is a IgG1 CH3 domains, specifically characterized by a human IgG1 CH3 sequence or an engineered variant thereof comprising one or more point mutations, preferably up to 10 point mutations” (see Wozniak pg. 2 para [0027]).
Regarding the knob-in-holes substitutions and disulfide bridges:
“one or more knob or hole mutations, preferably any of T366Y/Y407′T, F405A/T394′W, T366Y:F405A/T394′W:Y407′T, T366W/Y407′A and S354C:T366W/Y349′C:T366′S:L368′A:Y407′V” (see Wozniak pg. 5 para [0089], emphasis added; see also pg. 15 para (0274-0279]), and
“ a cysteine residue that is covalently linked to a cysteine residue of the other cognate CH3 domain, thereby introducing an interdomain disulfide bridge, preferably linking the c-terminus of both CH 3 domains” (see Wozniak pg. 5 para [0090]).
Wozniak also discloses,
“In order to allow proper pairing of the immunoglobulin chains or domains, any of the CH3 mutations may specifically be employed, e.g., the knobs-into-holes technology, the SEED technology, charge repulsion technology, disulfide linkage or the cross-mAb technology can be used in order to reduce the amount of not correctly associated molecules” (see Wozniak pg. 15 para [0282]).
Taylor discloses polypeptides comprising heterodimeric Fc regions specifically engineered to promote efficient dimerization (see Taylor abstract, pg. 1 para [0001]). Taylor teaches there is a need for Fc-containing binding molecules which can be produced and isolated efficiently and robustly while retaining desired Fc effector functions and providing desired valencies and specificities (see Taylor pg. 1 para [0004]). The disclosed structures take advantage of the spontaneous pairing between a CH1 moiety in a first polypeptide chain and a CL moiety in a second polypeptide chain (see Taylor pg. 1 para [0005]). The heterodimeric binding molecules of the invention are operably linked to a target binding moiety such as a Fab or scFv (see Taylor pg. 1 para [0007]). Taylor discloses the following structure to illustrate the concept:
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(see Taylor Figure 10D).
More specifically, wherein a multivalent binding molecule comprises the following: a first polypeptide: binding moiety-Fc-CL and second polypeptide: binding moiety-Fc-CH1 wherein the first and second polypeptides form a heterodimeric Fc region via CL:CH1 (see Taylor pg. 3 para [0056-0058]). The Fc portion of both the first and second polypeptide can be a CH3 or a portion of a CH3 domain (see Taylor pg. 3 para [0062]). Taylor also teaches a particular embodiment further comprises additional Fc regions:
“In one embodiment, the first polypeptide chain further comprises at least one Fc moiety operably linked to the C-terminus of the CL moiety (Fc-CL-Fc) and said second polypeptide chain further comprises at least one Fc moiety operably linked to the C-terminus of the CH1 moiety (Fc-CH1-Fc)” (see Taylor pg. 2 para [0017]; see also figure 10B).
The heterodimeric Fc regions link the Fc moiety to the FAB constant region (i.e., CH1 or CL) via a synthetic linker, specifically a glycine serine linker wherein the linker is a G4Sn wherein n=1-6 (see Taylor pg. 14 para [0202], pg. 17 para [0231]).
Therefore, at the time of filing the ordinary artisan would have recognized there were several established techniques for enhancing the preferred pairing of bispecific antibodies. Therefore, the ordinary artisan would combine the structure taught by Wozniak (see below, normal text) with a CH1-CL1 dimerization domain after the CH3 domain as taught by Taylor (see below, bold text) in order to further increase efficient production of the bispecific antibody while maintaining desirable Fc functions.
The combination results in the following:
First polypeptide: VL1-CH3 (knob)-CL1
Second polypeptide: VH1-CH3 (hole)-CH1-hinge-CH2-CH3 (hole)
Third polypeptide: VH2-CH1-hinge-CH2-CH3 (knob)
Forth polypeptide: VL2-CL2
Both Wozniak and Taylor disclose methods for enhancing preferential pairing of light and heavy chains in bispecific antibodies. Therefore, the ordinary artisan would be using known methods to yield predictable results. There is a reasonable expectation of success given Taylor discloses heterodimeric Fc molecules comprising a single Fc moiety fused to a FAB constant region had favorable pairing over the heterodimeric Fc molecules comprising 2 Fc moieties fused to a FAB constant region (see Taylor example 5 starting on pg. 68 para [0534]). Wozniak discloses the bispecific antibodies comprising a CH3 domain swap for a FAB constant region showed a “predominantly a single band with a molecular weight corresponding to the expected size for both domain exchanged antibody 1 and 2” (see Wozniak pg. 22 para [0361], figure 2A). Additional experiments demonstrate the CH3 domain did not interfere with the ability of the antibody to bind the relevant target (see Wozniak pg. 23 para [0373-0375]). This is pertinent to claims 1-3, 6, 11, 12, 14, 15, 18, 21, 22, 25, and 27.
Regarding claims 9, 10, 16, and 24 Taylor teaches the Fc-CH1 and Fc-CL heterodimerization can be further stabilized with a disulfide bridge but does not require one (see Taylor para [0024]). In addition, Wozniak teaches a disulfide bridge in the CH3 region (see Wozniak pg. 5 para [0090]). In fact, Taylor teaches it is the spontaneous pairing of the CH1 moiety and the CL moiety which is advantageous to efficient heterodimerization (see Taylor pg. 1 para [0005]).
Claims 1-3, 6, 9-12, 14-16, 18, 21, 22, 24, 25, and 27 are rejected under 35 U.S.C. 103 as being unpatentable over Wozniak (see US PG Publication 2018/0016354 A1, as cited on the IDS received 06/23/2023), Taylor (see US PG Publication 2014/0341906), and Bennett (see US PG Publication 2018/0179285 A1).
The reasons claim 14 are obvious are set forth above.
Bennett discloses engineered heterodimeric proteins which are more efficiently produced (see Bennett abstract, pg. 1 para [0005]). Bennett teaches on method for facilitating the proper folding and association of heterodimeric formation is with sterically complementary mutations in multimerization domains at the CH3 domain interface, referred to as a “knobs-into-holes” strategy well known in the art at the time (see Bennett pg. 1 para[0007]). As such, Bennett discloses a bispecific structure comprising a CH3 domain with “knob-into-holes” substitutions identical to those taught by Wozniak and further comprising a disulfide bridge as taught by Wozniak in Seq ID No: 47 (see Bennett pg. 19 para [0173], pg. 27 para [0270], Figure 22, Seq ID N:47; see sequence comparison below).
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(see Bennet Figure 22)
Bennett discloses the “knobs-into-holes” substitutions were made to “bias heavy chain heterodimerization (see Bennett pg. 63 para [0389]).
Therefore, the ordinary artisan would modify the Fc region taught by Wozniak to further comprise specifically the S354C/T366S/L368A/Y407V (elected; disulfide bridge and Knob-into-holes) substitutions also taught by Wozniak given Bennett discloses a bispecific antibody comprising the same substitutions and disulfide bridge for the same purpose (i.e., increasing favorable heterodimerization of polypeptides in antibodies). There is a reasonable expectation of success given the structure disclosed by Bennett was functional (see Bennett pg. 64 example 19).
Sequence Comparison
(Qy) Instant Seq ID No: 13 (Db) Bennett Seq ID No: 47
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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.
Claims 1-3, 6, 9, 11, 12, 18, 21, 22, and 25 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 10, 17, 18, and 20 of copending Application No. 19/487414 (referred to herein as ‘414 application). Although the claims at issue are not identical, they are not patentably distinct from each other.
The ‘414 application claim 10 is nearly identical to instant claim 1 except for claiming particular substitutions at the end of the claim. This is pertinent to instant claims 1-3, 6, 9, and 14-16. In addition, the ‘414 claims the identical Fc substitutions as instant claims 11, 12, 18, 21 (see ‘414 claim 18). The ‘414 application also claims a linker regarding the CH3:CH1 and CH3:CL domains (see ‘414 claim 18; see instant claim 22) and claims a hinge region (see ‘414 application claim 20; see instant claim 25).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 1-3, 6, 9, 11, 12, 18, 20-22, and 25 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 10, 17, 18, and 20 of copending Application No. 19/487414 (referred to herein as ‘414 application), Wozniak, Taylor, and Bennett. Although the claims at issue are not identical, they are not patentably distinct from each other.
The reasons claims 1 and 14 are anticipated by the ‘414 application are set forth above.
The teachings of Wozniak, Taylor, and Bennett are set forth above.
Therefore the ordinary artisan would have modified the claimed structure of the ‘414 application comprising a first part VH1-(CH3-CH1, any order)-Fc1 and a second part VL1-(CH3-CL, any order)-Fc with the teachings of Wozniak and Taylor thereby arriving at the instantly elected structure VH1-CH3-CH1-Fc1 and a second part VL1-CH3-CL-Fc given the order of domains is taught by Taylor as a method to facilitate proper dimerization of domains in bispecific antibodies by taking advantage of the favorable pairing of CH1 and CL domains. Wozniak teaches the CH3 domain also biases antibody dimerization increasing the efficiency of antibody production.
Regarding claim 20, Bennett discloses a functional bispecific antibody wherein the specifically claimed substitutions of the ‘414 application and taught by Wozniak were used to bias heterodimerization of a bispecific antibody.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
No claim allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to HILARY ANN PETRASH whose telephone number is (703)756-4630. The examiner can normally be reached Monday-Friday 8:30-4:30 EST.
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/H.A.P./Examiner, Art Unit 1644
/AMY E JUEDES/Primary Examiner, Art Unit 1644
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