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 .
1. Claims 1-12 and 15-17 are pending and being examined.
Claim Objections
2. Claim 3 is objected to because of the following informalities: claim 3 recites a typo “third targe” where the “t” is missing in “target”. Appropriate correction is required.
3. Claim 7 is free of the art but is objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims. The combination of the three chain sequences for the hexavalent trispecific antibody recited in claim 7 appear to be free of the prior art.
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.
4. Claims 4, 6, 8-11, 16, and 17 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.
Regarding claim 4, a broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) may be considered indefinite if the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c). In the present instance, claim 4 recites the broad recitation of a peptide linker of 1-35 amino acids in length, and the claim also recites “preferably a peptide linker of 6-30 amino acids in length”, which is the narrower statement of the range/limitation. The claim(s) are considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims.
Regarding claim 6, a broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) may be considered indefinite if the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c). In the present instance, claim 6 recites the broad recitation of a flexible peptide linker comprising 6-30 amino acids, and the claim also recites “preferably 10-25 amino acids”, which is the narrower statement of the range/limitation. The claim(s) are considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims.
Claim 8 recites “An isolated nucleic acid molecule, wherein the nucleic acid molecule encodes a hexavalent trispecific antibody of claim 1”. The language of claim 8 implies there are multiple antibodies of claim 1 and claim 8 is further limiting one of them, however, there is only one hexavalent trispecific antibody recited in claim 1, rendering claim 8 unclear as to what specific antibody it is referring to. Claims 9-11 are rejected for encompassing the rejected limitation of claim 8. Examiner suggests changing the word “a” to “the” in claim 8 to specifically refer back the antibody of claim 1.
Claim 11 recites a method comprising steps of: “(a) culturing the host cell of claim 10 to express the hexavalent trispecific antibody; (b) separating and purifying the hexavalent trispecific antibody described in (a).” Claim 11 is unclear with regard to whether both steps (a) and (b) are required by the method or if they are alternatively required because there is no conjunction word “and” or “or” between the two steps. Examiner suggests amending claim 11 to add the word and between steps (a) and (b)
Claim 11 recites “the hexavalent trispecific antibody described in (a)”. There is insufficient antecedent basis for this limitation in the claim. It is unclear what antibody the claim is referencing because no hexavalent trispecific antibody was “described” in part (a), but rather, a hexavalent trispecific antibody was expressed by cultured cells. Examiner suggests amending claim 11 part (b) to recite “(b) separating and purifying the hexavalent trispecific antibody expressed in (a)”.
Claim 16 recites “its immune conjugate”. There is insufficient antecedent basis for this limitation in the claim.
Claim 17 recites: “the cancer is selected from the following groups: melanoma, renal cancer, prostate cancer, …glioma, and other vegetative malignant diseases.” The claim is unclear with regard to what plurality of groups the cancer is selected from because there is only one list or one group of cancers recited in the claim. Additionally, the claim is unclear with regard to what constitutes “other vegetative malignant diseases” when no initial vegetative malignant diseases were recited in the claim. The metes and bounds of the claimed invention cannot be determined. Examiner suggests amending claim 17 to recite: “The method of claim 16, wherein the cancer is selected from the group consisting of: melanoma, renal cancer, prostate cancer, …glioma, and vegetative malignant diseases.”
Claim Rejections - 35 USC § 103
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.
5. Claim(s) 1, 2, 4, 6, 8-12, 15, and 16 are rejected under 35 U.S.C. 103 as being unpatentable over US Patent Application Publication 2021/0163620, Granda et al, published June 3, 2021 and claiming priority to April 2018; in view of Bhatta et al (Antibodies, 2018, 7:35, p. 1-16).
Granda teaches a hexavalent trispecific antibody construct that simultaneously binds three different targets A, B, and C, comprising:
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formed by two polypeptides: one tandem VL polypeptide (VLA-VLB-VLC-CL) and one tandem VH polypeptide (VHA-VHB-VHC-CH1=CH2-CH3), wherein the VL regions cooperate with their corresponding VH regions ([section 7.4.4; [311-315]).
Granda also teaches trispecific antibodies comprising the format:
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formed by separate VL polypeptides (VLX-CL, VLY-CL, and VLZ-CL) that cooperate with the corresponding heavy chain VH regions (section 7.4; [271-272]), wherein X, Y, and Z variable regions simultaneously target three different antigens X, Y, and Z.
Granda further teaches the linkers between the VH domains or between the VL domains are from 2-60 amino acids in length, including linkers from 4-30 amino acids long, or 5-25 amino acids long, including flexible linkers ([110]; section 7.3.3; [265-268]).
Granda teaches VH and VL domains can be mutated to introduce a disulfide bond between the two domains to stabilize the VL-VH association in the antibody ([113-114]).
Granda teaches variable domains bind to different antigens expressed on tumor cells and/or T cells ([315-317]; sections 7.5-7.6; Table 10).
Granda teaches nucleic acid molecules encoding the antibodies, expression vectors comprising the nucleic acids encoding the antibodies, host cells comprising the expression vectors, and methods of making the antibodies by culturing host cells comprising the vectors, expressing the antibodies, and purifying the antibodies ([80-82]; sections 7.7, 7.7.1, 7.7.2).
Granda teaches pharmaceutical compositions comprising the antibody in a pharmaceutically acceptable carrier (section 7.9).
Granda teaches antibody drug conjugates wherein the antibody is coupled to a drug or cytotoxin (section 7.8).
Granda teaches methods of treating cancer in a subject comprising administering to the subject the antibody, wherein the cancer expresses an antigen targeted by the antibody ([87-92]; section 7.10.1).
Granda does not teach the hexavalent trispecific antibody is formulated having two separate light chains: VLA-linker-VLB and VLC-CL, wherein VLB domain forms a disulfide bond with its corresponding VHB domain as in instant Figure 1:
[AltContent: textbox (Comprising three polypeptides:
VHA-Linker-VHB-Linker-VHC-CH1=CH2-CH3
VLA-Linker-VLB
VLC-CL)]
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Bhatta teaches methods of making multispecific antibodies by pairing VH-VL domains and Fab domains through disulfide linkages. In Figure 1, Bhataa teaches pairing of Fab-dsFv monomers through disulfide linkage between the VH-VL of single domains, and between the CH1 and CL linked to the VH and VL domains of a Fab region (see Figures 1A and 1C in particular):
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Bhatta suggests this technology applies to IgG formats (scaffolds) with attached dsFv/dsscFv (Figure 1; abstract).
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was effectively filed to format the trispecific hexavalent antibody of Granda with two separate light chain polypeptides, wherein the VLA-VLB polypeptide is paired to their corresponding VH domains through a disulfide linkage, and wherein the VLC-CL polypeptide is paired to its corresponding VH domain through a disulfide linkage of the CL to the CH1 of the heavy chain in Fab format. One would have been motivated to, and have a reasonable expectation of success to, because: (1) Granda suggests various formats of trispecific antibodies, including a format comprising two separate light chain polypeptides that pair with their corresponding VH domains on the single heavy chain; (2) Granda teaches that VL and VH domains can be altered to produce disulfide linkage between them for stability and demonstrates the known disulfide linkage between CL and CH1 of Fab domains; and (3) Bhatta also teaches known methods of pairing separate VH and VL domains, as well as Fabs, through disulfide linkage to create stable multispecific antibodies, and teaches this technology is applicable to IgG scaffods. Given the need to produce stable multispecific antibodies for pharmaceutical application taught by the cited references, the known technology for pairing separate light chain VL domains and Fabs to their corresponding VH domains in a single heavy chain through disulfide linkage, and the suggestion to apply this technology to IgG antibody formats, it is well within the level of the ordinary skill artisan to modify the trispecific hexavalent antibody of Granda to comprise two light chain polypeptides, VLA-VLB and VLC-CL, paired to their heavy chain VH domains and through disulfide linkage, with a reasonable expectation of success.
6. Claim(s) 3, 5, and 17 are rejected under 35 U.S.C. 103 as being unpatentable over US Patent Application Publication 2021/0163620, Granda et al, and Bhatta et al (Antibodies, 2018, 7:35, p. 1-16); as applied to claims 1, 2, 4, 6, 8-12, 15, and 16 above, and further in view of US Patent Application Publication 2012/0237442, Rossi et al, published 2012; WO2020136564, Beil et al; Wu et al (Protein Engineering, Design & Selection, 2018, Vol. 31, no. 7-8, p. 249-256); US Patent Application Publication 2018/0326054, Deak et al, published 2018; and Patel et al (Journal of Immunother. Cancer, 2020, 8(Suppl 3):A193; Abstract 313).
Granda and Bhatta (the combined references) teach a trispecific hexavalent antibody for the treatment of cancer, as set forth above. As stated above, Granda suggests the antibody target tumor antigens and T cell antigens.
The combined references do not teach treating breast, colorectal, esophageal, and ovarian cancers, or that the antibody targets PD-1, HER-2, and LAG-3 as target antigens A, B, and C, respectively.
Rossi, like Granda, teaches a hexavalent trispecific antibody comprising a first polypeptide comprising the three VH domains in tandem on the heavy chain, and a second polypeptide comprising three tandem VL domains (Figure 9; [23]):
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Rossi teaches the antibody targets tumor antigens, and suggests it targets HER2 tumor antigen ([48]; claim 15). Rossi teaches administering the antibody for the treatment of cancer, including gliomas, renal carcinoma, lung carcinoma, intestinal carcinoma, stomach carcinoma, breast carcinoma, prostate cancer, ovarian cancer, endometrial cancer, cervical cancer, bladder cancer, liver cancer, pancreatic cancer and/or melanoma ([47]; [218-219]; [224]; claim 38)
Wu teaches and demonstrates successfully making trispecific antibodies for the treatment of cancer, wherein the antibodies target tumor antigens including HER-2 and target immune checkpoint proteins including PD-1 (see Figure 1 below). Wu teaches combination of antibodies directed at immune checkpoint proteins have shown the ability to ablate tumors in mice (p. 249, col. 1).
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Beil teaches making bispecific and trispecific antibodies for the treatment of cancer (see Figures 10 and 13 below; [205]; [243-244]; [350-351]), and teaches construction of an antibody that binds to PD-1 and HER-2, with the PD-1 binding domain on the N-terminus ([121-124]; [133-134]):
Light chain:
SEQ ID NO: 32: anti-PD1-VL-(G4S)2-anti-Her2-(Trastuzumab-Q100C)-VL
Heavy chain:
SEQ ID NO: 33: anti-PD1-VH-(G4S)2-anti-Her2-(Trastuzumab-G44C)-VH-Fc-hulgG1.
It is noted that SEQ ID NO:32 shares significant homology to instant light chain SEQ ID NOs:15, 17, and 19 comprising the PD-1 VL and HER-2 VL binding regions (see sequence alignments below for SEQ ID NO:15 and 17).
Figure 10: Figure 13:
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Deak exemplifies making a PD-1 x LAG-3 bispecific IgG antibody against immune checkpoint proteins for successfully treating cancer (Examples 10-13; Figure 1A). The bispecific antibodies effectively block checkpoint molecules PD1 and LAG3 on T cells, rescue T cell effector functions from Treg suppression, show increased tumor-specific T cell effector functions, and increase tumor eradication in vivo ([6]; [7]). Deak teaches treatment of cancer includes bladder cancer, brain cancer, head and neck cancer, pancreatic cancer, lung cancer, breast cancer, ovarian cancer, uterine cancer, cervical cancer, endometrial cancer, esophageal cancer, colon cancer, colorectal cancer, rectal cancer, gastric cancer, prostate cancer, blood cancer, skin cancer, squamous cell carcinoma, bone cancer, and kidney cancer ([241]; [631]) Deak suggests the antibody can be formatted as trispecific, additionally binding a third antigen ([519-531]).
Patel teaches a PD-1 x LAG-3 bispecific successfully clinically treating HER2+ cancer patients in combination with an Fc-engineered anti-HER-2 antibody, wherein the cancer patients include breast, colorectal, esophageal, and ovarian. Patel teaches in vitro studies demonstrate that the HER2 antibody results in upregulation of PD-1/LAG-3 expression on immune cells and the combination of HER2 antibody and PD-1 x LAG-3 bispecific antibody results in enhanced lytic activity of immune cells on HER2+ cancer cells (see entire abstract).
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was effectively filed for the hexavalent trispecific antibody of the combined references to bind PD-1, HER-2, and LAG-3, and as antigen A, B, and C, respectively. One would have been motivated to, and have a reasonable expectation of success to because: (1) the combined references teach utilizing the hexavalent trispecific antibody as a pharmaceutical to treat cancer and to simultaneously bind thee antigens, including tumor antigens or T cell antigen; (2) Rossi, Beil, and Wu suggest making and using trispecific antibodies for the treatment of cancer that bind to HER-2 and/or PD-1; (3) Deak and Patel teach and demonstrate that an antibody binding to both T cell check point proteins PD-1 and LAG-3 successfully treats cancer, effectively blocks checkpoint molecules PD1 and LAG3 on T cells, rescues T cell effector functions from Treg suppression, and shows increased tumor-specific T cell effector functions; and (4) Patel demonstrates that the combination of inhibition of HER-2, PD-1, and LAG-3 by antibody binding successfully treats HER2+ cancer clinically, and in vitro studies demonstrate combination enhances lytic activity of immune cells on HER2+ cancer cells. Given the need taught by the prior art to treat cancer by simultaneously targeting antigens with a hexavalent trispecific antibody, the suggestion to target all of HER-2, PD-1, and LAG-3 for treatment, and the known and successful treatment of HER2+ cancer and killing of cancer cells by targeting all of HER-2, PD-1, and LAG-3 with antibodies, one of ordinary skill in the art could have predictably and successfully pursued making a hexavalent trispecific antibody binding to PD-1, HER-2, and LAG-3 antigens and in any order of binding.
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was effectively filed for the combined references to treat HER2+ cancers including breast, colorectal, esophageal, and ovarian cancers. One would have been motivated to, and have a reasonable expectation of success to because: (1) the combined references and Wu suggest treating cancer targeted by the hexavalent trispecific antibody; (2) Rossi, Beil, Deak, and Patel suggest treating breast, colorectal, esophageal, and ovarian cancers and targeting any of HER-2, PD-1, and/or LAG-3; and (3) Patel demonstrates successfully treating breast, colorectal, esophageal, and ovarian HER2+ cancers by inhibiting HER-2, PD-1, and LAG-3 with antibodies.
Instant PD-1-HER-2 light chain SEQ ID NO:15 aligned with Beil SEQ ID NO:32:
RESULT 4
BHY42698
ID BHY42698 standard; protein; 224 AA.
XX
AC BHY42698;
XX
DT 20-AUG-2020 (first entry)
XX
DE Anti-PD1-VL-(G4S)2-anti-Her2-(Trastuzumab-Q100C)-VL, SEQ ID 32.
XX
KW Erbb2 tyrosine kinase receptor; Her2 protein; PD-1 protein; antibody;
KW antibody production; antibody therapy; cancer; cytostatic;
KW immunoglobulin kappa; light chain variable region; mutein;
KW prophylactic to disease; therapeutic; trastuzumab;
KW tyrosine-protein kinase erbB-2.
XX
OS Unidentified.
OS Synthetic.
XX
CC PN WO2020136564-A1.
XX
CC PD 02-JUL-2020.
XX
CC PF 23-DEC-2019; 2019WO-IB061304.
XX
PR 24-DEC-2018; 2018EP-00306840.
PR 21-JUN-2019; 2019EP-00305813.
XX
CC PA (SNFI ) SANOFI.
XX
CC PI Beil C, Engel K, Hessler G, Hoelper S, Lange C, Langer T;
CC PI Lemoine C, Leuschner W, Oezguer Bruederle S, Rao E, Spindler N;
CC PI Weil S;
XX
DR WPI; 2020-594090/057.
XX
CC PT New binding protein comprising pseudo-antibody binding fragment portion,
CC PT and first stabilized knockout domain paired with first stabilized
CC PT knockout domain to form first stabilized knockout domain, used e.g. to
CC PT treat cancer.
XX
CC PS Example 3; SEQ ID NO 32; 164pp; English.
XX
CC The present invention relates to a novel binding protein, useful for
CC treating disorder in which antigen activity is detrimental. The binding
CC protein comprises at least one pseudoFab portion, where the pseudoFab
CC portion comprises: (a) a first light chain variable region VL domain
CC (VLa) paired with a first heavy chain variable region VH domain (VHa) for
CC forming a first functional antigen binding site that binds target antigen
CC A; and (b) a first stabilized knockout VH domain (VHX) paired with a
CC first stabilized knockout VL domain (VLX) for forming a first stabilized
CC knockout domain. The invention further relates to: (1) a multispecific
CC binding protein comprising a first pseudoFab portion, and a first Fab
CC portion; (2) an antigen binding protein comprising six polypeptide chains
CC that form four antigen binding sites; (3) a nucleic acid molecule
CC comprising a nucleotide sequence encoding the binding protein; (4) an
CC expression vector comprising the nucleic acid molecule; (5) a host cell
CC comprising the nucleic acid molecule, or the expression vector; (6) a
CC method for producing the binding protein; (7) a pharmaceutical
CC composition comprising a pharmaceutically acceptable carrier and a
CC therapeutically effective amount of the multispecific binding protein;
CC and (8) a method for treating disorder in which antigen activity is
CC detrimental. The novel binding protein of the invention can be used for
CC treating and preventing cancer.
XX
SQ Sequence 224 AA;
Query Match 89.8%; Score 1075.5; Length 224;
Best Local Similarity 91.3%;
Matches 209; Conservative 7; Mismatches 8; Indels 5; Gaps 1;
Qy 1 EIVLTQSPATLSLSPGERATLSCRASQSISNFLHWYQQKPGQAPRLLIKYASQSISGIPA 60
||||||||||||||||||||||||||||:|::| |||||||||||||| || :||||
Db 1 EIVLTQSPATLSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASNRATGIPA 60
Qy 61 RFSGSGSGTDFTLTISSLEPEDFAVYFCQQSNSWPHTFGQGTKVEIKGGGGSGGGGSGGG 120
||||||||||||||||||||||||||:||||::|| ||||||||||| ||||||||
Db 61 RFSGSGSGTDFTLTISSLEPEDFAVYYCQQSSNWPRTFGQGTKVEIK-----GGGGSGGG 115
Qy 121 GSDIQMTQSPSSLSASVGDRVTITCRASQDVNTAVAWYQQKPGKAPKLLIYSASFLYSGV 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 116 GSDIQMTQSPSSLSASVGDRVTITCRASQDVNTAVAWYQQKPGKAPKLLIYSASFLYSGV 175
Qy 181 PSRFSGSRSGTDFTLTISSLQPEDFATYYCQQHYTTPPTFGQGTKVEIK 229
||||||||||||||||||||||||||||||||||||||||| |||||||
Db 176 PSRFSGSRSGTDFTLTISSLQPEDFATYYCQQHYTTPPTFGCGTKVEIK 224
Instant PD-1-HER-2 light chain SEQ ID NO:17 aligned with Beil SEQ ID NO:32:
RESULT 4
BHY42698
ID BHY42698 standard; protein; 224 AA.
XX
AC BHY42698;
XX
DT 20-AUG-2020 (first entry)
XX
DE Anti-PD1-VL-(G4S)2-anti-Her2-(Trastuzumab-Q100C)-VL, SEQ ID 32.
XX
KW Erbb2 tyrosine kinase receptor; Her2 protein; PD-1 protein; antibody;
KW antibody production; antibody therapy; cancer; cytostatic;
KW immunoglobulin kappa; light chain variable region; mutein;
KW prophylactic to disease; therapeutic; trastuzumab;
KW tyrosine-protein kinase erbB-2.
XX
OS Unidentified.
OS Synthetic.
XX
CC PN WO2020136564-A1.
XX
CC PD 02-JUL-2020.
XX
CC PF 23-DEC-2019; 2019WO-IB061304.
XX
PR 24-DEC-2018; 2018EP-00306840.
PR 21-JUN-2019; 2019EP-00305813.
XX
CC PA (SNFI ) SANOFI.
XX
CC PI Beil C, Engel K, Hessler G, Hoelper S, Lange C, Langer T;
CC PI Lemoine C, Leuschner W, Oezguer Bruederle S, Rao E, Spindler N;
CC PI Weil S;
XX
DR WPI; 2020-594090/057.
XX
CC PT New binding protein comprising pseudo-antibody binding fragment portion,
CC PT and first stabilized knockout domain paired with first stabilized
CC PT knockout domain to form first stabilized knockout domain, used e.g. to
CC PT treat cancer.
XX
CC PS Example 3; SEQ ID NO 32; 164pp; English.
XX
CC The present invention relates to a novel binding protein, useful for
CC treating disorder in which antigen activity is detrimental. The binding
CC protein comprises at least one pseudoFab portion, where the pseudoFab
CC portion comprises: (a) a first light chain variable region VL domain
CC (VLa) paired with a first heavy chain variable region VH domain (VHa) for
CC forming a first functional antigen binding site that binds target antigen
CC A; and (b) a first stabilized knockout VH domain (VHX) paired with a
CC first stabilized knockout VL domain (VLX) for forming a first stabilized
CC knockout domain. The invention further relates to: (1) a multispecific
CC binding protein comprising a first pseudoFab portion, and a first Fab
CC portion; (2) an antigen binding protein comprising six polypeptide chains
CC that form four antigen binding sites; (3) a nucleic acid molecule
CC comprising a nucleotide sequence encoding the binding protein; (4) an
CC expression vector comprising the nucleic acid molecule; (5) a host cell
CC comprising the nucleic acid molecule, or the expression vector; (6) a
CC method for producing the binding protein; (7) a pharmaceutical
CC composition comprising a pharmaceutically acceptable carrier and a
CC therapeutically effective amount of the multispecific binding protein;
CC and (8) a method for treating disorder in which antigen activity is
CC detrimental. The novel binding protein of the invention can be used for
CC treating and preventing cancer.
XX
SQ Sequence 224 AA;
Query Match 90.5%; Score 1087.5; Length 224;
Best Local Similarity 91.7%;
Matches 210; Conservative 7; Mismatches 7; Indels 5; Gaps 1;
Qy 1 EIVLTQSPATLSLSPGERATLSCRASQSISNFLHWYQQKPGQAPRLLIKYASQSISGIPA 60
||||||||||||||||||||||||||||:|::| |||||||||||||| || :||||
Db 1 EIVLTQSPATLSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASNRATGIPA 60
Qy 61 RFSGSGSGTDFTLTISSLEPEDFAVYFCQQSNSWPHTFGQGTKVEIKGGGGSGGGGSGGG 120
||||||||||||||||||||||||||:||||::|| ||||||||||| ||||||||
Db 61 RFSGSGSGTDFTLTISSLEPEDFAVYYCQQSSNWPRTFGQGTKVEIK-----GGGGSGGG 115
Qy 121 GSDIQMTQSPSSLSASVGDRVTITCRASQDVNTAVAWYQQKPGKAPKLLIYSASFLYSGV 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 116 GSDIQMTQSPSSLSASVGDRVTITCRASQDVNTAVAWYQQKPGKAPKLLIYSASFLYSGV 175
Qy 181 PSRFSGSRSGTDFTLTISSLQPEDFATYYCQQHYTTPPTFGCGTKVEIK 229
|||||||||||||||||||||||||||||||||||||||||||||||||
Db 176 PSRFSGSRSGTDFTLTISSLQPEDFATYYCQQHYTTPPTFGCGTKVEIK 224
7. Conclusion: Claim 7 is objected to. Claims 1-6 and 8-12, and 15-17 are rejected.
8. Any inquiry concerning this communication or earlier communications from the examiner should be directed to LAURA B GODDARD whose telephone number is (571)272-8788. The examiner can normally be reached Mon-Fri, 7am-3:30pm.
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, Samira Jean-Louis can be reached at 571-270-3503. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/Laura B Goddard/Primary Examiner, Art Unit 1642
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