Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
DETAILED ACTION
This action is in response to claim amendments filed 7/13/26. Claims 1-17, 24-31 are pending and under examination.
Withdrawn Rejections
The objection to the specification is withdrawn in light of the amendments.
The rejection over “derived” is withdrawn in light of the removal of this term from the claims.
The rejection over the substitution language in claim 11 is withdrawn. The claim now clearly indicates that the CH3 contains D239 and L241 as a structural limitation. By still reciting the original, non-existent parent amino acid, the claim is clearly a product-by-process claim requiring the actual mutations (E239D and M241L) be made to infringe the claim (previous interpretation 2).
The rejection of claims 22-23 is withdrawn because the claim was canceled.
The rejection under §112d is withdrawn. Claim 17 has been appropriately amended and claims 18-21 have been canceled.
Maintained Rejections and New Rejections Necessitated by Amendment
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.
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.
Claim(s) 1-5, 8-10, 12, and 16-28 is/are rejected under 35 U.S.C. 103 as being unpatentable over Solovyev (US20200270345; previously cited) in view of Swanson (US20160257751; previously cited) and further in view of Zhou (US 20170218066; previously cited).
Regarding claim 1, Solovyev teaches an anti-CD47/PD-1 antibody (title; abstract; figure 6; paragraph 47; claim 1).
Solovyev does not teach the specific sequences of the instantly claimed CDRs.
Nevertheless, one of ordinary skill in the art would have found it obvious to substitute a known antibody that binds the same target of Solovyev into the bispecific antibody of Solovyev with a reasonable expectation of obtaining predictable results.
With respect to the CD47 portion of the bispecific antibody, Solovyev differs from the prior art in the particular sequences. However, the instantly claimed sequences of a CD47 antibody were known in the art. Swanson teaches CD-47 antibodies (title; abstract). Swanson teaches one exemplary antibody (C47B10) comprises a heavy chain of SEQ ID NO: 22, which contains the CDRs of instantly claimed SEQ ID NOs: 17, 19, and 21 and teaches this same antibody has a light chain of SEQ ID NO:8, which contains the CDRs of instantly claimed SEQ ID NOs: 23, 25, and 27 (claims 1 and 2). Substituting one known CD47 antibody (Solovyev) with another (Swanson) would lead to the predictable result of preserving the binding of CD47 in the bispecific antibody of Solovyev because Swanson teaches the antibody binds the same target.
With respect to the PD-L1 portion of the bispecific antibody, Solovyev differs from the prior art in the particular sequences. However, the instantly claimed sequences of a CD47 antibody were known in the art. Zhou teaches PD-L1 antibodies (title; abstract). Zhou teaches one exemplary antibody (H6B1L-EM) comprises a heavy chain of SEQ ID NO: 1, which contains the CDRs of instantly claimed SEQ ID NOs: 29, 31, and 33 and teaches this same antibody has a light chain of SEQ ID NO:2, which contains the CDRs of instantly claimed SEQ ID NOs: 35, 37, and 39 (paragraph 175; claims 1, 3, 5, and 6). Substituting one known PD-L1 antibody (Solovyev) with another (Zhou) would lead to the predictable result of preserving the binding of CD47 in the bispecific antibody of Solovyev because Zhou teaches the antibody binds the same target.
Thus, substituting known CD-47 and PD-L1 binding regions/antibodies of Swanson/Zhou into the bispecific CD47/PD-L1 antibody of Solovyev would have been predictable and obvious to the person of ordinary skill at the time of filing. As this is every limitation of instant claim 1, the claimed antibody would have been obvious.
Regarding claim 2, Swanson SEQ ID NO: 22 comprises instant SEQ ID NO: 1. Swanson SEQ ID NO: 8 comprises instant SEQ ID NO: 3.
Regarding claim 3, Zhou SEQ ID NO: 1 comprises instant SEQ ID NO: 5. Zhou SEQ ID NO: 2 comprises instant SEQ ID NO: 7.
Regarding claim 4, the first and second antigen binding domains are discussed above. Solovyev further teaches the bispecific antibody having an Fc domain (example 16) as well as being a “full length antibody” (claim 2), wherein a full-length antibody has an Fc domain (e.g., paragraphs 64, 70, 95).
Regarding claim 5, Solovyev teaches the CD47 (first antigen binding fragment) as a Fab (examples 4, 5, 9; claim 13). Similarly, Swanson teaches the above sequences as a Fab (paragraphs 5 and 6). The alternatives in Solovyev represent a finite number of known, predictable antibody formats, while Swanson exemplifies specifically the Fab format, which would have made such a fragment obvious.
In the same way, Solovyev teaches the PD-L1 (second antigen binding fragment) as an scFv (claim 14). Zhou teaches the PD-L1 antibody as an scFv (paragraphs 20, 27, 170). The alternatives in Solovyev and Zhou represent a finite number of known, predictable antibody formats, which would have made such a fragment obvious.
Regarding claim 8, the PD-L1 fragment being an scFv is discussed above.
Regarding claim 9, the CD47 fragment being a Fab is discussed above.
Regarding claim 10, the Fc region is discussed above. Solovyev teaches the antibody is preferably IgG1 (paragraph 65).
Regarding claim 12, this claim is directed entirely to a function of the Fc region. The claim does not provide any distinct structure which would differentiate the Fc region from that of claim 10 or of the prior art. Function flows from structure and since the art makes obvious the same structure as discussed above (an IgG1 Fc region), the evidence supports the conclusion that the function must also be present.
Regarding claim 16, this claim is directed entirely to a function of the antibody. The claim does not provide any distinct structure which would differentiate the binding regions from that of the above claims or of the prior art. Function flows from structure and since the art makes obvious the same structure as discussed above (CD47 binding CDRs and PDL1 binding CDRs), the evidence supports the conclusion that the function must also be present.
Regarding claim 17, Solovyev teaches the composition is pharmaceutical and comprises a pharmaceutically acceptable excipient (claim 24).
Regarding claim 24, Solovyev teaches administering the antibody to a subject in need to treat cancer (claims 26-27).
Regarding claim 25, Solovyev teaches administering the antibody to a subject in need to treat cancer (claims 26-27). Administering the same drug (bispecific CD47/PD-L1 antibody) to the same subject (subject having cancer, which is a species of tumor), will have the same results.
Regarding claim 26, Solovyev teaches a nucleic acid encoding the antibody (claim 18).
Regarding claim 27, Solovyev teaches a host cell comprising the nucleic acid (claim 22).
Regarding claim 28, Solovyev teaches cultivating (culturing) the host cell comprising the polynucleotide to obtain the antibody (claim 23).
Regarding claims 29-30, Solovyev teaches the cancer is breast cancer (claim 25).
Regarding claim 31, Solovyev teaches combining the antibody therapy with additional therapeutics including “a different cancer medicament/drug” (paragraph 272) and teaches known chemotherapeutics for this purpose (paragraph 274), which would have made the inclusion of such obvious.
Therefore, claims 1-5, 8-10, 12, and 16-31 would have been obvious.
Claim(s) 11 is/are rejected under 35 U.S.C. 103 as being unpatentable over Solovyev (US20200270345) in view of Swanson (US20160257751) and Zhou (US 20170218066) as applied to claims 1-5, 8-10, 12, and 16-31 above, and further in view of Uniprot H (previously cited).
Claims 1-5, 8-10, 12, and 16-31 would have been obvious as discussed above and incorporated herein. The IgG1 heavy chain constant region would have been obvious as discussed (Solovyev teaches the antibody is preferably IgG1). Further, Solovyev suggests the human IgG1 (paragraph 328), suggests the antibody is “essentially human” (paragraph 68), the intended interaction of the antibody with human antigens (example 13), and that the subject for treatment is “preferably a human” (paragraph 124).
The references do not disclose a particular sequence for IgG1.
Uniprot H discloses the human IgG1 heavy chain and teaches residues 120-449 are the constant domain. These residues in the disclosed sequence, when aligned with instant SEQ ID NO: 11, comprise D239 and L241 as instantly claimed (see arrows).
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As this is the whole of IgG1, this sequence comprises the Fc region, comprises the heavy chain constant regions CH1, CH2, and CH3, and contains the instantly claimed mutations respective to the positions “of” instant SEQ ID NO: 1.
Regarding claim 11, it would have been obvious to one of ordinary skill in the art at the time of filing to use the Uniprot H sequence in the bispecific antibody discussed above because the art teaches using IgG1 and particularly suggests human forms, which are suitable for administration to humans. Uniprot H provides such a sequence, rendering this an obvious choice. Further, as a product-by-process, the composition is determined based on the structure and there is no requirement that one have actively made the substitution from an E/M residue for the purposes of prior art analysis; see §2113.
Therefore, claims 1-5, 8-12, and 16-31 would have been obvious.
Claim(s) 6 and 13-15 is/are rejected under 35 U.S.C. 103 as being unpatentable over Solovyev (US20200270345) in view of Swanson (US20160257751), Zhou (US 20170218066), and Uniprot H as applied to claims 1-5, 8-12, and 16-31 above, and further in view of McGilligan (US 20220033507; previously cited) and Uniprot M (previously cited).
Claims 1-5, 8-12, and 16-31 would have been obvious as discussed above and incorporated herein.
Regarding claim 15, instant claim 15 requires the Fc region to comprise SEQ ID NO: 11, reproduced below:
ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS
GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGG
PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYN
STYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDE
LTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRW
QQGNVFSCSVMHEALHNHYTQKSLSLSPGKGSAGGSGGDS
The underlined portion is human IgG1, as taught by Uniprot H (see rejection of claim 11). Using this sequence in the constant region of the antibody would have been obvious as described in that rejection.
SEQ ID NO: 11 further contains:
GSAGGSGGDS
This sequence is found in bispecific antibodies, such as taught in McGilligan; see for example SEQ ID NO: 59 and the description in paragraphs 68-69; example 8). McGilligan discloses the antibody comprises the mouse IgG2A sequence and that “a short linker was added to the C-terminal end of the heavy chain and the NLRP3 variable domains in an ScFv format” (paragraph 331). As taught by Uniprot M, the sequence preceding the GSAGGSGGDS sequence is the entirety of the mouse IgG2A heavy chain Fc sequence and so this sequence is what McGilligan was referring to when teaching mouse IgG2A. Thus, one of ordinary skill in the art would have recognized the sequence prior to the GSAGGSGGDS as the mouse IgG2a heavy chain sequence and so would have also recognized the GSAGGSGGDS to be the “short linker” added to the C-terminal end of the heavy chain taught by McGilligan.
The art as discussed suggests PD-L1 as an scFv fragment. One of ordinary skill in the art would have found it obvious to arrange a bispecific antibody, such as the one taught by Solovyev, in a known manner. Solovyev teaches fusing the antigen binding sites to the CH2/CH3 region, which is in the Fc region of an antibody (paragraph 240). McGilligan teaches bispecific antibodies in an acceptable format, where one of the binding moieties is provided as an scFv and fused to the C-terminus of the heavy chain CH3 constant region via the GSAGGSGGDS linker. Thus, one of ordinary skill in the art would have found it obvious to use the same, known arrangement with the CD43/PD-L1 IgG1 bispecific antibody discussed above, attaching the PD-L1 scFv to the C-terminus of the human IgG1 heavy chain Fc domain using the known GSAGGSGGDS linker, which would arrive at a sequence comprising instant SEQ ID NO: 11 and meeting the limitations of instant claim 15.
Regarding claims 6 and 13, fusing the second antibody fragment (PD-L1 scFv) to the C-terminus of the Fc domain via a peptide linker would have been obvious for the same reasons as instant claim 15 above.
Regarding claim 14, the sequence following the GSAGGSGGDS in McGilligan is the NLRP3 scFv, comprising SEQ ID NO: 36 (heavy chain; paragraph 63), a linker (GGGGSGGGGSGGGGS), and SEQ ID NO: 43 (light chain; paragraph 65).
Instant SEQ ID NO: 9 is the following:
SeqIDNO:5—(GGGGS)3—SEQIDNO:7
Both SEQ ID NOs: 5 and 7 representing the heavy and light chains of the PD-L1 antibody were known as discussed above. Further, the art suggested this PD-L1 binding moeity as an scFv, motivating one of ordinary skill in the art to make an scFv according to known methods. McGilligan teaches a functional scFv as part of a bispecific antibody arranged as HC—(GGGGS)3—LC, which would have suggested the same format to one of ordinary skill in the art. Connecting the heavy chain and light chain (SEQ ID NOs: 5 and 7, respectively) with the (GGGGS)3 linker arrives at a sequence comprising instant SEQ ID NO: 9. As such, SEQ ID NO: 9—and instant claim 14—would have been obvious.
Therefore, claims 1-6 and 8-31 would have been obvious.
Claim(s) 1-10, 12, and 16-31 is/are rejected under 35 U.S.C. 103 as being unpatentable over Haiqing (CN112125975A; previously cited) in view of Swanson (US20160257751) and further in view of Zhou (US 20170218066). Note that references to Haiqing refer to the machine translation (previously cited).
Regarding claim 1, Haiqing teaches a PD-L1/CD47 bispecific antibody (title). While Haiqing teaches certain CDRs for the binding portions of the antibody, Haiqing does not teach the specific sequences of the instantly claimed CDRs.
Nevertheless, one of ordinary skill in the art would have found it obvious to substitute a known antibody that binds the same target of Haiqing into the bispecific antibody of Haiqing with a reasonable expectation of obtaining predictable results.
With respect to the CD47 portion of the bispecific antibody, Haiqing differs from the prior art in the particular sequences. However, the instantly claimed sequences of a CD47 antibody were known in the art. Swanson teaches CD-47 antibodies (title; abstract). Swanson teaches one exemplary antibody (C47B10) comprises a heavy chain of SEQ ID NO: 22, which contains the CDRs of instantly claimed SEQ ID NOs: 17, 19, and 21 and teaches this same antibody has a light chain of SEQ ID NO:8, which contains the CDRs of instantly claimed SEQ ID NOs: 23, 25, and 27 (claims 1 and 2). Substituting one known CD47 antibody (Haiqing) with another (Swanson) would lead to the predictable result of preserving the binding of CD47 in the bispecific antibody of Haiqing because Swanson teaches the antibody binds the same target.
With respect to the PD-L1 portion of the bispecific antibody, Haiqing differs from the prior art in the particular sequences. However, the instantly claimed sequences of a CD47 antibody were known in the art. Zhou teaches PD-L1 antibodies (title; abstract). Zhou teaches one exemplary antibody (H6B1L-EM) comprises a heavy chain of SEQ ID NO: 1, which contains the CDRs of instantly claimed SEQ ID NOs: 29, 31, and 33 and teaches this same antibody has a light chain of SEQ ID NO:2, which contains the CDRs of instantly claimed SEQ ID NOs: 35, 37, and 39 (paragraph 175; claims 1, 3, 5, and 6). Substituting one known PD-L1 antibody (Haiqing) with another (Zhou) would lead to the predictable result of preserving the binding of CD47 in the bispecific antibody of Haiqing because Zhou teaches the antibody binds the same target.
Thus, substituting known CD-47 and PD-L1 binding regions/antibodies of Swanson/Zhou into the bispecific CD47/PD-L1 antibody of Haiqing would have been predictable and obvious to the person of ordinary skill at the time of filing. As this is every limitation of instant claim 1, the claimed antibody would have been obvious.
Regarding claim 2, Swanson SEQ ID NO: 22 comprises instant SEQ ID NO: 1. Swanson SEQ ID NO: 8 comprises instant SEQ ID NO: 3.
Regarding claim 3, Zhou SEQ ID NO: 1 comprises instant SEQ ID NO: 5. Zhou SEQ ID NO: 2 comprises instant SEQ ID NO: 7.
Regarding claim 4, Haiqing teaches the bispecific antibody includes an Fc region (figure 1; p.5).
Regarding claim 5, Haiqing teaches the binding moieties may be Fabs or scFvs (p.3,5). The list of alternatives is finite (nine) and represent well-known antibody formats. One of ordinary skill in the art would have been able to select from this list with predictable results.
Regarding claims 6 and 7, Haiqing teaches the bispecific antibody in figure 1:
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Here, the CD47 binding protein is clearly fused via a peptide linker (peptide fragment) to the C-terminus of the heavy chain Fc domain. The image shows two Fab fragments (circled):
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The image further shows two fragments that are not Fabs, suggesting another format. This being an scFv would have been obvious as above.
Thus, Haiqing differs in that Haiqing shows the Fabs bind PD-L1 and the fused scFvs bind CD47, whereas the instant claims require the Fabs binding CD47 and the fused scFvs binding PD-L1.
Nevertheless, the instant arrangement would have been an obvious variation to one of ordinary skill in the art at the time of filing. Haiqing teaches it is “preferable” that the CD47 is linked to the heavy chain of the PD-L1 antibody, clearly suggesting the alternative is also possible. Further, reversing parts or rearranging parts is prima facie obvious (MPEP §2144.04(VI)(A,C) so this arrangement—the two Fabs binding CD47 and two scFvs binding PD-L1—would have been obvious.
Regarding claim 8, the PD-L1 fragment being an scFv is discussed above.
Regarding claim 9, the CD47 fragment being a Fab is discussed above.
Regarding claim 10, the Fc region is discussed above. Haiqing teaches the antibody may be IgG1 (p. 5) and uses IgG1 antibodies as a control (p.12), suggesting the bispecific antibody is also IgG1.
Regarding claim 12, this claim is directed entirely to a function of the Fc region. The claim does not provide any distinct structure which would differentiate the Fc region from that of claim 10 or of the prior art. Function flows from structure and since the art makes obvious the same structure as discussed above (an IgG1 Fc region), the evidence supports the conclusion that the function must also be present.
Regarding claim 16, this claim is directed entirely to a function of the antibody. The claim does not provide any distinct structure which would differentiate the binding regions from that of the above claims or of the prior art. Function flows from structure and since the art makes obvious the same structure as discussed above (CD47 binding CDRs and PDL1 binding CDRs), the evidence supports the conclusion that the function must also be present.
Regarding claims 17, Haiqing teaches the composition is pharmaceutical and comprises a carrier (claim 15).
Regarding claim 24, Haiqing teaches administering the antibody to a subject in need to treat cancer (claims 26-27).
Regarding claim 25, Haiqing teaches administering the antibody to a subject in need to treat cancer or tumors (p.4). Administering the same drug (bispecific CD47/PD-L1 antibody) to the same subject (subject having cancer/tumors), will have the same results.
Regarding claim 26, Haiqing teaches a nucleic acid encoding the antibody (claim 11).
Regarding claim 27, Haiqing teaches a host cell comprising the nucleic acid (claim 13).
Regarding claim 28, Haiqing teaches cultivating (culturing) the host cell comprising the polynucleotide to obtain the antibody (p.5).
Regarding claims 29-30, Haiqing teaches treatment of breast cancer (claim 16).
Regarding claim 31, Haiqing teaches adding additional therapeutics (p.4). While arriving at the instant antibody would have been obvious as above, Haiqing teaches their own antibody that is not disclosed as having the same instant sequences. This meets the definition of “another cancer immunotherapeutic agent” and would have been obvious to include because Haiqing teaches using more than one treatment and that the Haiqing antibody also works for the same subject.
Therefore, claims 1-10, 12, and 16-31 would have been obvious.
Response to Arguments
Applicant's arguments filed 7/13/26 have been fully considered but they are not persuasive.
Applicant argues the technical feature is the specific combination of CDR sequences for the two binding portions and that the instant bispecific antibody exhibits “significantly improved” binding affinity to CD47 compared to the monospecific antibody while still binding Pd-L1 and showing minimal hemagglutination. Applicant points to figures 5 and 6 as well as example 2 in support of this assertion.
Essentially, Applicant is arguing surprising results. This is not persuasive. First, the CDR sequences are not “novel” as asserted by Applicant and supported by the rejection of record. It is true that the specific CD47 and PDL1 sequences had not been previously combined, though CD47/PDL1 bispecific antibodies were known in the art. Thus, the closest prior art are the other known bispecific antibodies. Applicant argues that the combination is better than monotherapy but this is not a comparison to the closest prior art as required to establish superior results (MPEP §716.02(a)). There is insufficient evidence to establish the expected specificity to the two antigens when using a bispecific antibody and so there is no way to determine if the instant specificity is “significantly improved” compared to other known bispecific antibodies. The same is true of the hemagglutination, where there is insufficient evidence to determine the expected hemagglutination of prior art CD47/PDL1 antibodies.
Applicant argues the antibody demonstrates excellent inhibition of cancer growth in an in vivo model (example 3; figures 14-16). As above, there is insufficient evidence to determine if the inhibition rises to the level of surprising results. Example 3 uses less of the monospecific antibodies (2.1 mg/kg vs 3 mg/kg) so even the combination of G4 is not an equivalent comparison. Further, comparing two monospecific antibodies is not equivalent to comparing known bispecific antibodies.
Additionally, surprising results must be commensurate in scope with the claims. Efficacy in treating cancer is not probative of the composition claims as there is no requirement that the antibody is used to treat cancer in these claims (e.g., claim 1) nor is there sufficient evidence to presume these results will be achieved in any cancer other than the tested cancer lines. There are currently no claims limited to breast and/or colorectal cancer.
Applicant argues “none of the asserted references provide motivation to combine the teachings thereof and then modify the combined teaching to arrive at the specific combination recited in the claims with a reasonable expectation of success. This is not persuasive because this does not point to any specific deficiency in the rejections of record nor is this supported by any objective evidence.
Applicant argues the references do not suggest or expect the “remarkable effects” asserted above. As above, there is insufficient evidence to determine that these effects are “remarkable” or surprising.
Conclusion
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ADAM M WEIDNER whose telephone number is (571)272-3045. The examiner can normally be reached M-T 9-18; W-R 9-15.
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/Adam Weidner/ Primary Examiner, Art Unit 1675
