DETAILED ACTION
Election/Restrictions
Applicant’s election without traverse of Group V, claims 32, 37 and 41-64 and the Species: heavy variable domain (HC) comprising amino acids 25 to 144 of SEQ ID NO: 1 and a light chain variable region (LC) comprising amino acids 21 to 132 of SEQ ID NO: 7 in the reply filed on 1/7/26 is acknowledged.
Withdrawn claims 1-11, 13-20, 22-24, 26, 27, 29, 30, 34, 38 and 41 were canceled by Applicants.
Elected claims 32, 37 and 42-64, with Species HC: SEQ ID NO: 1 (25-144) and LC: SEQ ID NO: 7 (21-132) (and the related CDRH1-3 AND CDRL1-3 in the claims) are currently under examination.
Claim Rejections - 35 USC § 112-2nd paragraph
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 32, 37 and 42-64 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 32, 37 and 42-64 are rejected on the basis that it contains an improper Markush grouping of alternatives. See In re Harnisch, 631 F.2d 716, 721-22 (CCPA 1980) and Ex parte Hozumi, 3 USPQ2d 1059, 1060 (Bd. Pat. App. & Int. 1984). A Markush grouping is proper if the alternatives defined by the Markush group (i.e., alternatives from which a selection is to be made in the context of a combination or process, or alternative chemical compounds as a whole) share a “single structural similarity” and a common use. A Markush grouping meets these requirements in two situations. First, a Markush grouping is proper if the alternatives are all members of the same recognized physical or chemical class or the same art-recognized class, and are disclosed in the specification or known in the art to be functionally equivalent and have a common use. Second, where a Markush grouping describes alternative chemical compounds, whether by words or chemical formulas, and the alternatives do not belong to a recognized class as set forth above, the members of the Markush grouping may be considered to share a “single structural similarity” and common use where the alternatives share both a substantial structural feature and a common use that flows from the substantial structural feature. See MPEP § 2117.
The Markush grouping of the different antibodies (with different heavy and light chains; different CDR regions) is improper because the alternatives defined by the Markush grouping do not share both a single structural similarity and a common use for the following reasons: these antibodies are each different products which have different binding regions and different amino acid sequences. The antibody elected: HC: SEQ ID NO: 1 (aa 25-144) and LC: SEQ ID NO: 7 (21-132) is structurally different from the other antibodies in the Markish group and not a mere species.
To overcome this rejection, Applicant may set forth each alternative (or grouping of patentably indistinct alternatives) within an improper Markush grouping in a series of independent or dependent claims and/or present convincing arguments that the group members recited in the alternative within a single claim in fact share a substantial structural similarity as well as a common use.
Claim 37 is vague and confusing for the wording: administering to the subject a composition or combination comprising…” followed by (a) HGMB protein and (b) an antibody, making it unclear if the composition does, in fact, contain both a HMGB and an anti-DNABII antibody which is how the invention is described in the instant specification. Appropriate clarification and/or correction is required.
Claim 42 is vague and confusing because it also refers to ‘the composition or combination”, as well as being unclear how SEQ ID NO: 52 relates to the product. Appropriate clarification and/or correction is required.
Claim 43 is vague and confusing because the claims and specification are drawn to the use of antibody and HGMB, while the claim recites the use of just a light chain or just a heavy chain which appears to be a mistake. Appropriate clarification and/or correction is required.
Claim 47 is vague and confusing because it recites in part a) that the antibody or antigen-binding fragment thereof is ‘modified’, yet does not describe how it is modified in part a) which leaves the claim vague and confusing. The metes and bounds of this term cannot be readily understood. While the specification can be used to provide definitive support, the claims are not read in a vacuum. Rather, the claim must be definite and complete in and of itself. Limitations from the specification will not be read into the claims. The claims as they stand are incomplete and fail to provide adequate structural properties to allow for one to identify what is being claimed. Appropriate clarification and/or correction is required.
Claim 49 and 52 are vague and confusing because it does not recite what type of mutation is at K12, C23, C45, C106 or K114. Is this a deletion or substitution? If it is a substitution the claim should recite the amino acid which is to replace it. While the specification can be used to provide definitive support, the claims are not read in a vacuum. Rather, the claim must be definite and complete in and of itself. Limitations from the specification will not be read into the claims. The claims as they stand are incomplete and fail to provide adequate structural properties to allow for one to identify what is being claimed. Appropriate clarification and/or correction is required.
Claim 50 is vague and indefinite because it recites “or a fragment thereof” (from the HGMB polypeptides). A fragment can read on a single amino acid to many more. The metes and bounds of the claim are unclear. While the specification can be used to provide definitive support, the claims are not read in a vacuum. Rather, the claim must be definite and complete in and of itself. Limitations from the specification will not be read into the claims. The claims as they stand are incomplete and fail to provide adequate structural properties to allow for one to identify what is being claimed. Appropriate clarification and/or correction is required.
Claim 51 is vague and confusing because HGMB already comprises an AB box. The wording of the claim does not make it clear that it is the fragment that comprise a B box or A box leaving the claim confusing. The wording should recite “wherein the fragment thereof comprises and A box or B box”. Appropriate clarification and/or correction is required.
Allowable Subject Matter
Claims 32, 37 and 42-64 would be allowable if rewritten or amended to overcome the rejection(s) under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), 2nd paragraph, set forth in this Office action; corresponding to the elected antibody.
Status of Claims
The prior art of record, individually or in combination, does not teach or fairly suggest methods which use a composition or combination comprising: (a) a high mobility group box protein (HMGB) polypeptide, and (b) an anti-DNABII antibody, where the anti-DNABII antibody comprises a heavy chain variable region (VH). and a light chain variable region (VL), where the VH is selected to be amino acids 25-144 of SEQ ID NO:1, and the VL is selected to be amino acids 21-132 of SEQ ID NO:7; wherein the methods include: methods for preventing the formation of or disrupting a biofilm, or inhibiting, preventing or treating a microbial infection that produces a biofilm in a subject or treating a condition characterized by the formation of a biofilm in a subject.
The closest prior art is:
WO 2018/170178 A1 to Research Institute At Nationwide Children's Hospital (hereinafter, "Nationwide") teaches a composition or combination (composition, Para. [0012]) comprising: (a) a high mobility group box protein (HMGB) polypeptide comprising a B box or an A box or an AB box thereof, and (b) an anti-DNABII antibody (HMGB1 has two tandem DNA binding domains (A and B box), Para. [0010]; method for inhibiting, competing or titrating the binding of a deoxyribonucleic acid B II (DNABII) polypeptide to a microbial DNA in a biofilm, comprising contacting the microbial DNA in the biofilm with an effective amount of a modified high mobility group-box 1 domain comprising one or more substitutions, Para. [0014]; the compositions and related methods of the present invention may be used in combination with the administration of other therapies. These include, but are not limited to, the administration of DNase enzymes, antibiotics, antimicrobials, or other antibodies, Para. [0236]; [t]he antibiotic or antimicrobial can be added prior to, concurrent with, or subsequent to the addition of the anti-DNABII antibody, Para. [0238]), but fails to fairly teach or suggest either alone or in combination with the prior art where the anti-DNABII antibody comprises a heavy chain variable region (VH), and a light chain variable region (VL), where the VH is selected to be SEQ ID NO:1, and the VL is selected to be SEQ ID NO:7.
(ii) WO 2020/092554 A1 to Delinia, Inc. (hereinafter, "Delinia") teaches an antibody comprising a heavy chain variable region wherein the heavy chain variable region is similar to SEQ ID NO:1 (antibody comprising a heavy chain amino acid sequence selected to be SEQ ID NO: 231, wherein SEQ ID NO: 231 of Delinia comprises 94.6% sequence identity to instant SEQ ID NO:1, Claim 5), but fails to fairly teach or suggest either alone or in combination with the prior art a composition or combination comprising: (a) a high mobility group box protein (HMGB) polypeptide, and (b) an anti-DNABII antibody, where the anti-DNABII antibody comprises a heavy chain variable region (VH), and a light chain variable region (VL), where the VH is selected to be SEQ ID NO:1, and the VL is selected to be SEQ ID NO:7.
(iii) WO 2013/177596 A2 to Sloan Kettering Institute for Cancer (hereinafter, "Sloan") teaches an antibody comprising a light chain variable region wherein the light chain variable region is similar to SEQ ID NO:7 (amino acid sequence of humanized 2A2 light chain selected to be SEQ ID NO. 8, wherein SEQ ID NO. 8 of Sloan comprises 95.2% sequence identity to instant SEQ ID NO:7, Para. [0111]), but fails to fairly teach or suggest either alone or in combination with the prior art a composition or combination comprising: (a) a high mobility group box protein (HMGB) polypeptide, and (b) an anti-DNABII antibody, where the anti-DNABII antibody comprises a heavy chain variable region (VH), and a light chain variable region (VL), where the VH is selected to be SEQ ID NO:1, and the VL is selected to be SEQ ID NO:7.
Correspondence regarding this application should be directed to Group Art Unit 1645. Papers related to this application may be submitted to Group 1600 by facsimile transmission. Papers should be faxed to Group 1600 via the PTO Fax Center located in Remsen. The faxing of such papers must conform with the notice published in the Official Gazette, 1096 OG 30 (November 15,1989). The Group 1645 Fax number is 571-273-8300 which is able to receive transmissions 24 hours/day, 7 days/week.
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Any inquiry concerning this communication or earlier communications from the examiner should be directed to Jennifer E. Graser whose telephone number is (571) 272-0858. The examiner can normally be reached on Monday-Friday from 8:00 AM-4 PM.
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/JENNIFER E GRASER/ Primary Examiner, Art Unit 1645 4/9/26
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