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 .
Response to Amendment
Applicant’s amendment filed 17 February 2026 has been received and entered. Applicant’s substitute specification has been received and entered. Claims 1-2, 5-6, and 10 have been amended. Claims 1-42 are currently pending in the instant application.
Election/Restrictions
Applicant’s election without traverse of Group I, claims 1-11, 14, 40 and 41 in the reply filed on 17 February 2026 is acknowledged.
Claims 12-13, 15-39 and 42 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 17 February 2026.
Information Disclosure Statement
The listing of references in the specification is not a proper information disclosure statement. 37 CFR 1.98(b) requires a list of all patents, publications, or other information submitted for consideration by the Office, and MPEP § 609.04(a) states, "the list may not be incorporated into the specification but must be submitted in a separate paper." Therefore, unless the references have been cited by the examiner on form PTO-892, they have not been considered.
Applicant is reminded of their duty to disclose information material to patentability (37 CFR 1.56). At the time of the instant Office action, no IDS had been filed.
Drawings
The drawings are objected to because they do not comply with 37 CFR 1.84(a)(1) which requires that black and white drawings use India ink, or its equivalent that secures solid black lines. See example below: .
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The drawings are also not compliant with 37 CFR 1.84(I) which requires that all drawings be made by a process which will give them satisfactory reproduction characteristics. Every line, number, and letter must be durable, clean, black, sufficiently dense and dark, and uniformly thick and well-defined. See example above.
Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
Specification
The title of the invention is not descriptive. A new title is required that is clearly indicative of the invention to which the claims are directed.
The elected invention is directed to an anti-CCR5 humanized monoclonal antibody and compositions thereof. Methods are not included and therefore, the title should be reflective of such.
The disclosure is objected to because of the following informalities: the specification, filed 17 February 2026, contains text which is not plainly and legibly written in permanent dark ink or its equivalent or presented in a form having sufficient clarity and contrast between the paper and the writing thereon to permit the direct reproduction of readily legible copies by conventional means (see 37 CFR 1.52 (a)(1)(iv-v). The specification contains text which does not demonstrate solid black lines at pages 1 (paragraph 3) and page 41, 42, 43, 45, 46, 49, 50, 52 and 53 (paragraph headers).
See example below (specifically “Maddon-8PUS”):
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Appropriate correction is required.
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.
Claim(s) 1, 4, 14 and 40-41 is/are rejected under 35 U.S.C. 103 as being unpatentable over U.S. Pat. No. 7,122,185 (Olson et al.) in view of Dumet et al. (Insights into the IgG heavy chain engineering patent landscape as applied to IgG4 antibody development. MABS 11(8): 1341-1350, 2019).
Olson et al. teach humanized anti-CCR5 antibodies, designated PRO 140#1 and PRO 140#2 which comprises a heavy chain variable region (Figures 9 and 10) and a light chain variable region (Figure 8; the PRO 140 antibodies have identical light chain variable regions). The amino acid sequences of these antibodies are identical to the amino acid sequences of SEQ ID NO:8, 10 and 12, as acknowledged in the instant specification (see page 6 under description of Figure 1). Olson et al. do not teach a heavy chain modification that increases the antibody’s terminal half-life.
Dumet et al. teach heavy chain modifications to antibodies which increase an antibody’s terminal half-life. Dumet et al. teach that half-life is critical for any IgG subclass used as a therapeutic because increasing the half-life can help decrease the dosage or the spacing of administrations (see page 1346, column 1, second to last paragraph). At page 1346, several different mutations are described which increase the half-life of an antibody including M252Y/S254T/T256E (YTE) (column 2, line 6-7) and M428L/N434S (LS) (column 2, 3rd paragraph, line 6). Both of these mutation combinations (in claim 4) are taught by Dumet et al. and extend the half-life of the antibody which contains the mutation 4-fold.
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to include a modification to the antibody of Olson et al. which increases the half-life of the antibody. One would be motivated to include a modification to the heavy chain of the antibody because Dumet et al. teach that modifications can increase the half-life of the antibody and that half-life is critical for therapeutic antibodies. One of ordinary skill in the art would have selected one of the well-known mutation combinations taught by Dumet, including the YTE or the LS mutation combination because both of these mutations result in a 4-fold extended half-life of the antibody. One would have had a reasonable expectation of success because the mutations are made in the heavy chain constant domain which is not involved in antibody-ligand binding and therefore, the mutations would not impact antigen binding.
Olson et al. also teach that the antibodies could be used therapeutically (see column 18, last paragraph) as well as used in combination with other antibodies for diagnostic or detection purposes (see column 19, first full paragraph). Claim 14 of Olson et al. is directed to the anti-CCR5 antibody in a composition with a carrier. While Olson et al. do not specifically specify that the carrier is pharmaceutically acceptable, it would be obvious to include a pharmaceutically acceptable carrier because Olson et al. clearly intend therapeutic uses of the antibody. While Olson et al. do not specifically indicate that the antibody would be included in a kit, the disclosure of Olson et al. that the antibody could be used in combination with other antibodies for diagnostic or detection purposes would be indicative of an assay which normally includes additional components such as diluents, wherein the different components of the kit are in separate containers. Lastly, while Olson et al. do not specifically recite an antibody in lyophilized form, such would have been obvious over the disclosure of Olson et al. that the antibody could be used for diagnostic or detection purposes with other antibodies, which is indicative of a kit. Antibodies are commonly lyophilized for storage purposes or for including in assay kits because this form preserves the antibody. Therefore, it would have been prima facie obvious to include the antibody of Olson et al. with the half-life extending mutations of Dumet et al. in a composition with a pharmaceutical carrier because Olson et al. teach therapeutic uses of the antibody. Additionally, it would have been prima facie obvious to include the antibody of Olson et al. with the half-life extending mutations of Dumet et al. in a kit because Olson et al. teach diagnostic uses and uses of the antibody for detection, which are consistent with uses in an assay which is commonly in the form of a kit which includes reagents for the diagnostic/detection methods. Therefore, the invention as a whole would have been obvious over the combination of Olson et al. in view of Dumet et al. absent evidence to the contrary.
Claim(s) 2-3 is/are rejected under 35 U.S.C. 103 as being unpatentable over U.S. Pat. No. 7,122,185 (Olson et al.) in view of Dumet et al. (MABS 11(8): 1341-1350, 2019).
Olson et al. teach humanized anti-CCR5 antibodies, designated PRO 140#1 and PRO 140#2 which comprises a heavy chain variable region (Figures 9 and 10) and a light chain variable region (Figure 8; the PRO 140 antibodies have identical light chain variable regions). The amino acid sequences of these antibodies are identical to the amino acid sequences of SEQ ID NO:8, 10 and 12, as acknowledged in the instant specification (see page 6 under description of Figure 1). Olson et al. do not teach a heavy chain modification that inhibits half antibody formation or increases the antibody’s terminal half-life.
Dumet et al. teach heavy chain modifications to antibodies which increase an antibody’s terminal half-life. Dumet et al. teach that half-life is critical for any IgG subclass used as a therapeutic because increasing the half-life can help decrease the dosage or the spacing of administrations (see page 1346, column 1, second to last paragraph). At page 1346, several different mutations are described which increase the half-life of an antibody.
Dumet et al. also teach heavy chain modification to antibodies which abolish the formation of half antibody molecules. At page 1347, column 1, paragraph 2, Dumet et al. teach that the S228P mutation in the hinge region abolishes heterogeneity of human IgG4 antibodies. Dumet et al. also teach the combination S228P/R409K (see column 2, first paragraph) which add the benefit of reducing aggregation under low pH conditions (see last paragraph of column 1). Dumet et al. also teach the combination of S228P/K447del (see column 2, second to last paragraph) wherein the reduction of C-terminal heterogeneity is achieved by deletion of K447.
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to include modifications to the antibody of Olson et al. which increases the half-life of the antibody as well as inhibit half antibody formation. One would be motivated to include a modification to the heavy chain of the antibody because Dumet et al. teach that modifications can increase the half-life of the antibody and that half-life is critical for therapeutic antibodies as well as teaching inhibition of half antibody formation for stabilization. One of ordinary skill in the art would have been motivated to select one of the well-known mutation combinations taught by Dumet, such as the YTE or the LS mutation combination for increasing half-life because both of these mutations result in a 4-fold extended half-life of the antibody as well as one of the S228P mutations or combinations for inhibiting half antibody formation because these mutations are taught as being used in the art for this purpose. One would have had a reasonable expectation of success because the mutations are made in the heavy chain constant domain which is not involved in antibody-ligand binding and therefore, the mutations would not impact antigen binding. Therefore, the invention as a whole would have been obvious over the combination of Olson et al. in view of Dumet et al. absent evidence to the contrary.
Claim(s) 5, 8-9 is/are rejected under 35 U.S.C. 103 as being unpatentable over U.S. Pat. No. 7,122,185 (Olson et al.) in view of Dumet et al. (MABS 11(8): 1341-1350, 2019).
Olson et al. teach humanized anti-CCR5 antibodies, designated PRO 140#1 and PRO 140#2 which comprises a heavy chain variable region (Figures 9 and 10) and a light chain variable region (Figure 8; the PRO 140 antibodies have identical light chain variable regions). The amino acid sequences of these antibodies are identical to the amino acid sequences of SEQ ID NO:8, 10 and 12, as acknowledged in the instant specification (see page 6 under description of Figure 1). Olson et al. do not teach a heavy chain modification that inhibits half antibody formation or increases the antibody’s terminal half-life.
Dumet et al. teach heavy chain modifications to antibodies which increase an antibody’s terminal half-life. Dumet et al. teach that half-life is critical for any IgG subclass used as a therapeutic because increasing the half-life can help decrease the dosage or the spacing of administrations (see page 1346, column 1, second to last paragraph). At page 1346, several different mutations are described which increase the half-life of an antibody.
Dumet et al. teach heavy chain modifications to antibodies which abolish effector functions (see page 1343, bottom of page) which has the benefit of preventing unwanted immune activation, minimizing toxicity and avoiding inflammatory responses. A number of single mutations are described (L235A, L235E, F234A, G237A – page 1343, column 2; D265A, L328, A330R, F243L – page 1344, column 1) as well as combinations of mutations (see Table 2; F243A/V264A; E2333P/F234A/L235A/G236del/G237A; S228P/L235E).
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to include modifications to the antibody of Olson et al. which increases the half-life of the antibody as well as reduce effector function. One would be motivated to include a modification to the heavy chain of the antibody because Dumet et al. teach that modifications can increase the half-life of the antibody and that half-life is critical for therapeutic antibodies as well as teaching modifications to reduce effector function. One of ordinary skill in the art would have been motivated to select one of the well-known mutation combinations taught by Dumet, such as the YTE or the LS mutation combination for increasing half-life because both of these mutations result in a 4-fold extended half-life of the antibody as well as one of the mutations or combinations of mutations for inhibiting effector function as noted above because these mutations are taught as being used in the art for this purpose. One would have had a reasonable expectation of success because the mutations are made in the heavy chain constant domain which is not involved in antibody-ligand binding and therefore, the mutations would not impact antigen binding. Therefore, the invention as a whole would have been obvious over the combination of Olson et al. in view of Dumet et al. absent evidence to the contrary.
Claim(s) 6-7 is/are rejected under 35 U.S.C. 103 as being unpatentable over U.S. Pat. No. 7,122,185 (Olson et al.) in view of Dumet et al. (MABS 11(8): 1341-1350, 2019).
Olson et al. teach humanized anti-CCR5 antibodies, designated PRO 140#1 and PRO 140#2 which comprises a heavy chain variable region (Figures 9 and 10) and a light chain variable region (Figure 8; the PRO 140 antibodies have identical light chain variable regions). The amino acid sequences of these antibodies are identical to the amino acid sequences of SEQ ID NO:8, 10 and 12, as acknowledged in the instant specification (see page 6 under description of Figure 1). Olson et al. do not teach a heavy chain modification that inhibits half antibody formation or increases the antibody’s terminal half-life.
Dumet et al. teach that IgG4 antibodies are used therapeutically because they have weaker effector functions than IgG1 antibodies (see abstract). Dumet et al. also teach heavy chain modifications to antibodies which increase an antibody’s terminal half-life. Dumet et al. teach that half-life is critical for any IgG subclass used as a therapeutic because increasing the half-life can help decrease the dosage or the spacing of administrations (see page 1346, column 1, second to last paragraph). At page 1346, several different mutations are described which increase the half-life of an antibody.
Dumet et al. also teach heavy chain modification to antibodies which abolish the formation of half antibody molecules. At page 1347, column 1, paragraph 2, Dumet et al. teach that the S228P mutation in the hinge region abolishes heterogeneity of human IgG4 antibodies. Dumet et al. also teach the combination S228P/R409K (see column 2, first paragraph) which add the benefit of reducing aggregation under low pH conditions (see last paragraph of column 1). Dumet et al. also teach the combination of S228P/K447del (see column 2, second to last paragraph) wherein the reduction of C-terminal heterogeneity is achieved by deletion of K447.
Dumet et al. teach heavy chain modifications to antibodies which abolish effector functions (see page 1343, bottom of page) which has the benefit of preventing unwanted immune activation, minimizing toxicity and avoiding inflammatory responses. A number of single mutations are described (L235A, L235E, F234A, G237A – page 1343, column 2; D265A, L328, A330R, F243L – page 1344, column 1) as well as combinations of mutations (see Table 2; F243A/V264A; E2333P/F234A/L235A/G236del/G237A; S228P/L235E).
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to include modifications to the antibody of Olson et al. which increases the half-life of the antibody as well as reduce effector function. Further, it would have been obvious to use an IgG4 Fc with the antibody of Olson et al. because IgG4 has less effector function than other IgG antibodies. One would be motivated to include modifications to the heavy chain of the antibody of Olson et al. because Dumet et al. teach modifications to (1) increase the half-life of the antibody and that half-life is critical for therapeutic antibodies, (2) reduce effector function and (3) inhibit half antibody formation for increased stability. One of ordinary skill in the art would have been motivated to select one of the well-known mutation combinations taught by Dumet, such as the YTE or the LS mutation combination for increasing half-life because both of these mutations result in a 4-fold extended half-life of the antibody as well as one of the mutations or combinations of mutations for inhibiting effector function and for inhibiting half antibody formation as noted above because these mutations are taught as being used in the art for this purpose. One would have had a reasonable expectation of success because the mutations are made in the heavy chain constant domain which is not involved in antibody-ligand binding and therefore, the mutations would not impact antigen binding. Therefore, the invention as a whole would have been obvious over the combination of Olson et al. in view of Dumet et al. absent evidence to the contrary.
Claim(s) 10 and 11 is/are rejected under 35 U.S.C. 103 as being unpatentable over U.S. Pat. No. 7,122,185 (Olson et al.) in view of Dumet et al. (MABS 11(8): 1341-1350, 2019).
Olson et al. teach humanized anti-CCR5 antibodies, designated PRO 140#1 and PRO 140#2 which comprises a heavy chain variable region (Figures 9 and 10) and a light chain variable region (Figure 8; the PRO 140 antibodies have identical light chain variable regions). The amino acid sequences of these antibodies are identical to the amino acid sequences of SEQ ID NO:8, 10 and 12, as acknowledged in the instant specification (see page 6 under description of Figure 1). Olson et al. do not teach a heavy chain modification that increases the antibody’s terminal half-life or an IgG2 joined to IgG4 (T260).
Dumet et al. teach (page 1344, column 2, last paragraph) that joining an IgG2 (up to T260) with the end of an IgG4 Fc abolishes effector functions of the antibody.
Dumet et al. also teach heavy chain modifications to antibodies which increase an antibody’s terminal half-life. Dumet et al. teach that half-life is critical for any IgG subclass used as a therapeutic because increasing the half-life can help decrease the dosage or the spacing of administrations (see page 1346, column 1, second to last paragraph). At page 1346, several different mutations are described which increase the half-life of an antibody including M252Y/S254T/T256E (YTE) (column 2, line 6-7) and M428L/N434S (LS) (column 2, 3rd paragraph, line 6). Both of these mutation combinations (in claim 4) are taught by Dumet et al. and extend the half-life of the antibody which contains the mutation 4-fold.
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to include modifications to the antibody of Olson et al. which increase the half-life of the antibody as well as reduce effector function because these are desirable properties for a therapeutic antibody. One would be motivated to use an IgG2 (up to T260) joined to the end of an IgG4 Fc because this combination results in reduced effector function as well as including a modification to the heavy chain of the antibody because Dumet et al. teach that modifications can be introduced to increase the half-life of the antibody and that half-life is critical for therapeutic antibodies. One of ordinary skill in the art would have selected one of the well-known mutation combinations taught by Dumet, including the YTE or the LS mutation combination because both of these mutations result in a 4-fold extended half-life of the antibody. One would have had a reasonable expectation of success because the mutations are made in the heavy chain constant domain which is not involved in antibody-ligand binding and therefore, the mutations would not impact antigen binding.
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 1-11, 14 and 40-41 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 6-8 of U.S. Patent No. 7,122,185 in view of Dumet et al. Although the claims at issue are not identical, they are not patentably distinct from each other because the instant claims are directed to obvious, well-known modifications to a known antibody as claimed in ‘185.
The claims of ‘185 are directed to an anti-CCR5 antibody which has the same amino acid sequence structure as that of the instant claims (see the instant specification at page 6 which points out that the light and heavy chain variable regions are identical to the antibodies defined in U.S. Patent No. 7,122,185). ‘185 also claims a composition of the antibody with a carrier. ‘185 does not claim or disclose modifications to the heavy chain which (1) increase terminal half-life, (2) inhibit half antibody formation or (3) decrease effector function.
Dumet et al. provides a review of IgG heavy chain engineering which provides for improved functionality of therapeutic antibodies and which includes a disclosure of heavy chain amino acid modifications that (1) increase terminal half-life, (2) inhibit half antibody formation or (3) decrease effector function.
Dumet et al. teach heavy chain modifications to antibodies which increase an antibody’s terminal half-life. Dumet et al. teach that half-life is critical for any IgG subclass used as a therapeutic because increasing the half-life can help decrease the dosage or the spacing of administrations (see page 1346, column 1, second to last paragraph). At page 1346, several different mutations are described which increase the half-life of an antibody including M252Y/S254T/T256E (YTE) (column 2, line 6-7) and M428L/N434S (LS) (column 2, 3rd paragraph, line 6). Both of these mutation combinations (in claim 4) are taught by Dumet et al. and extend the half-life of the antibody which contains the mutation 4-fold.
Dumet et al. teach heavy chain modification to antibodies which abolish the formation of half antibody molecules. At page 1347, column 1, paragraph 2, Dumet et al. teach that the S228P mutation in the hinge region abolishes heterogeneity of human IgG4 antibodies. Dumet et al. also teach the combination S228P/R409K (see column 2, first paragraph) which add the benefit of reducing aggregation under low pH conditions (see last paragraph of column 1). Dumet et al. also teach the combination of S228P/K447del (see column 2, second to last paragraph) wherein the reduction of C-terminal heterogeneity is achieved by deletion of K447.
Dumet et al. teach heavy chain modifications to antibodies which abolish effector functions (see page 1343, bottom of page) which has the benefit of preventing unwanted immune activation, minimizing toxicity and avoiding inflammatory responses. A number of single mutations are described (L235A, L235E, F234A, G237A – page 1343, column 2; D265A, L328, A330R, F243L – page 1344, column 1) as well as combinations of mutations (see Table 2; F243A/V264A; E2333P/F234A/L235A/G236del/G237A; S228P/L235E). Dumet et al. also teach (page 1344, column 2, last paragraph) that joining an IgG2 (up to T260) with the end of an IgG4 Fc abolishes effector functions of the antibody.
It would have been prima facie obvious to modify the antibody of ‘185 to include any one or all of the improved functionality modifications taught by Dumet et al. in order to obtain an antibody which has increases terminal half-life, decreased half antibody formation and/or decreases effector function because these are desired properties for a therapeutic antibody. ‘185 claims methods of treatment using the anti-CCR5 antibody and Dumet et al. teach that it was well-known in the prior art before the effective filing date of the claimed invention in modify the IgG heavy chain to improve the functionality of antibodies which are going to be administered to subjects. One would be motivated to modify the antibody of ‘185 but including the mutations disclosed in Dumet et al. for the benefits which are described in Dumet et al. with a reasonable expectation of success based on the number of antibodies which have already been modified by such means as evidenced by the numerous antibodies identified in Dumet et al.
While ‘185 does not specifically claim the antibody with a pharmaceutically acceptable carrier, ‘185 does claim therapeutic methods which administer the antibody, which necessarily implies the use of a pharmaceutically acceptable carrier and such, a composition of the antibody of ‘185 modified by the mutations taught by Dumet et al. would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention. ‘185 also does not claim a kit which comprises the antibody however, ‘185 discloses that the antibody could be used in combination with other antibodies for diagnostic or detection purposes would be indicative of an assay which normally includes additional components such as diluents, wherein the different components of the kit are in separate containers. Even if ‘185 did not disclose such uses, it was well-known in the art that antibodies can be used in methods of detection and measuring the antigen to which the antibody binds and one of ordinary skill in the art would have readily envisioned a kit comprising the antibody of ‘185 which is modified by the mutations of Dumet et al. in a kit which comprised components such as a diluent for use in methods of detection/measuring CCR5. Lastly, while ‘185 does not specifically recite an antibody in lyophilized form, such would have been obvious because the antibody could be used for diagnostic or detection purposes with other antibodies, which is indicative of a kit and antibodies are commonly lyophilized for storage purposes or for including in assay kits because this form preserves the antibody. Therefore, the instant claims are not patentably distinct from the claims of ‘185 in view of Dumet et al. for the reasons provided.
Citation of Prior Art
Saunders, Kevin O. (2019) Conceptual Approaches to Modulating Antibody Effector Functions and Circulation Half-Life. Front. Immunol. 10: 1296. doi: 10.3389/Immu.2019.01296.
Namisaki et al. (2020) R409K mutation prevents acid-induced aggregation of human IgG4. PLoS ONE 15(3): e0229027. doi.org/10.1371/journal.pone.0229027.
Conclusion
No claim is allowed.
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/Christine J Saoud/Primary Examiner, Art Unit 1645
Prosecution Insights