DETAILED ACTION
1. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
2. Applicant's election with traverse of the invention of Group I in the reply filed on 01/12/2026 is acknowledged.
The traversal is based on the assertion that it would not be unduly burdensome to examine the inventions together.
This is unpersuasive, because search burden is not a consideration in national stage applications submitted under 35 USC 371, which are evaluated for unity of invention under 37 CFR 1.499 and 37 CFR 1.475.
The restriction requirement is still deemed proper and is therefore made FINAL.
Claim 34, and claim 41 dependent thereon, are withdrawn from further consideration by the Examiner under 37 C.F.R. § 1.142(b) as being drawn to nonelected inventions.
Claims 1-2, 5-6, 13-14, 16, 19, 21-24, 27, 29, 31, 39 and 42-45 are presently under consideration.
3. 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.
4. Claims 16, 21-23 and 29 are rejected under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor regards as the invention.
(i) Claim 16 is indefinite in the recitation of alternative conditions (a)-(c) connected by the conjunction “and/or,” because the conjunction “and” requires that the alternative conditions be present in the same embodiment.
(ii) Claims 21 and 22 are indefinite in the recitation of “high” and “low” molecular weight species, and in the recitation of “acidic” and “basic” species, because the relative terms “high,” “low,” “acidic,” and “basic” are not defined by the claim, and the specification does not appear to provide a standard for ascertaining the respective degree so as to determine whether a specific value is within the scope of the claim.
(iii) Claim 23 is indefinite in the recitation of a “formulation” which has the specified “volume,” because the two terms are incompatible. “Volume” is not a property of a “formulation,” but rather of the packaging of the formulation, and as such does not define the formulation.
(iv) Claim 29 is indefinite in the recitation of a “stabilized” IgG4 constant region, because the requisite degree of stability is not defined.
In view of the above, a person of ordinary skill in the art cannot unequivocally interpret the metes and bounds of the claims so as to understand how to avoid infringement. Applicant is reminded that any amendment must point to a basis in the specification so as not to add New Matter. See MPEP 714.02 and 2163.06.
5. The following is a quotation of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
6. Claims 1-2, 5-6, 13-14, 16, 19, 21-24, 29 and 39 are rejected under 35 U.S.C. 112(a) as failing to comply with the written description requirement. The claim(s) contain(s) subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, at the time the application was filed, had possession of the claimed invention.
Specifically, the inventor or a joint inventor is not in possession of a generically recited “protein comprising an antigen binding domain that binds to or specifically binds to G-CSF receptor (G-CSFR).”
The recited genus of proteins is defined solely by their ability to bind G-CSFR, i.e. by their function, without imposing any limitations on the structure of the proteins.
The specification discloses amino acid sequences of anti-G-CSFR antibody C1.2, its almost identical derivative C1.2G, and several variants of HCDR3 and LCDR3 of C1.2.
It is well established in the art that the antigen-binding properties of antibodies are primarily, although not exclusively, determined by the amino acid sequences of their CDR regions, and that antibodies having a broad variety of CDR sequences can bind to the same epitope, compete with each other, and possess essentially the same antigen-binding and other functional properties. For example, Khan et al. (2017) identified two antibodies from HIV patients which competed with two known mAbs specific for the CD4 binding site on HIV gp120 (p. 2-6). The two new mAbs had unrelated CDRH3 and CDRL3 sequences. Zhu et al. (2015) analyzed co-crystal structures of 16 mAbs recognizing the same CD4-binding site on the HIV gp120, and found two main types, whose binding interfaces were dominated by either CDRH2 or CDRH3. Some mAbs of the first group and all four mAbs of the second had unrelated CDR sequences, indicating that the immune system finds diverse structural solutions for the same antibody specificity. Lee et al. (2016) identified three groups of cross-competing anti-HA antibodies in human sera after influenza vaccination (e.g. p. 1458-1462). Antibodies within each group differed in CDRH3 and CDRL3 sequences, including the length, hydrophobicity and/or charge (id.), i.e. repertoires of antibodies to the same epitope differ greatly between individuals. Abdiche et al. (2016) characterized epitope diversity of mAbs obtained by chicken or mouse immunization and by phage display. Some epitopes were recognized by both chicken and mouse mAbs, while some were chicken-specific or mouse-specific, with chicken antibodies covering a broader range of epitopes (e.g. p. 265-270). Each epitope could be recognized by mAbs having unrelated CDR sequences (e.g. p. 268 and Figs. 3 and 4). Konitzer et al. (2017) generated 694 mAbs against GIPR by chicken immunization, 462 of which had unique sequences. When 40 chicken and 5 rodent anti-GIPR mAbs were tested by cross-competition they formed 5 epitope clusters, each containing from 6 to 12 unique mAbs. Ferrara et al. describe a method for generating polyclonal pools of antibodies by combining phage and yeast display. Applied to ubiquitin, the method generated 107 distinct HCDR3 clusters (groups which differ by no more than one amino acid from the commonest HCDR3). For eight other targets, the numbers of unique HCDR3 clusters ranged from 74 to 460 (p. 33-35). Parola et al. (2018) teach that combining antibody display with high-throughput sequencing makes it possible to isolate a greater variety of epitope-specific mAbs than either method alone. This approach yielded 40 mutants of an anti‐ErbB2 mAb with improved affinity. While those skilled in the art are aware of the extensive allelic variation of germline antibody gene segments in the human population, the present knowledge underestimates the extent of genetic diversity, as novel alleles are continually being identified (Boyd et al. (2016); e.g. p. 105-107). Accordingly, the instant claims encompass a genus of antibodies with an extremely broad variety of CDR sequences.
The written description requirement for a claimed genus may be satisfied either through sufficient description of a representative number of species, or by disclosure of relevant, identifying characteristics, i.e., structure or other properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics. MPEP 2163(II)(A)(3)(a)(ii).
A "representative number of species" means that the species which are adequately described are representative of the entire genus. For inventions in an unpredictable art, written description of a genus which embraces widely variant species must adequately reflect the structural diversity of the claimed genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus. MPEP 2163(II)(A)(3)(a)(ii).
As amply demonstrated by the references cited above, it is impossible for the skilled artisan to even estimate the size of the genus of possible CDR sequences of antibodies which can bind to the same epitope or compete for binding with the specified antibody, let alone visualize or recognize the identity of such sequences. As such, the outer boundary of the claimed genus is unknown, both in terms of size and structural diversity. Thus, neither applicant’s disclosure nor the knowledge in the art allows the skilled artisan to predict the undisclosed members of the genus. Accordingly, the disclosed antibodies are not representative of the structural diversity of the recited genus.
Next, we address whether there is a known or disclosed correlation between the recited functions of binding to or competing for an epitope, and the structural features which must be possessed by antibodies to accomplish these functions. The specification does not disclose such correlation, and the teachings of the references cited above make it abundantly clear that at the present state of the art the skilled artisan cannot visualize or recognize the vast genus of possible CDR sequences which would endow an antibody with the recited properties. It is impossible for the skilled artisan to know in perfect detail the physiological and genetic backgrounds of all immune systems capable of producing antibodies, nor their prior immunological exposure.
Van Regenmortel (2018) highlights the difficulties inherent in immunological “inverse problems,” which start with the result (e.g. binding to an epitope) and then try to guess the multiple causes (i.e. structures) that could have produced it. According Van Regenmortel, the extent of the immune system degeneracy, including the ability of numerous different antibodies and T cell receptors to bind to the same epitope, is still underappreciated. Kanyavuz et al. (2019) review unconventional strategies of diversifying the repertoire of human antibodies far beyond that generated by VDJ recombination and somatic mutations, which include insertion of large amino acid sequences, post-translational modifications, conformational heterogeneity and use of nonprotein cofactors. Examples include an insertion of 98 amino acids from LAIR1 into the VH region; a different LAIR1-containing antibody with a camel-like structure lacking CH1 and the entire light chain; and insertions of 100–1,000 nucleotides from other chromosomes into the elbow region (p. 356). Additionally, about 2% of circulating B cells contain in-frame insertions or deletions of 3 to 33 nucleotides in the V regions, mostly in the CDRs but also in the framework (p. 357). Another diversification strategy is a global reconfiguration of the Fab region, as exemplified by human anti-HIV-1 antibody 2G12. Its Fabs form a tight side-by-side dimer resulting from mutations which weaken VH/VL contacts and create a favorable VH/VH interface. The antibody has a compact linear configuration, as opposed to Y- or T-shape of typical antibodies, with an extended binding surface composed of four antigen-binding sites (p. 361-362).
The difficulty of accounting for all types of antibody structures capable of binding a specific epitope is further compounded by inter-species differences, as well as by the potential of synthetic and other specialized antibody display libraries. For example, Conroy et al. (2017) review the broad variety of vertebrate antibody structures and mechanisms of generating antibody diversity. While repertoire of a species may comprise billions of paratopes, interspecific differences provide access to novel structural features (p. 14-16). Camelid VHH have a higher rate of hypermutation and cysteine usage, creating greater sequence and length diversity of CDRH1 and CDRH2. Shark VNAR is the most distant evolutionarily from mammalian antibodies, and display technologies have been successfully applied to select specific binders from VNAR libraries. Chicken utilize gene conversion and cysteine incorporation for creating enormous repertoire diversity, the latter resulting in intra- and inter-CDR disulfide bonds creating “mosaic” CDRs. Ultra-long CDRH3 of cow antibodies present unique paratope topology containing disulfide-bonded mini-folds (p. 14-16). Sheehan et al. (2015) review the diverse types of libraries used in antibody display systems which differ in repertoires and allow selection of specialized types of antigen-specific antibodies. Naïve libraries have the diversity of the antigen-unbiased variants, while immune libraries are enriched for antigen-reactive variants of affinity matured VH and VL, which allows significantly more unique mAbs to be isolated by phage library than by hybridoma screening. Synthetic libraries designed to obtain specific immunogenetic profiles for a variety of purposes have been developed.
The above examples clearly demonstrate the absence of a known correlation between the ability of an antibody to perform a certain function and the structure of antibodies possessing this function.
To summarize, present specification does not describe a representative number of species or structural features common to the species encompassed by generic claims, nor is there a known or disclosed correlation between function and structure; therefore, the specification fails to satisfy the written description requirement of 35 U.S.C. 112(a).
7. Claims 2, 21-22 and 44 are rejected under 35 U.S.C. 112(a) because the specification, while being enabling for:
a liquid pharmaceutical formulation comprising a generically recited G-CSF-binding protein at a concentration of up to 50 mg/mL, wherein the formulation does not satisfy the conditions recited in claims 19, 21 and/or 22, and
a liquid pharmaceutical formulation comprising a G-CSF-binding protein as defined in claim 27 or claim 31 at a concentration of at least 50 mg/mL, wherein the formulation satisfies the conditions recited in claims 19, 21 and/or 22, and wherein the formulation composition is as defined in claim 45,
does not reasonably provide enablement for:
a liquid pharmaceutical formulation comprising a generically recited G-CSF-binding protein at a concentration of at least 50 mg/mL,
a liquid pharmaceutical formulation comprising a generically recited G-CSF-binding protein wherein the formulation satisfies the conditions recited in claims 19, 21 and/or 22,
a liquid pharmaceutical formulation comprising a G-CSF-binding protein as defined in claim 27 or claim 31 at a concentration of at least 50 mg/mL, and wherein the formulation composition is other than as defined in claim 45, or
a liquid pharmaceutical formulation comprising a G-CSF-binding protein as defined in claim 27 or claim 31, wherein the formulation satisfies the conditions recited in claims 19, 21 and/or 22, and wherein the formulation composition is other than as defined in claim 45.
The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the invention commensurate in scope with these claims without undue experimentation.
Factors to be considered in determining whether undue experimentation is required to practice the claimed invention are summarized in In re Wands (858 F2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988)). The factors most relevant to this rejection are the scope of the claim, the amount of direction or guidance provided, limited working examples, the unpredictability in the art and the amount of experimentation required to enable one of skill in the art to make and use the claimed invention.
To the specification states at [0520]: “The aim of the experiments described in the following examples was to produce a formulation of CSL324, an antibody that binds to GCSF-R, which had long term stability and was suitable for subcutaneous administration.” The working examples that follow describe experiments wherein a broad variety of formulation compositions of one specific antibody were tested, to select a composition satisfied the requirements for subcutaneous administration, including high antibody concentration with acceptable viscosity and limited aggregation.
Kollar et al. (2020) review the challenges of developing high concentration monoclonal antibody formulations suitable for subcutaneous administration. In particular, Kollar notes concentrations above 50 mg/mL pose particular challenges from a product development perspective (e.g. the Abstract). Extensive trial-and-error experimentation is required, because each antibody has different physical and chemical properties, and requires a unique set of conditions to obtain a formulation with the desired properties.
Instant claim 1 is not limited to an antibody, but encompasses proteins of any structure which can bind G-CSF. Claims 1, 5-6, 13-14 and 16 generically recite a broad range of parameters typically used in optimizing biopharmaceutical formulations. Given these generic starting conditions, a person of skill in the art would have to engage in extensive trial-and-error experimentation, separately for each particular G-CSF-binding protein or antibody, in order to discover a composition with suitable properties.
Accordingly, the entire scope of experimentation required to develop formulations with the recited properties for each of the almost infinite number of proteins within the scope of the claims is left to those skilled in the art, the present claims and disclosure amounting to nothing more than an invitation to the skilled artisan to invent such formulations.
8. The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
9. Claims 1-2, 5, 19, 21-24, 27, 31, 39, 42 and 44 are rejected under 35 U.S.C. 102(a)(1) and 35 U.S.C. 102(a)(2) as being anticipated by Morris et al. (US 20160368980).
Morris teaches inhibitors of granulocyte colony stimulating factor (G-CSF) and of G-CSF receptor (G-CSFR) (e.g. the Abstract), in particular anti-G-CSFR antibody CSL324 (e.g. [0052]), which is the same antibody as used in the working examples described in the present specification (e.g. Example 2 et seq.).
Morris teaches formulations of the antibody comprising an organic acid buffer, such as citrate or acetate buffer of about pH 4.0-5.5 (e.g. [0070]-[0072]), amino acids such as arginine, and non-ionic surfactants such as polysorbate 20 and polysorbate 80. These formulations are within the scope of instant claims 1, 5, and 24, and as such anticipate at least these claims.
Claims 2, 19, 21-22, 42 and 44 are included in the rejection because, since Morris’ formulations are the same as recited in claim 1, they inherently support the same antibody concentrations and have the same properties as the formulation of claim 1.
Claims 27 and 31 are included, because anti-G-CSFR antibody CSL324 described by Morris is the same anti-G-CSFR antibody CSL324 used in the present application, and as such inherently comprises the same animo acid sequences.
Claim 23 is included, because a formulation can be dispensed in any volume, including the recited volumes.
Claim 39 is included, because a person of skill in the art would at once envisage a prefilled syringe or autoinjector device in view of a therapeutic antibody formulation.
Accordingly, Morris teaches all of the limitations of the present claims, and as such anticipates the claimed invention.
10. 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 of this title, 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.
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.
11. Claims 1-2, 5-6, 13-14, 16, 19, 21-23, 29, 39, 42 and 44 are rejected under 35 U.S.C. 103 as being unpatentable over Morris et al. (US 20160368980) in view of Morichika et al. (US 8568720, of record), Mandelin et al. (US 20230235046), and Kollar et al. (2020).
Morris’ teachings, described in section 9 above, include formulations of anti-G-CSFR antibody CSL324 comprising an organic acid buffer of pH 4.0-5.5, amino acids such as arginine, and non-ionic surfactants such as polysorbate 80.
Although Morris does not specifically exemplify all of the ingredients and concentration ranges recited in claims 6, 13 and 16, these were well-known and routinely used in optimizing therapeutic antibody formulations by those skilled in the art before the effective filing date of the claimed invention, as illustrated e.g. by the teachings of Morichika, Mandelin, and Kollar.
Instant claim 16 recites in embodiment (a) an antibody formulation comprising:
12-30 mM histidine buffer, pH 5.5-5.9
0.02-0.04% polysorbate 80,
60-125 mM proline, and
60-125 mM arginine.
The limitations of claims 6 and 13 are broader than those of claim 16.
Mandelin teaches (claim 1) a stable pharmaceutical formulation comprising up to 100 mg/ml of an antibody, and
5-50 mM histidine buffer pH 5.5-6.5,
0.01-0.1% polysorbate, and
150-400 mM proline.
Morichika teaches (claim 1) a stable liquid formulation suitable for subcutaneous administration comprising 180 mg/mL a humanized antibody, and:
20 mM histidine buffer, pH of 6.
0.005-3% polysorbate 80, and
100 mM arginine.
Kollar reviews the state of the art of developing stable high concentration antibody formulations, which involves optimization of concentrations of several common ingredients, including histidine buffer, arginine and proline (Table 2), and polysorbate 80 (p. 35). Kollar highlights the significant advantages of stable high concentration antibody formulations (e.g. p. 31-32), thereby providing a strong motivation for those skilled in the art to develop such formulations.
Before the effective filing date of the claimed invention, it was routine in the art to adjust administration regimen to meet the needs of the patient. The frequency of administration required to achieve a specified trough serum concentration of a therapeutic agent while minimizing adverse events is a result effective variable. It is well settled that discovery of an optimum value of a result effective variable in a known process is ordinarily within the skill of the art. MPEP § 2144.05, part II(A). Further, it has been held that where the general conditions of a claim are disclosed in the prior art, discovering the optimum or workable ranges involves only routine skill in the art. In re Aller, 220 F2d 454,456,105 USPQ 233; 235 (CCPA 1955). See MPEP § 2144.05, part IIA.
Claims 2, 19, 21-23, 39, 42 and 44 are included in the rejection for the same reasons as articulated in section 9 above.
Claim 29 is included in the rejection, because Mandelin’s formulation comprises bexmarilimab, which is an IgG4 antibody comprising S241P in the hinge region to increase stability by preventing Fab arm exchange and formation of a half-antibody, i.e. Mandelin’s formulation comprises an antibody with a stabilized IgG4 constant region.
Therefore, the invention as a whole was prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention, as evidenced by the references, especially in the absence of evidence to the contrary.
12. Claims 1-2, 5-6, 13-14, 16, 19, 21-24, 27, 29, 31, 39, 42 and 44 are rejected under 35 U.S.C. 103 as being unpatentable over Johnston et al. (US 20240277839) in view of Morris et al. (US 20160368980) and Kollar et al. (2020).
Johnston teaches high concentration antibody formulations of the same composition as recited in claims 1, 5-6, 13-14, and 16. Specifically, Johnston teaches and claims a liquid pharmaceutical formulation comprising at least 100 mg/ml of an antibody, wherein the formulation has a pH of 5.8 to 6.4 and comprises 12 mM to 25 mM L-histidine buffer, 0.01% to 0.03% (w/v) polysorbate 80, 90 mM to 150 mM L-proline, and 100 mM to 160 mM L-arginine monohydrochloride (e.g. claims 1 and 16).
Although the antibody in Johnston’s formulation is different than the antibody in the formulations of the present claims, Morris (described in section 9 above) teaches therapeutic applications of pharmaceutical compositions comprising anti-G-CSFR antibody CSL324 (same as the antibody of the present claims), and Kollar (described in section 11 above) provides both motivation for and expectation of success in developing high concentration formulations of therapeutic antibodies.
Claims 2, 19, 21-23, 27, 31, 39, 42 and 44 are included in the rejection for the same reasons as articulated in section 9 above. Claim 29 is included in the rejection, because the antibody in Johnston’s formulation comprises a stabilized IgG4 constant region (e.g. claims 28-29)
At least in view of the above, the invention as a whole was prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention, as evidenced by the references, especially in the absence of evidence to the contrary.
13. 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 §§ 706.02(l)(1) - 706.02(l)(3) 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 USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The 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/process/file/efs/guidance/eTD-info-I.jsp.
14. Claims 1-2, 5-6, 13-14, 16, 19, 21-24, 27, 29, 31, 39, 42 and 44 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over the claims of copending applications USSN 18/004004 (published as US 20240277839) and USSN 18/715228 (published as US 20250042984), in view of Morris et al. (US 20160368980) and Kollar et al. (2020).
Although the claims at issue are not identical, they are not patentably distinct from each other because the instant claims are obvious over the claims of each of the copending applications in view of Morris and Kollar.
USSN ‘004 is published as Johnston et al. (US 20240277839) described in section 12 above, which describes the subject matter recited in Johnston’s claims 1 and 16, and articulates the reasons why instant claims are obvious over the Johnston’s claims.
Claims 1, 2 and 16(iii) of USSN ‘228 recite a liquid pharmaceutical formulation comprising at least 100 mg/ml of an antibody, wherein the formulation has a pH of 5.4-5.6 and comprises 20 mM histidine buffer, 0.03% (w/v) polysorbate 80, 100 mM proline and 100 mM arginine. These ingredients and concentration ranges are within the scope of instant claims 1, 5-6, 13-14, and 16.
Although the antibody in the formulation recited in USSN ‘228 is different than the antibody in the formulations of the present application, instant claims would have been obvious over the claims of USSN ‘228 in view of Morris and Kollar for the same reasons as articulated in section 12 above. Claim 29 is included in the rejection, because the antibody in the formulation recited in USSN ‘228 comprises a stabilized IgG4 constant region (claim 32).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
15. Claims 43 and 45 are objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all relevant limitations of the base claim and any intervening claims.
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/ILIA I OUSPENSKI/ Primary Examiner, Art Unit 1644