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 .
DETAILED ACTION
Claim Status
Claims 1-16, 19-20 are currently pending. Claim 13 has been amended. Claims 17-18 are canceled. There are no new claims. Claims 1-4, 6, 9, 14-16 will be examined on the merits.
Election/Restrictions
Applicant’s election without traverse of Group I (claims 1-9, 14-16) in reply filed on February 19, 2026 is acknowledged. Claims 5, 7-8, 10-13, 19-20 are withdrawn from further consideration pursuant to 37 CFR 1.142 (b) as being drawn to nonelected invention, there being no allowance generic or linking claim. Applicants elected species of CDR sequences: HCDR1, HCDR2, HCDR3, LCDR1, LCDR2 and LCR3 of SEQ ID NO: 1, 3, 5, 81, 9 and 10, respectively; the VH of SEQ ID: 53, and/or the VL of SEQ ID NO: 82 in the remarks filed 02/19/2026.
Priority
Acknowledgement is made of applicant’s claim for foreign priority based on an application filed in Republic of China on November 5, 2020. Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55. However, certified English copies have not been filed. For the sake of searching the art, the effective filing date is November 4, 2021.
Information Disclosure Statement (IDS)
The IDS submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner. Signed copies of these statements are attached with this action. However, the IDS filed 05/05/2023 has no application number and the foreign references, CN111378043A, CN104507969A, CN104321430 and CN110035769 are in non-English language. Thus, these references have not been considered by the examiner.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
Claims 1-4, 6, 9 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 1, 4 and 9 recite the terms “preferably, more preferably, or both”. However, it is unclear which genus of isolated antibody binding to Siglec-15 is being claimed. Therefore, “preferably, more preferably, or both” is indefinite.
Claim 2 recites “conservatively modified variant”. However, no definition was provided in order to clarify the meaning of “conservatively modified variant”. The term is vague and can be understood under different textbooks, and patents use different definitions. Therefore, the scope of the claim is unclear in reference to “conservatively modified variant”.
Claim 4 recites the term “may be” a murine antibody, a chimeric antibody, a humanized antibody, a human antibody, or a fragment each thereof….”. However, it is unclear whether the claim is limited to these, or what else might be encompassed. Therefore, this recitation is indefinite.
Claims 1-3, 4 and 6 recite “one or more heavy chain CDR sequences” and “and/or, one or more light chain CDRs sequences”. However, it is unclear whether the claim is limited to these, or what else might be encompassed. Therefore, these recitations are indefinite.
The following is a quotation of the first paragraph 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.
Claims 1-9, 14-16 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains 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, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
The following quotation from section 2163 of the Manual of Patent Examination
Procedure is a brief discussion of what is required in a specification to satisfy the 35 U.S.C. 112 written description requirements for a generic claim covering several distinct inventions:
The written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice... reduction to drawings...or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus... See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406.
A "representative number of species" means that the species which are adequately described are representative of the entire 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.
Thus, when a claim covers a genus of inventions, the specification must provide written description support for the entire scope of the genus. Support for a genus is generally found where the applicant has provided a number of examples sufficient so that one in the art would
recognize from the specification the scope of what is being claimed.
Instant claim 1 recites an isolated antibody binding to Siglec-15 or an antigen binding fragment thereof, comprising one or more CDR sequences selected from a group consisting of SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, and 81; preferably, the isolated antibody binding to Siglec-15 or an antigen binding fragment thereof comprises one or more heavy chain CDR sequences selected from a group consisting of SEQ ID NOs: 1, 2, 3, 4, 5, 11, 12, 13, 17, 18, 19, 20, 25, 26, 27, 28, 29, 35, 36, and 37, and/or, one or more light chain CDR sequences selected from a group consisting of SEQ ID NOs: 6, 7, 8, 9, 10, 14, 15, 16, 21, 22, 23, 24, 30, 31, 32, 33, 34, 38, 39, 40, and 81. The “one or more CDR sequences” are iterated in claims 2, 4-9; as well applying the CDR sequences to claims 14-16;
Regarding the claims to an isolated antibody binding to Siglec-15 or an antigen binding fragment thereof, whereby requires a genus of antibodies which has one of the recited sequences as one of the CDRs binds to Siglec-15. Claim 1 discloses 41 alternative CDR sequences that may be combined to any alternative CDR sequences not claimed in the invention. Thus, the claims are interpreted to encompass a significant number of variant antibodies, comprising a sub-genus of any one of the isolated antibody binding to Siglec-15 or an antigen binding fragment thereof, of instant 41 recited sequences, with no limitation as to which CDRs may be substituted, or its combination with any other different antibody framework structure. The claims encompass a sub-genus of variant embodiments which comprise unidentified CDR sequences that were not claimed in the invention; thus, under the broadest reasonable interpretation, claim 1 encompass a genus of antibodies to bind Siglec-15. Further, the full genus of antibodies must be able to binding to Siglec-15.
However, it is apparent that the specification does not teach the full breath of genus, wherein an isolated antibody binding to Siglec-15 or an antigen binding fragment thereof, has only one of the 41 recited CDR sequences of claim 1.
The full genus of antibodies binding to Siglec-15 is unknown and/or not readily reproducible by the artesian. When determining the representative examples and the art, it is important to consider whether there is evidence of a singular shared structural feature which imparts the defining property of the claimed genus, and which would necessarily be present in every species of the claimed genus.
Thus, one of skill in the art would not readily recognize the use of one genus of antibodies, which is a CDR sequence claimed by the applicant if there is lack of written description of functionality, which is the ability of the genus to bind Siglec-15. Claim 1 is rejected for lack of adequate written description support.
Claim 2 recites “a conservatively modified variant each thereof” of the HCDR1-3 and LCDR1-3 sequences, whereby the alternative residues may occur at any positions within the 3 CDRs of the heavy chain and the 3 CDRs of the light chain sequences. The claim is interpreted to encompass a significant number of variant peptides, comprising a sub-genus of variant embodiments which comprise unidentified variant CDR sequences; with no limitation as to which residues may be substituted, or with which amino acids, and wherein the substitutions may occur anywhere any of the CDR sequences; thus, under the broadest reasonable interpretation, claim 2 encompasses a genus of anti-Siglec-15. Claim 2 is rejected for lack of adequate written description support.
In support of the claimed genus, the specifications disclose the variant of the antibody of the invention or an antigen binding fragment thereof may comprise one, two or three conservative amino acid substitutions. See specifications, page 15; paragraph [0063]. However, it is not clear what underlies the suggested substitutions as the alternative embodiments were not reduced to practice to demonstrate that they maintain binding to the target; no guidance it provided to the skilled artisan as to which substitutions to choose to incorporate. Further, the potential alternative residue substitutions are not claimed; rather, the claim encompasses numerous potential substitutions beyond those described in the specifications. When determining the representative examples and the art, it is important to consider whether there is evidence of a singular shared structural feature which imparts the defining property of the claimed genus, and which would necessarily be present in every species of the claimed genus.
Claim 3 is rejected as depending on claim 1, without rectifying the issues. The claim uses “and/or” language which suggests that the HCDRs and the LCDRs can be mixed and matched between the species, and therefore does not provide adequate descriptive support for all embodiments encompassed in the claims. Claim 3 is rejected for lack of adequate written description support.
Claim 4 is rejected as depending on claim 1, without rectifying the issues. In addition, claim 4 recites a “human antibody” which depends from the antibody of claim 1. Claim 1 defines the CDRs of the VH and VL of the antibody binding to Siglec-15. In support of the claimed genus of variants, the specifications disclose the preparation of hybridomas producing anti-human Siglec-15 monoclonal antibodies, wherein “fifteen mice (5 C57bl/6, 5 balb/c, and 5 SJL) were immunized with hS15-hFc emulsified with adjuvant and, 2 weeks later, boosted with hS15-hFc or hS15-D1-hFc” (Example 2; page 24; paragraph 0121). Thus, the defined CDRs, of claim 1 are murine antibodies/CDRs.
While it is known in the art that a murine antibody may be “humanized” by mutating various individual residues, usually in the framework regions only; it is also known in the art that “human” antibodies are those that are raised in humans. As humans are a different species that rodents, the CDRs of antibodies raised in humans, even if they bind the same antigen, would be wholly different from the amino acid sequences of antibodies raised in rodents. The specifications fail to disclose any fully human antibodies which have the CDRs set forth in claim 1, and the person skilled in the art cannot envision the structure of a fully human antibody which comprises the murine CDR sequences. Therefore, applicants have failed to provide a) a representative number of species to encompass the scope of the claimed genus of fully human antibodies which comprise the CDRs of claim 1 and which bind Siglec-15, or b) described the shared structural feature, encompassed in every species of the claimed genus, which imparts the defining property of the claimed genus. As no shared structure and no representative examples have been provided of fully human antibodies which comprise the murine CDRs of claim 1; the fully human antibodies of claim 4 are rejected for lack of adequate written description support.
Claim 5 recites the heavy chain and/or light chain variable regions having “at least 90%” of homology to a sequence. However, it is not clear what underlies the suggested substitutions as the alternative embodiments were not reduced to practice to demonstrate that they maintain binding to the target; no guidance it provided to the skilled artisan as to which substitutions to choose to incorporate. Further, the attempted consensus sequences, and potential alternative residue substitutions are not claimed; rather, the claims encompass numerous potential substitutions beyond those described in the specifications. When determining the representative examples and the art, it is important to consider whether there is evidence of a singular shared structural feature which imparts the defining property of the claimed genus, and which would necessarily be present in every species of the claimed genus. The specifications do not teach the physical features (or amino acid residues encoding said features) which impart the property of binding the same epitope of Siglec-15. Further, a description of the type and number of amino acid residue substitutions that may be made at such identified positions within the sequence, that result in “at least 90%, at least 95%, or at least 99%” sequence identity to a selected sequence, would be essential in determining the degree of variability that may be allotted in total sequence identity. This lack of definition complicates the determination of the boundaries of the claimed genus with regard to which, as of yet unidentified, species variants (variable domains with 90%, 95% or 99% identical sequences) would be anticipated, a priori, by one skilled in the art, to fall within the scope of the claims. Without the identification of the necessary shared structural properties of all species variants that fall within the scope of the genus, it may be that an embodiment species comprising an H3-CDR with < 90% in shared sequence identity to any of claimed sequences, would still bind Siglec-15; or conversely, that antibodies with > 99% sequence identity, but comprising a deleterious mutation in the H3-CDR region would lose functional binding to Siglec-15. The claims encompass a sub-genus of variant embodiments which comprise unidentified variant CDR sequences; thus, under the broadest reasonable interpretation, claim 5 encompasses a genus of anti-Siglec-15 polypeptides. Further, the “and/or” language separates the dependency of the VH and VL regions being combined. Thus, the VH and VL domains are highly promiscuous, and there is insufficient descriptive support for possession of a genus of VH and VL domains with at least 10% of amino acid substitutions or 90% sequence identity to the VL and VH domains of the isolated antibody or fragment thereof, which still maintains specificity for Siglec-15.
Claim 5 is rejected for lack of adequate written description support.
Claims 6-8 are rejected as lacking descriptive support as outlined for claims 1 above. The claims recite “an […] antibody binding to Siglec-15 […] with one or more mutations introduced at a position selected from the group consisting of […]”. The specification teaches that “In any of the embodiments described above, the variant of the antibody of the invention or an antigen binding fragment thereof may comprise one, two or three conservative amino acid substitutions” (see page 16, [0063]). However, the specification does not teach antibodies that have mutations in all of those positions claimed and still binding to Siglec-15. Claims 6-8 are rejected for lack of adequate written description support.
Claim 9 is also rejected as lacking descriptive support as outlined for claim 1 above. The claim recites the anti-Siglec-15 comprising a constant region or a variant thereof, preferably a IgG1 or IgG4 constant region or variant each thereof. In support of the claimed genus of variants, the specifications teach “the antibody of the invention or an antigen binding fragment thereof may comprise: a human heavy chain constant region or a variant thereof, wherein the variant comprises up to 20 conservative amino acid substitutions; and/or a human light chain constant region or a variant thereof, wherein the variant comprises up to 20 conservative amino acid substitutions. In some embodiments, the variant may comprise up to 10 conservative amino acid substitutions. In some embodiments, the variant may comprise up to 5 conservative amino acid substitutions. In some embodiments, the variant may comprise up to 3 conservative amino acid substitutions. In any of the embodiments described above, the human heavy chain constant region or a variant thereof may be IgG1, IgG2, IgG3, IgG4, IgA, IgE, IgM or IgD constant region or a variant each thereof, preferably, IgG1 or IgG4 constant region or a variant each thereof.” See for example page 16; [0064]. The specification teaches humanized protocols of heavy and light chain regions of chimeric antibodies, such as 124B11F6-hH1L1, 124B11F6-hH2L2, 124B11F6-hH3L3, 174C11C9- hH1L1, 174C11C9-hH2L2, 174C11C9-hH3L3, 21F6C6-hH1L1, 21F6C6-hH2L2, 21F6C6- hH2L3, 21F6C6-hH3L3, 21F6C6-hH2L4 and 21F6C6-hH4L4. See for example page 23; Figures 4-6.
However, the specification does not provide adequate descriptive support for all embodiments encompassed in the claim. Thus, claim 9 is rejected for lack of adequate written description support.
Claims 14-16 are also rejected as they depend from rejected claim 1, yet fail to resolve the issues of descriptive support over the scope of the claimed anti-Siglec-15.
Regarding the state of the art; it is known in the art that the antigen binding domain of an antibody requires the 6 complementarity determining regions (CDR) of the heavy and light chains, whereby the 3 CDRs of the heavy chain and the 3 CDRs of the light chain are structurally inter-dependent in forming the unique binding pocket of the antibody paratope region; and thus, the CDRs constitute critical aspects of the antibody paratope and ultimately impart the paratope-epitope binding functionality with regard to specificity and affinity (for review see MacCallum et al., 1996). However, the structure-to-function correlation continues to be highly unpredictable. For example, Chen et al., (1992) teaches that a single amino acid substitution in the VH CDR2 of PC-specific T15 antibody could increase, decrease or ablate binding the target antigen (abstract, Fig. 3), and this occurred in an unpredictable manner based on which residue was mutated. Similarly, a single point mutation in the heavy chain CDR3 region of the high affinity anti-VEGF antibody G6.31, could in some cases enhance, or otherwise completely ablate binding to the target antigen, and this also occurred in an unpredictable manner (Koenig et al., PNAS, 2017). That is, only screening each mutation individually provided insight as to the resulting changes in functionality. In some cases, this extends even beyond the CDRs. Within the framework regions, Koenig et al. (PNAS, 2017) teaches that various amino acid point mutations can increase or decrease binding or neutralization capacity. Some amino acid residues are more tolerant to substitution, while other “conserved” residues are less tolerant, such that a single amino acid substitution may defunctionalize the antibody (pg. E487, Figure 1).
Further, it is known that the heavy chain CDR2 and CDR3 regions contain most of the residues that have a major contribution to the binding free energy of the antigen binding domain (Dondelinger et al., 2018; page 8, column 1, paragraph 2 – column 2, paragraph 1). Regarding single domain antibodies (sdAbs), which comprise only a VHH heavy chain, comprising the 3 heavy chain CDRs, Sheriff et al., (1998) teaches that while the usual conception is that an antibody (or receptor) envelops its ligand, with sdAbs derived from camels, the antibody inserts a part of its binding surface deeply into a pocket on the surface of the ligand; and that about 70% of the total surface area buried in this interaction is contributed by CDR3 (page. 735, column 2, paragraph 2 – column 3, paragraph 1). Thus, the CDR3 of sdAbs is of considerable importance to the functionality of the sdAb with regard to specificity and affinity.
Thus, the hyper-variable regions, comprising the complementary set of CDRs, are well established in the art as the portion of the binding regions which impart the specificity of the antibody; and yet, there is no way to look at an amino acid sequence and envision, a priori, whether the combination of CDRs will bind a particular epitope, even when the CDRs are highly related, without teachings of the basic shared amino acid residues that are sufficient to impart functional binding across all variants. Further, even when provided with several related antibodies that bind the desired target, this does not represent the potentially unknowable breadth of all possible amino acid sequences which will result in the desired binding properties. This is exemplified by the Court decision in Abbvie (Abbvie v Janssen 759 F.3d 1285 (Fed. Cir. 2014)), where Abbvie developed over 200 antibodies that shared 99.5% identity in the variable regions (pg. 7) and which bound the target, but in no way allowed one to envisage the unique structure of Centocor’s antibodies which bound the same target but shared only 50% sequence similarity (see table on pg. 11). Thus, when claiming a genus of antibodies, or antigen binding polypeptides, based on their binding to a common target, the representative examples must cover the full scope of structural variabilities which encompass all species variants that would bind the target.
Section 2163(II)(A)(3)(a)(ii) of the MPEP states that the written description for a claimed genus may be satisfied through either a) a representative number of species, or b) disclosed correlation between function and structure. Here the applicants do not provide any variants of the claimed embodiments, in which alternative mutations were made, which were reduced to practice; nor do they identify the shared structural properties of the variants, such as the CDR residues or humanized framework regions, that would define the genus beyond the desired functionality.
Thus, one of skill in the art would not readily recognize the use of one genus of antibodies claimed by the applicant if there is lack of written description of the ability of the genus to bind Siglec-15. The written description requirement is not fulfilled by the applicant. The written description requirement is not fulfilled by the applicant.
“The purpose of the written description requirement is to ‘ensure that the scope of the right to exclude, as set forth in the claims, does not overreach the scope of the inventor’s contribution to the field of art as described in the patent specification.’” Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1353-54 (Fed. Cir. 2010) (en banc) (quoting Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 920 (Fed. Cir. 2004)). To satisfy the written description requirement, the specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. Vas-Cath, Inc. v. Mahurkar, 935 F.2d 1555, 1562-63, 19 USPQ2d 1111 (Fed. Cir. 1991). See also MPEP 2163.04. Otherwise, the “claims merely recite a description of the problem to be solved while claiming all solutions to it and … cover any compound later actually invented and determined to fall within the claim’s functional boundaries- leaving it to the pharmaceutical industry to complete an unfinished invention.” Ariad Pharmaceuticals, Inc. v. Eli Lilly and Co., 598 F.3d 1336, 1353 (Fed. Cir. 2010).
The MPEP states that the purpose of the written description requirement is to ensure that the inventor had possession, as of the filing date of the application, of the specific subject matter later claimed. The MPEP lists factors that can be used to determine if sufficient evidence of possession has been furnished in the disclosure of the application. These include “level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention.”
The written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, disclosure of drawings, or by disclosure of relevant identifying characteristics, for example, structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the Applicants were in possession of the claimed genus.
Therefore, neither the art nor the specification provide the full antibodies genus that can be bound to Siglec-15 as claimed by the invention.
MPEP § 2163.02 states, “[a]n objective standard for determining compliance with the written description requirement is, 'does the description clearly allow person of ordinary skill in the art to recognize that he or she invented what is claimed’”. The courts have decided: the purpose of the "written description" requirement is broader than to merely explain how to "make and use"; the Applicant must convey with reasonable clarity to those skilled in the art, that as of the filing date sought, he or she was in possession of the invention. The invention is for purposes of the “written description” inquiry, whatever is now claimed. See Vas-Cath, Inc v. Mahurkar, 935 F.2d 1555, 1563-64, 19 USPQ2d 1111, 1117 (Federal Circuit, 1991).
Furthermore, the written description provision of 35 USC §112 is severable from its enablement provision; and adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method for isolating it. Fiers v. Revel, 25 USPQ2d 1601, 1606 (CAFC 1993). And Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. Moreover, an adequate written description of the claimed invention must include sufficient description of at least a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics sufficient to show that Applicant was in possession of the claimed genus. However, factual evidence of an actual reduction to practice has not been disclosed by Applicant in the specification; nor has Applicant shown the invention was “ready for patenting” by disclosure of drawings or structural chemical formulas that show that the invention was complete; nor has the Applicant described distinguishing identifying characteristics sufficient to show that Applicant were in possession of the claimed invention at the time the application was filed.
Therefore, for all these reasons the specification lacks adequate written description, and one of skill in the art cannot reasonably conclude that Applicant had possession of the claimed invention at the time the instant application was filed.
In view of this uncertainty and the lack of a representative number of examples of the claimed genus, the claims 1-2, 4-9, 14-16 are rejected for lack of adequate written description support.
In order to comply with the written description requirement, the applicant must fully disclosure the full genus of antibodies to bind Siglec-15 by the applicant’s invention in the specifications.
Allowable Subject Matter
All claims are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. However, the elected species of HCDR1, HCDR2, HCDR3; SEQ ID NO: 1, 3, 5 (HCDR1-3 of SEQ ID: 82), the LCDR1, LCDR2 and LCR3; SEQ ID NO: 81, 9, 10 (LCDR1-3 of SEQ ID NO: 82); the VH of SEQ ID: 53 (21F6C6-hH2L2 VH), and/or the VL of SEQ ID NO: 82 (21F6C6-hH2L4V VL), have been searched and are free of the prior art. Thus, the embodiments of claim 3, regarding the elected species mentioned above would otherwise be allowable.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to PRICILA HAUK TEODORO whose telephone number is (571) 272-2784. The examiner can normally be reached M-F 6:15 AM-3:00 PM.
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/PRICILA NMN HAUK TEODORO/Examiner, Art Unit 1645
/HEATHER CALAMITA/Supervisory Patent Examiner, Art Unit 1684
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