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 .
Priority
The current application is a 371 of PCT/US2022/075207 filed 08/19/2022. PCT/US2022/075207 claims priority to PRO 63/235425 filed 08/20/2021. The claims are all examined using this earlier filing of 08/20/2021.
Claim Status
Claims 4, 6, 8, 18, 23-24, and 27-58 were cancelled prior to examination. Claim 1 is the only independent claim. Claims 1-3,5,7,9-17,19-22 and 25-26 are pending and under examination.
Drawings
Nucleotide and/or Amino Acid Sequence Disclosures
Specific deficiency – Nucleotide and/or amino acid sequences appearing in the drawings, are not identified by sequence identifiers in accordance with 37 CFR 1.821(d)(See Fig. 13A). Sequence identifiers for nucleotide and/or amino acid sequences must appear either in the drawings or in the Brief Description of the Drawings.
Required response – Applicant must provide:
Replacement and annotated drawings in accordance with 37 CFR 1.121(d) inserting the required sequence identifiers;
AND/OR
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required sequence identifiers into the Brief Description of the Drawings, consisting of:
A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
A copy of the amended specification without markings (clean version); and
A statement that the substitute specification contains no new matter.
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.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1, 3, 5, 7, 9-15, and 17 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.
Claim 1 recites “comprising or consisting essentially of,” reciting two translational phrases of different legal scope in the alternative. “Comprising” is open-ended while “consisting essentially of” is a hybrid transitional phrase that limits the claim to the recited elements and those that do not materially affect the basic and novel characteristics of the claimed invention. Reciting both in the alternative renders it unclear which standard governs the claim’s scope, and as to the “consisting essentially of” branch, the specification does not identify the basic and novel characteristics against which materiality would be assessed. Applicant is required to select a single translational phrase.
Claim 1 further recites “at least a portion of a beta-2 microglobulin domain” and “at least a portion of a[n]… HLA-B*35… alpha chain.” Neither the claim nor the specification places any lower bound on what constitutes a qualifying “portion”, structurally, functionally, or by minimum length, such that the metes and bounds of the claim cannot be determined with reasonable certainty. It is unclear, for example, if a single amino acid would satisfy the claim.
Claim 1 further recites “a pharmaceutically acceptable derivative thereof.” The term “derivative” does not identify what modification to the recited SCT polypeptide fall within its scope, rendering the boundary of the claim indeterminate.
Claims 3, 5, 7, and 17 each recites that the first linker is “at least about [X}% homologous to” a named sequence. The specification defines “homologous,” “homology,” and “percent homology” only with reference to a formula for comparing nucleic acid sequences, while the claims apply this percentage to amino acid sequences (see [0093] of the instant specification). The specification does not identify which algorithm, scoring matrix, gap penalty, or other parameters are to be used for the claimed amino acid “homology” comparison, nor does it reconcile this term with the separately defined “percent sequence identity” (which does specify ALIGN-2 as the applicable algorithm for amino acid comparison; see [0090]-[0091] of the instant specification). Because “homologous” as applied to amino acid sequences is not a fixed, art standard metric absent specified parameters, and because the specification’s own definition of the term is directed to nucleic acids rather than the polypeptides actually claimed, a person of ordinary skill cannot determine with reasonable certainty which sequences fall within the claimed percentage thresholds.
Claims 9-15 each recites one or more amino acids substitutions “compared to a wild-type HLA-B*35 alpha chain.” HLA-B*35 is not a single, fixed molecular sequences but a serotype encompassing numerous distinct, named allelic subtypes, the specification itself lists twenty as viable options for the claimed “HLA-B*35 alpha chain” without designating any one of them as a reference “wild-type” sequence against which the recited substitutions are to be measured (see [0113] of the instant specification). This ambiguity is not merely theoretical, the specification discloses that the claimed S116F substitutions correspond to the native, unsubstituted, residue in at least two of the twenty listed subtypes, HLA-B*3503 and HLA-B*3506 (see [0210] of the instant specification). Consequently, whether a given polypeptide “comprises” the claimed substitution(s) depends entirely on which of the twenty disclosed subtypes is taken as the wild-type reference, a choice the claims and specification never make. A person of ordinary skill in the art cannot determine, with reasonable certainty, the scope of these claims. Claim 14 likewise recites “the linker has an amino acid substitution {G2C}” without ever citing a starting linker sequence in which the substitution is to be made.
Claim Interpretation
For purposes of examination, certain claim terms that are broad or otherwise require construction have been interpreted in accordance with their broadest reasonable interpretation consistent with the specification, as is required during prosecution. See MPEP 2111; In re Am. Acad. of Sci. Tech. Ctr., 367 F.3d 1359, 1369, 70 USPQ2d 1827, 1834 (Fed. Cir. 2004). The following claim constructions have been applied in this office action. This construction section governs application of the art below. Where a rejection depends on a construction issue not addressed here, it is separately noted within that rejection.
Claim 1: for purpose of compact prosecution and without conceding that “comprising or consisting essentially of” is a proper of definite transitional phrase, the Examiner interprets claim 1 and each claim depending therefrom under the “comprising” standard, i.e., an open ended and not limited to the recited elements.
Claims 3, 5, 7, and 17: for purposes of compact prosecution and without conceding that “homologous” as applied to the claimed amino acid sequences has a definite, ascertainable meaning under the specifications stated definitions, the Examiner interprets the claimed percentage “homology” thresholds in claims 3, 5, 7, and 17 as percentage sequence identity, consistent with the specification’s separately defined “percent sequence identity” metric.
Claims 9-15: for purposes of compact prosecution and without conceding that the specification supports any particular HLA-B*35 subtype as the default “wild-type” reference, the Examiner interprets claims 9-15 as if HLA-B*35:01 were the wild-type HLA-B*35 alpha chain against which the recited substitutions are measured. This interpretation is adopted solely to permit the prior art analysis below to proceed on a single, stated basis and to give Applicant a concrete target for either traversing the indefiniteness rejection above or amending the claims to resolve it. It is not a finding that HLA-B*35:01 is the wild-type sequence intended by the claims, nor a waiver of the indefiniteness rejection set forth above. Should applicant amend the claims to specify a different subtype as the refence, or to recite the resulting amino acid identity directly rather than by comparison to a wild-type, the prior art rejections below will be reassessed accordingly.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claims 1-3, 5, 7, 9-17, 19-21, 26 are rejected under 35 U.S.C. 102(a)(1)/102(a)(2) as anticipated by or, in the alternative, under 35 U.S.C. 103 as obvious over Dalmas. (US 2020/0062819 A1, published Feb. 27, 2020).
In regards to claim 1, Dalmas discloses a single chain trimer (SCT) polypeptide, termed a “comPACT", comprising a first universal target peptide, antigenic peptide, a second universal target peptide that is distinct from the first universal target peptide [first linker, as the second universal target peptide “further comprises a linker”(see Dalmas [0041]), a beta-2 microglobulin (β2M) peptide, and an major histocompatibility complex (MHC) peptide (see Dalmas [0031]). Dalmas further discloses “the polypeptide comprises a second linker sequence between the β2M sequence and the MHC allele sequence” (see Dalmas [0042]).
Dalmas discloses that the MHC peptide is a class I HLA peptide comprising an HLA-B allele and expressly lists HLA-B35:01 and HLA-B35:03 among the discloses alleles, each correspond to disclosed sequences (see Dalmas [0035], [0037], [0045]; SEQ ID NOs: 70 and 88 (peptide), 140 and 158 (nucleotide)).
In regards to claim 2, Dalmas’s disclosed linker sequences (e.g., SEQ ID NOs: 9, 11, 13, 15, 17, and 19) are peptide sequences.
In regards to claim 3, Dalmas discloses a first linker having the sequence shown in SEQ ID NO: 15, GCGGSGGGGSGGGGS, which is 100% identical to SEQ ID NO: 1 of the instant application.
In regards to claim 5, Dalmas discloses a first linker having the sequence shown in SEQ ID NO: 19, GGGGSGGGGSGGGGSGGGGS, which shares 18 of the 20 identical residues, i.e., “at least about 90% homologous”, to GCGASGGGGSGGGGSGGGGS of SEQ ID NO: 2 of the instant application.
In regards to claim 7, Dalmas discloses a first linker having the sequence shown in SEQ ID NO: 15, GCGGSGGGGSGGGGS, which shares 14 or 15 identical residues, i.e., “at least about 90% homologous”, to GCGASGGGGSGGGGS of SEQ ID NO: 3 of the instant application.
In regards to claims 9-11, Dalmas discloses that “the HLA peptide comprises a Y84A or Y84C mutation” (see Dalmas [0035]), therefore teaching that the HLA-B*35 alpha chain comprises one or more amino acid substitutions compared to a ‘wild-type’ HLA-B*35 alpha chain of claim 9 and the Y84A mutation of claim 10. Dalmas disclosed HLA-B35:01 sequence (SED ID NO: 70) has serine at residue 116, while Dalmas’s disclosed HLA-B35:03 sequences (SEQ ID NO: 88) has phenylalanine at the corresponding residue, both sequences otherwise are identical at that region. Thus, Dalmas discloses HLA-B*35 alpha chain comprises [S116F] mutation (see Dalmas [0037], [0045]).
In regards to claim 12, Dalmas discloses “the MHC class I heavy chain sequence of a comPACT comprises a tyrosine-84 to alanine substitution” (see Dalmas [0113]), and further teaches that “the
MHC alleles may also be modified or mutated (e.g., Y84A or Y84C) to improve folding or increase binding of the antigenic peptide with the MHC protein” (see Dalmas [0190]). Further Dalmas discloses the S116F mutation between its own disclosed HLA-B35:01 sequence and HLA-B35:03 sequences as outlined above in the rejection of claim 11.
It would have been obvious to a person of ordinary skill in that to apply the Y84A modification to the HLA-B35:03 allele disclosed at SEQ ID NO: 88 (which already carries S116F mutation), because Dalmas expressly teaches that “any MHC or HLA allele may be used in the
comPACT described herein” (see Dalmas [0115]), and that “the MHC allele encoded in each comPACT can be easily swapped out for other MHC I or II alleles” (see Dalmas [0112]). Additionally, Dalmas expressly identifies Y84A/Y84C substitutions as a routine technique applied “to improve folding or increasing binding of the antigenic peptide with the MHC protein” (see Dalmas [0190]), a stated benefit that would motivate its application to any disclosed allele, including HLA-B35:03. A person of ordinary skill would have had a reasonable expectation of success, as Dalmas’s own disclosure demonstrates that Y84A positional substitutions are tolerated and functional across the platform generally. This is a combination of known prior art elements according to known methods to yield predictable results. See KSR International Co. v. Teleflex Inc. (KSR), 550 U.S. 398, 82 USPQ2d 1385 (2007).
In regards to claims 13 and 14, Dalmas disclosed sequences SEQ ID NOs: 13 (“linker peptide 3”; GCGGS) and SEQ ID NO: 15 (“Linker L1a peptide”; GCGGSGGGGSGGGGS) each have cysteine as the second amino acids, reading on claim 13. As claim 14 does not list a starting linker for which a substitution would occur a linker possessing a cysteine at the 2nd position is considered the structural match for {G2C} of claim 14.
In regards to claim 15, Dalmas discloses “Linkers can also comprise cysteine residues for
disulfide bonds between the linker sequence and the MHC allele sequence, such that the cysteine residues form a disulfide trap” (see Dalmas [0129]).
Claim 16, depends on claim 15 and requires the disulfide bridge to form at the G2C of the first linker and the HLA-B*35 alpha chain. Dalmas’s Table 1 discloses an exemplary comPACT protein, SEQ ID NO: 201, in which the disclosed linker (SEQ ID NO: 15) is fused directly to a heavy chain sequence that itself carries cysteine, rather than the wild-type tyrosine, at the correspond position, i.e., a worked disclosed embodiment of the claimed linker to heavy-chain disulfide trap architecture (see Dalmas [0112], [0129], SEQ ID NO: 201). The heavy chain sequence used in that construct is annotated as HLA-A02:01, not HLA-B35.
Dalmas separately and expressly discloses that “full sequences for each of the 66 HLA-I alleles in the repertoire were obtained from the IMGT database and modified to include the Y84C mutation” (see Dalmas [0229]), a repertoire that expressly contains HLA-B35:01 and HLA-B35:03 (see Dalmas [0011], [0030], [0037], [0045], SEQ ID NOs: 140, 158). Directed comparison of these disclosed HLA-B*35 sequences confirms cysteine, not tyrosine, at the position corresponding to residue 84 (see Dalmas SEQ ID NOs: 140, 158).
It would have been obvious to a person having ordinary skill in the art to substitute the disclosed Y84C modified HLA-B35:01 or HLA-B35:03 sequence for the exemplary HLA-A02:01 sequence in the linker plus heavy chain disulfide trap construct of SEQ ID NO: 201, because Dalmas expressly teaches “the MHC allele encoded in each comPACT can be easily swapped out for other MHC I or II alleles” (see Dalmas [0112]) and the substituted component a Y84C modified HLA-B35 sequence is itself already disclosed in the same reference (as outlined above). Further Dalmas’s worked example demonstrates that the claimed linker cysteine heavy-chain cysteine disulfide trap architecture is functional. This amounts to nothing more than substitution of one disclosed known element for another disclosed known, and interchangeable element to obtain a predictable result, with a reasonable expectation of success established by Dalmas’s own disclosure. See KSR 550 U.S. 398, 82 USPQ2d 1385 (2007).
In regards to claim 17, Dalmas discloses a first linker having the sequence shown in SEQ ID NO: 17, GGGGSGGGGSGGGGS, which shares 14 of the 15 identical residues, i.e., “at least about 90% homologous”, to GGGASGGGGSGGGGS of SEQ ID NO: 4 of the instant application.
In regards to claim 19, Dalmas discloses “a comPACT can comprise a third flexible linker” (see Dalmas [0127]).
In regards to claim 20, Dalmas discloses that the first universal target sequence further comprises a signal sequence, i.e., a leader peptide, with example sequences shown in Table 3. (see Dalmas [0018], Table 3, SEQ ID NOs: 1-2, 23-28).
In regards to claim 21, Dalmas expressly states that its disclosed leader peptides are “secretion signal sequences” that “direct translated proteins in mammalian cells through the secretory pathway” (see Dalmas [0130]).
In regards to claim 26, Dalmas discloses that “the antigenic peptide is 7-15 amino
acids, 7-10, 8-9, 7, 8, 9, 10, 11, 12, 13, 14, or 15 amino acids in length” (see Dalmas [0034], [0150]), which falls entirely within the claimed range of about 8 to about 20 amino acids.
Claims 1-3, 5, 7, 9-17, 19-22, and 25-26 are rejected under 35 U.S.C. 103 as being unpatentable over Dalmas. (US 2020/0062819 A1, published Feb. 27, 2020) as applied to claim 1-3, 5, 7, 9-17, 19-21, and 26 above, and further in view of Ring et al. (US 2018/0037898 A1, and Boder et al. (“Yeast surface display for screening combinatorial polypeptide libraries”, Nature Biotechnology, 1997 June, 1, 15 ( 6 ) : 553-557).
In regards to claim 22, Dalmas teaches all of the limitations of claim 21 for which claim 22 depends. Dalmas further discloses that the host cell may be a yeast cell (see Dalmas [0155]), but does not discloses a yeast-specific leader sequence such as the alternatives listed in claim 22. Ring discloses PHO5 and SUC2 native yeast secretory signal sequences (SEQ ID NOs: 14 and 15, respectively) that contain 100% of the sequence of PHO5 and SUC2 (SEQ ID NOs: 18 and 19, respectively) of the instant application and further discloses that signal polypeptides may be used across yeast species (see Ring [0037]). It would have been obvious to a person of ordinary skill to select Ring’s discloses PHO5 or SUC signal sequences for use as the leader peptide in Dalmas’s comPACT construct when expressed in the yeast host cells Dalmas itself contemplates, with a reasonable expectation of success.
In regards to claim 25, Dalmas discloses the SCT polypeptide of claim 19 including tag sequences (e.g., HIS6, Flag, HA, Myc; see Dalmas [0019]), and a third linker sequence (see Dalmas [0023], [0127]). Dalmas does not teach a tether peptide, nor that the peptide is Aga2. While Dalmas discloses comPACT polypeptides isolation and capture, they are not disclosed as genetically fused to a cell-surface anchor protein for cell-surface display (see Dalmas [0046]).
Boder teaches a tether peptide that is Aga2. Boder discloses a yeast cell-surface display construct in which a protein of interest is genetically fused to the C-terminal end of the Aga2p mating adhesion receptor of S. cerevisiae, thereby anchoring the fused protein to the yeast cell wall via the Aga complex.
It would have been prima facie obvious to one of ordinary skill in the art at the time of filing to modify Dalmas’s comPACT polypeptide to include Boder’s Aga2 tether peptide, in place of or in addition to Dalmas’s discloses particle-based capture with a reasonable expectation of success. Dalmas itself contemplates expression of its comPACT constructs in yeast host cells (see Dalmas [0155]) and Boder’s Aga2 fusion approach was a well-established technique for achieving cell surface display in yeast. This is the same underlying goal Dalmas’s particle-capture approach serves for T-cell isolation and antigen specific screening (see Dalmas [0111], [0181]). Substituting Boder’s known cell-surface tethering mechanism for Dalmas’s own particle capture mechanism, both being known means of isolating and identifying proteins of interest bound entities amounts to combination of known elements according to know methods to yield predictable results. See KSR 550 U.S. 398, 82 USPQ2d 1385 (2007).
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.
Claim 1 is provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 17/800,933 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other.
Instant claim 1 recites a single chain trimer (SCT) polypeptide comprising or consisting essentially of a target peptide, a first linker, at least a portion of a beta-2 microglobulin domain, second linker, and at least a portion of an HLA-B*35 alpha chain, or a pharmaceutically acceptable derivative thereof. Whereas claim of ‘933 recites the same SCT polypeptide architecture, further limited to require an NY-EPO-1 target peptide, a first linker consisting of the peptide sequence set for in SEQ ID NO: 1 and a Y84C substitution in the MHC I alpha chain. The differences between these are differences a person of ordinary skill in the art would find obvious in view of the shared specification, which the two applications hold in common, apart from immaterial differences at the beginning referencing sequence listings.
Narrowing to HLA-B*35- the shared specification discloses that the MHC I alpha chain of the claimed SCT architecture may be drawn from any of several class I HLA alleles and expressly identifies HLA-B*35 as one such allele. Selection of a single, expressly named species from a genus already disclosed and enabled in the shared specification (MHC I generally) is an obvious variant of the copending claims “function portion of a major histocompatibility complex (MHC) I alpha chain” limitation. See In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970). MPEP 804.
The shared specification discloses NY-ESO-1 as one of several interchangeable exemplified target peptides rather than as peptides, rather than as a peptide uniquely required for the claimed architecture to function. The shared specification likewise discloses the SEQ ID NO: 1 linker sequences as one of several disclosed linker embodiments (including SED ID NOs: 2-4), each achieving the same disclosed purpose as a peptide linker. Claiming the SCT architecture generically, without limitation to the specific exemplified peptide or linker species is accordingly no more than an obvious generalization of what the shared specification discloses as interchangeable embodiments serving a common purpose.
Because the instant claim differs from the copending claim only in ways that the specification itself discloses as either an enabled genus member (HLA-B*35) or an interchangeable, non-critical species selection (NY-ESO-1, SEQ ID NO: 1), the claims are not patentably distinct.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
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/MATTHEW HAROLD RAYMONDA/Examiner, Art Unit 1684
/AARON A PRIEST/Primary Examiner, Art Unit 1681
Prosecution Insights