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 .
Location of Application
The subject application is now located in Workgroup 1680, Art Unit 1682, and has been docketed to Primary Examiner Bradley L. Sisson.
Drawings
New corrected drawings in compliance with 37 CFR 1.121(d) are required in this application because:
In Figure(s) 1-4 the reference characters, sheet numbers, and view numbers are not all oriented in the same direction so as to avoid having to rotate the sheet. See 37 CFR 1.84(p)(1).
The numbering of the sheets of drawings bearing FIG(s). 1-4 is not in compliance with all aspects of 37 CFR 1.84(t).
Applicant is advised to employ the services of a competent patent draftsperson outside the Office, as the U.S. Patent and Trademark Office no longer prepares new drawings. The corrected drawings are required in reply to the Office action to avoid abandonment of the application. The requirement for corrected drawings will not be held in abeyance.
INFORMATION ON HOW TO EFFECT DRAWING CHANGES
Replacement Drawing Sheets
Drawing changes must be made by presenting replacement sheets which incorporate the desired changes and which comply with 37 CFR 1.84. An explanation of the changes made must be presented either in the drawing amendments section, or remarks, section of the amendment paper. 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). A replacement sheet must 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 the amended drawing(s) must not be labeled as “amended.” If the changes to the drawing figure(s) are not accepted by the examiner, applicant will be notified of any required corrective action in the next Office action. No further drawing submission will be required, unless applicant is notified.
Identifying indicia, if provided, should include the title of the invention, inventor’s name, and application number, or docket number (if any) if an application number has not been assigned to the application. If this information is provided, it must be placed on the front of each sheet and within the top margin.
Annotated Drawing Sheets
A marked-up copy of any amended drawing figure, including annotations indicating the changes made, are required by the examiner. The annotated drawing sheet(s) must be clearly labeled as “Annotated Sheet” and must be presented in the amendment or remarks section that explains the change(s) to the drawings.
Timing of Corrections
Applicant is required to submit acceptable corrected drawings within the time period set in the Office action. See 37 CFR 1.85(a). Failure to take corrective action within the set period will result in ABANDONMENT of the application.
If corrected drawings are required in a Notice of Allowability (PTOL-37), the new drawings MUST be filed within the THREE MONTH shortened statutory period set for reply in the “Notice of Allowability.” Extensions of time may NOT be obtained under the provisions of 37 CFR 1.136 for filing the corrected drawings after the mailing of a Notice of Allowability.
Claim Interpretation
Attention is directed to MPEP 904.01 [R-08.2012].
The breadth of the claims in the application should always be carefully noted; that is, the examiner should be fully aware of what the claims do not call for, as well as what they do require. During patent examination, the claims are given the broadest reasonable interpretation consistent with the specification. See In re Morris, 127 F.3d 1048, 44 USPQ2d 1023 (Fed. Cir. 1997). See MPEP § 2111 - § 2116.01 for case law pertinent to claim analysis.
It is noted with particularity that narrowing limitations found in the specification cannot be inferred in the claims where the elements not set forth in the claims are linchpin of patentability. In re Philips Industries v. State Stove & Mfg. Co, Inc., 186 USPQ 458 (CA6 1975). While the claims are to be interpreted in light of the specification, it does not follow that limitations from the specification may be read into the claims. On the contrary, claims must be interpreted as broadly as their terms reasonably allow. See Ex parte Oetiker, 23 USPQ2d 1641 (BPAI, 1992). In added support of this position, attention is directed to MPEP 2111 [R-11.2013], where, citing In re Prater, 415 F.2d 1393, 1404-05, 162 USPQ 541, 550-51 (CCPA 1969), is stated:
The court explained that “reading a claim in light of the specification, to thereby interpret limitations explicitly recited in the claim, is a quite different thing from ‘reading limitations of the specification into a claim,’ to thereby narrow the scope of the claim by implicitly adding disclosed limitations which have no express basis in the claim.” The court found that applicant was advocating the latter, i.e., the impermissible importation of subject matter from the specification into the claim.
Additionally, attention is directed to MPEP 2111.01 [R-01.2024], wherein is stated:
II. IT IS IMPROPER TO IMPORT CLAIM LIMITATIONS FROM THE SPECIFICATION
“Though understanding the claim language may be aided by explanations contained in the written description, it is important not to import into a claim limitations that are not part of the claim. For example, a particular embodiment appearing in the written description may not be read into a claim when the claim language is broader than the embodiment.” Superguide Corp. v. DirecTV Enterprises, Inc., 358 F.3d 870, 875, 69 USPQ2d 1865, 1868 (Fed. Cir. 2004).
Attention is also directed to MPEP 2111.02 II [R-07.2022]. As stated herein:
II. PREAMBLE STATEMENTS RECITING PURPOSE OR INTENDED USE
PNG
media_image1.png
18
19
media_image1.png
Greyscale
The claim preamble must be read in the context of the entire claim. The determination of whether preamble recitations are structural limitations or mere statements of purpose or use "can be resolved only on review of the entirety of the [record] to gain an understanding of what the inventors actually invented and intended to encompass by the claim" as drafted without importing "'extraneous' limitations from the specification." Corning Glass Works, 868 F.2d at 1257, 9 USPQ2d at 1966. If the body of a claim fully and intrinsically sets forth all of the limitations of the claimed invention, and the preamble merely states, for example, the purpose or intended use of the invention, rather than any distinct definition of any of the claimed invention’s limitations, then the preamble is not considered a limitation and is of no significance to claim construction. Shoes by Firebug LLC v. Stride Rite Children’s Grp., LLC, 962 F.3d 1362, 2020 USPQ2d 10701 (Fed. Cir. 2020) (The court found that the preamble in one patent’s claim is limiting but is not in a related patent); Pitney Bowes, Inc. v. Hewlett-Packard Co., 182 F.3d 1298, 1305, 51 USPQ2d 1161, 1165 (Fed. Cir. 1999). See also Rowe v. Dror, 112 F.3d 473, 478, 42 USPQ2d 1550, 1553 (Fed. Cir. 1997) ("where a patentee defines a structurally complete invention in the claim body and uses the preamble only to state a purpose or intended use for the invention, the preamble is not a claim limitation")… (Emphasis added)
Attention is directed to MPEP 2111 [R-10.2019]. As stated therein:
During patent examination, the pending claims must be "given their broadest reasonable interpretation consistent with the specification." The Federal Circuit’s en banc decision in Phillips v. AWH Corp., 415 F.3d 1303, 1316, 75 USPQ2d 1321, 1329 (Fed. Cir. 2005) expressly recognized that the USPTO employs the "broadest reasonable interpretation" standard:
The Patent and Trademark Office ("PTO") determines the scope of claims in patent applications not solely on the basis of the claim language, but upon giving claims their broadest reasonable construction "in light of the specification as it would be interpreted by one of ordinary skill in the art." In re Am. Acad. of Sci. Tech. Ctr., 367 F.3d 1359, 1364[, 70 USPQ2d 1827, 1830] (Fed. Cir. 2004). Indeed, the rules of the PTO require that application claims must "conform to the invention as set forth in the remainder of the specification and the terms and phrases used in the claims must find clear support or antecedent basis in the description so that the meaning of the terms in the claims may be ascertainable by reference to the description." 37 CFR 1.75(d)(1). (Emphasis added).
Attention is directed to MPEP 2173.04 [R-10.2019]. As stated therein:
Breadth of a claim is not to be equated with indefiniteness. In re Miller, 441 F.2d 689, 169 USPQ 597 (CCPA 1971); In re Gardner, 427 F.2d 786, 788, 166 USPQ 138, 140 (CCPA 1970) ("Breadth is not indefiniteness."). A broad claim is not indefinite merely because it encompasses a wide scope of subject matter provided the scope is clearly defined. But a claim is indefinite when the boundaries of the protected subject matter are not clearly delineated and the scope is unclear. For example, a genus claim that covers multiple species is broad, but is not indefinite because of its breadth, which is otherwise clear. But a genus claim that could be interpreted in such a way that it is not clear which species are covered would be indefinite (e.g., because there is more than one reasonable interpretation of what species are included in the claim). (Emphasis added)
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.
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.
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, 5, 6, 9, 11, 12, 21, 23, 25, and 106 are rejected under 35 U.S.C. 103 as being unpatentable over US 2022/0113318 A1 (McDonnell et al.), and US 2012/0115244 A1 (Adamezyk et al.).
McDonnell et al., at paragraph [0384], teach:
[0384] Referring to FIG. 12A, in an instance where cells are labelled with labeling agents, capture sequence 1223 may be complementary to a capture handle sequence of a reporter oligonucleotide. Cells may be contacted with one or more reporter oligonucleotide 1220 conjugated labelling agents 1210 (e.g., polypeptide, antibody, or others described elsewhere herein). In some cases, the cells may be further processed prior to barcoding… In some instances, the partition comprises at most a single cell bound to labelling agent 1210. In some instances, reporter oligonucleotide 1220 conjugated to labelling agent 1210 (e.g., polypeptide, an antibody, pMHC molecule such as an MHC multimer, etc.) comprises a first adapter sequence 1211 (e.g., a primer sequence), a barcode sequence 1212 that identifies the labelling agent 1210 (e.g., the polypeptide, antibody, or peptide of a pMHC molecule or complex), and a capture handle sequence 1213. Capture handle sequence 1213 may be configured to hybridize to a complementary sequence, such as a capture sequence 1223 present on a nucleic acid barcode molecule 1290. In some instances, oligonucleotide 1220 comprises one or more additional functional sequences, such as those described elsewhere herein.
McDonnell et al., at paragraph [0140], teach:
[0140] In some embodiments, a cell population is engineered to express a target binding partner (e.g., a target protein or peptide of interest, a target antigen, or a target epitope). (Emphasis added)
McDonnell et al., at paragraph [0178], teach:
[0178] In some embodiments, the binding molecule (e.g., antibody or antigen-binding fragment thereof) is covalently coupled to the first nucleic acid barcode sequence, e.g., via an isopeptide reaction such as a sortase-catalyzed ligation. (Emphasis added)
McDonnell et al., at paragraph [0188], teach:
[0188] In some embodiments, a reporter barcode labeled binding molecule (e.g., antibody or antigen-binding fragment thereof) is covalently coupled to a binding partner (e.g., an antigen or epitope) via a spontaneous isopeptide reaction between peptide tags. (Emphasis added)
McDonnell et al., at paragraph [0119], teach:
In some embodiments, the antibody can be a monoclonal antibody (mAb), a recombinant bispecific monoclonal antibody such as a Bi-specific T-cell engager (BiTE), a simultaneous multiple interaction T-cell engaging (SMITE) bispecific antibody, or a bi-, tri-, or tetra-valent antibody.
The aspect of using antibodies that interact with T cells speaks to T cells being in the
McDonnell et al., at paragraph [0136], teach:
[0136] In some embodiments, the cell is a primary cell or a cell line cell. In some embodiments, the cell is a blood cell. In some embodiments, the blood cell is an immune cell. In some embodiments, the immune cell is a lymphocyte. In some embodiments, the immune cell is a T cell, B cell, natural killer (NK) cell, dendritic cell (DC), NKT cell, mast cell, monocyte, macrophage, basophil, eosinophil, or neutrophil. In some embodiments, the immune cell is an adaptive immune cell such as a T cell and B cell.
The above showing is deemed to fairly suggest limitations of claim 21.
McDonnell et al., at paragraph [0200], teach:
In some embodiments, cells bound by binding molecules can be detected by a fluorochrome-labeled antibody recognizing the cell-bound binding molecules, and subsequently analyzed using FACS. In some embodiments, cells bound by binding molecules can be detected by an antibody (e.g., a fluorochrome-labeled antibody, a magnetic bead-labeled antibody, a microbubble-labeled antibody, or a combination thereof) recognizing a tag or target of the cell-bound antibodies, and subsequently analyzed. (Emphasis added)
McDonell et al., at paragraph [0382], teaches:
In some instances, the MHC molecule is coupled to a support 1033. In some instances, support 1033 may be a polypeptide, such as streptavidin, or a polysaccharide, such as dextran. (Emphasis added)
McDonnell’s “support” is deemed to fairly support the limitation of applicant’s “scaffold” (claim 106).
McDonnell et al., at paragraph [0239], teach that the sample can be a “biological sample”. As disclosed therein:
[0239] A sample may be a biological sample, such as a cell sample (e.g., as described herein). A sample may include one or more analyte carriers, such as one or more cells and/or cellular constituents, such as one or more cell nuclei. For example, a sample may comprise a plurality of cells and/or cellular constituents. Components (e.g., cells or cellular constituents, such as cell nuclei) of a sample may be of a single type or a plurality of different types. For example, cells of a sample may include one or more different types of blood cells. (Emphasis added)
McDonnell et al., at paragraphs [0099] and {0100], teach:
[0099] In some embodiments, the binding candidate identification and the analysis of one or more binding attributes are achieved in the same assay or assays, e.g., assays using the same readout such as a sequencing readout. In some embodiments, the binding candidate identification and the analysis of one or more binding attributes do not require different assay formats, such as identification using a readout based on nucleic acid hybridization or sequencing, and analysis using an immunoassay, such as a fluorescent sandwich immunoassay or ELISA, or using SPR. In some embodiments, the methods disclosed herein do not comprise performing an immunoassay, such as a fluorescent sandwich immunoassay or ELISA, or performing SPR. In some embodiments, the methods disclosed herein enable not only identification but also validation that an antibody does indeed bind an antigen or epitope, e.g., via multiple measurement modalities, as well as an assessment of one or more other binding attributes (such as binding affinity) of an antibody to an antigen or epitope.
[0100] In some embodiments, a label is attached to a binding molecule (e.g., a monoclonal antibody) of interest in order to assess one or more binding attributes (e.g., binding specificity and/or affinity) of the binding molecule to one or more binding partners. In some embodiments, the label comprises a reporter oligonucleotide comprising a reporter barcode sequence unique to the binding molecule. The attachment can be done directly or indirectly, e.g., via multiple chemical methods varying in their site specificity. In some embodiments, the binding molecule (e.g., a monoclonal antibody) is engineered or fused to one or more moieties to enable the labeling. In the case of natively IgM or IgD or IgA antibody candidates, for example, the antibody candidate may be converted to an IgG format. In some embodiments, the labeling comprises attaching one or more oligonucleotide-conjugated fluorophores, directly or indirectly, to a binding molecule (e.g., a monoclonal antibody). In some embodiments, the labeling comprises conjugating an oligonucleotide (e.g., a reporter oligonucleotide comprising a reporter barcode sequence) or an oligonucleotide-conjugated fluorophore to biotin and then attaching the biotin-conjugated reporter to the binding molecule of interest via a biotinylation reaction. In some embodiments, a biotin-conjugated reporter oligonucleotide or reporter oligonucleotide-conjugated fluorophore can be attached to a streptavidin-tagged binding molecule.
Adamczyk et al., in claim 13, teach:
13. An anti-neopterin antibody, which is labeled with an acridinium compound and which is optionally part of a conjugate/complex comprising anti-neopterin antibody and a carrier scaffold, or an anti-neopterin antibody, which is part of a conjugate/complex comprising anti-neopterin antibody and a carrier scaffold and which is optionally detectably labeled, wherein the carrier scaffold is selected from the group consisting of a protein, a polysaccharide, a polynucleotide, dextran, streptavidin, and a dendrimer, and wherein the ratio of antibody:carrier scaffold is greater than about 4. (Emphasis added)
In view of the above presentation, it would have been quite obvious to one of ordinary skill in the art to have designed and arranged a biological sample with a detection complex whereby any number of antigens can be detected in a simultaneous manner through the use of probes that hybridize to the reporter oligonucleotide.
Claim Rejections - 35 USC § 102
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 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.
Claim(s) 1 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Bentzen et al. (2016) (Bentzen et al., Large-scale detection of antigen-specific T cells using peptide-MHC-I multimers labeled with DNA barcodes, Nat Biotechnol., 2016 Oct;34(10):1037-1045. doi: 10.1038/nbt.3662. Epub 2016 Aug 29).
Bentzen et al. (2016) teaches:
“Identification of the peptides recognized by individual T cells is important for understanding and treating immune-related diseases. Current cytometry-based approaches are limited to the simultaneous screening of 10–100 distinct T-cell specificities in one sample. Here we use peptide–major histocompatibility complex (MHC) multimers labeled with individual DNA barcodes to screen >1,000 peptide specificities in a single sample and detect low-frequency CD8 T cells specific for virus- or cancer restricted antigens. When analyzing T-cell recognition of shared melanoma antigens before and after adoptive cell therapy in melanoma patients, we observe a greater number of melanoma-specific T-cell populations compared with cytometry-based approaches. Furthermore, we detect neoepitope-specific T cells in tumor-infiltrating lymphocytes and peripheral blood from patients with non-small cell lung cancer. Barcode-labeled pMHC multimers enable the combination of functional T-cell analysis with large-scale epitope recognition profiling for the characterization of T-cell recognition in various diseases, including in small clinical samples” (See Abstract).
Bentzen et al. (2016) teaches:
“Large-scale detection of T-cell specificities: We generated DNA barcode-labeled MHC-I multimer reagents on a dextran backbone that carried the common fluorescent label phycoerythrin (PE) (Fig. 1a, b). The DNA barcodes were designed from a set of 240,000 unique 25-mer oligonucleotides with sequences described that have similar amplification properties while maintaining maximum diversity of their identification motifs To provide a system adaptable to large library screenings, we applied a combinatorial design of DNA barcodes (Fig. 1c and Supplementary Tables 1–3). Through this design we could generate at least 5.8 × 106 different barcodes. To determine the number of unique DNA sequences originating from each pMHC-associated barcode (clonally reduced barcode reads), we incorporated unique molecular identifiers (UMIs) next to the barcode sequence (Fig. 1c), allowing the clonal reduction of sequences from the amplified product. MHC multimers were generated by addition of average two biotinylated DNA barcodes and 12 pMHC complexes per dextramer backbone. pMHC complexes were generated through UV-induced conditional ligand exchange to synthetic peptides of predicted relevance using methods described previously (See bridging paragraph pages 1037-1038).
PNG
media_image2.png
240
628
media_image2.png
Greyscale
PNG
media_image3.png
236
628
media_image3.png
Greyscale
PNG
media_image4.png
392
624
media_image4.png
Greyscale
Figure 1 Preparation and use of DNA barcode-labeled MHC multimers. (a) Schematic overview showing the strategy for using DNA barcode labeled MHC multimers for detection of antigen-specific T cells in complex cellular suspensions. Biotinylated DNA barcodes and pMHC molecules are attached to a PE-labeled dextran backbone carrying streptavidin; B, biotin. (b) Each MHC multimer is assembled with a given DNA barcode, forming a tag for the corresponding specificity (1 to >1,000). MHC multimer-binding T cells are sorted based on the PE label. DNA barcodes are amplified and sequenced, and the relative number s of DNA barcode reads is used to determine the composition of antigen-responsive T cells in the sample. (c) Schematic overview of the DNA barcode design. B, biotin; FR, forward region; UMI, unique molecular identifier; coding region, 25-mer barcode sequence assigning pMHC specificity; AR, annealing region; CAR, complementary annealing region; and RR, reverse region. The biotinylated oligo Ax comprises a 16-nucleotide region partially complementary to oligo By. Oligos Ax and By both contain an individual 25-mer oligonucleotide barcode sequence (determined by the ‘x or y’) and six randomly incorporated nucleotides, providing a UMI for each synthesized oligo. Oligo A contains a forward primer region (FR), and oligo B contains a reverse primer region (RR) (the oligonucleotide sequences are listed in Supplementary Tables 1 and 2). Following annealing of Oligo Ax and Oligo By and before the attachment to the multimerization backbone, the oligos are elongated to obtain their double-stranded form. After the isolation of MHC multimer-binding T cells, the DNA barcodes are amplified by PCR. The forward primer is flanked by a 5? sample identifier sequence (sampleID), and both the forward and reverse primers encode a 5? sequencing adaptor sequence (IonTorrent, A-Key and P1-key, respectively).
Bentzen et al. (2016) further teaches:
“Feasibility and detection limit for large-scale T-cell analysis: Using DNA barcodes to identify pMHC–TCR interactions enables, in principle, distinction of >1010 different pMHC complexes in a single sample. However, several factors such as efficient and specific pMHC–TCR interactions, protein concentration and production, and peptide synthesis capabilities limit library sizes. To prove the feasibility of staining antigen-specific T cells in mixtures of >1,000 different pMHC multimers, we compared DNA-barcoded MHC multimers and combinatorial fluorescently labeled MHC multimers to detect T-cell populations responsive to virus or cancer- derived peptides5,6. We tested specific T-cell interactions using PE-labeled MHC multimers with and without an attached DNA barcode. The DNA barcode did not interfere with pMHC multimer binding, and MHC multimers with and without DNA barcodes showed identical staining capacities when staining healthy donor peripheral blood mononuclear cells (PBMCs) or tumor-infiltrating lymphocytes (TILs) from a melanoma patient (detection with HLA-A*0201 cytomegalovirus (CMV) pp65 NLV multimers or HLAA* 0201 hTERT p988 (YLQVNSLQTV) multimers, respectively) (Supplementary Fig. 1a,b). Moreover, specific DNA barcodes could be amplified after the isolation of HLA-B*0702 CMV pp65TPR-multimer- binding T cells from healthy donor PBMCs, either following single MHC multimer staining or after mixture with 999 irrelevant MHC multimers. DNA barcodes associated with irrelevant MHC multimers were not identified (Supplementary Fig. 1c,d) (See right column, page 1038).
Conclusion
The prior art made of record and not relied upon is considered pertinent to applicant's disclosure.
US 2018/0180601 A1 (Pedersen et al.), in paragraphs [0053] and [0392] teaches:
[0053] Antigenic peptide: Used interchangeably with binding peptide. Any peptide molecule that is bound or able to bind into the binding groove of either MHC class 1 or MHC class 2 molecules.
[0392] Different types of MHC's may form part of the multimer. Thus, in an embodiment the MHC is selected from the group consisting of class I MHC, a class II MHC, a CD1, or a MHC-like molecule. For MHC class I the presenting peptide is a 9-11 mer peptide; for MHC class II, the presenting peptide is 12-18 mer peptides.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Bradley L. Sisson whose telephone number is (571)272-0751. The examiner can normally be reached Monday to Thursday, from 6:30 AM to 5 PM..
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Wu-Cheng Shen can be reached at 571-272-3157. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/Bradley L. Sisson/Primary Examiner, Art Unit 1682
Prosecution Insights