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 .
2. A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 07/25/2025 has been entered.
3. Claims 12-14, 18 and 20 are pending.
4. Claims 14 and 20 stand withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected Group, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 11/22/2024.
5. Claims 12-13 and 18 are currently under examination as they read on a kit or composition comprising SEQ ID NO:455. The examiner has extended the search to SEQ ID NO:455 after Applicant canceled the elected variant of SEQ ID NO:959.
6. 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.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
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 of carrying out his invention.
7. Claim 13 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the enablement requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention. The specification disclosure does not enable one skilled in the art to practice the invention without an undue amount of experimentation.
Factors to be considered in determining whether undue experimentation is required to practice the claimed invention are summarized 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, the lack of sufficient working examples, the unpredictability in the art and the amount of experimentation required to enable one of skill in the art to practice the claimed invention.
The specification is not enabled for the use of any of the “hyposensitization polypeptides” recited in claim 13 in a treatment that results in hyposensitization.
The genus of recited sequences cannot be used in hyposensitization therapy. The claims recite “hyposensitization polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 697, 702, 703, 917, 921, 923, 928, 929, 931, 933, 934, 442-453,455-479 and 481-484.” This group of “hyposensitization polypeptides encompasses peptides which ranges from 6 amino acids to 42 amino acids in length. There are many peptides with X residues within these peptides. For example, SEQ ID NOs: 934 is an 8 amino acid long peptide with only 4 amino acids specified. The art of Prickett et al (PTO-982; Reference U) teaches that “identifying CD4+ T cell epitopes within allergens is mandatory for the design of T cell targeted therapeutics.” and “To identify all potential T cell epitopes, allergen-specific T cell lines and clones generated from a large patient cohort are screened for reactivity against overlapping synthetic peptides spanning the entire sequence of the allergen molecule, each usually 15–20 amino acids in length with overlaps ranging from five amino acids upwards. Following identification of T cell reactive peptides, precise core epitope sequences are mapped utilizing peptide sets truncated from the N- and C-termini, for example as demonstrated in early studies for a rye grass pollen allergen Lol p 5 T cell epitope. Minimal core CD4+ T cell epitopes are typically eight or nine residues long, but lengths for optimal T cell stimulation may be longer and vary between subjects. This likely reflects varied requirements for flanking residues in stabilizing different HLA-peptide-TCR complexes and increasing persistence of the peptide at the APC surface. Peptides selected for immunotherapy tend to range from 12 to 20 residues, consistent with naturally processed peptides eluted from HLA class II molecules.” (In particular, last paragraph of page 1016 to end of first paragraph of page 1018, whole document).
As such, peptides for use in a hyposensitization must be at a minimum 8-9 amino acids in length, no longer than 20 amino acids in length and have been confirmed to comprise a CD4+ T cell epitope. The specification is not enabled for using any hyposensitization peptides which do not meet these standards. As such all peptides comprising undefined “X” amino acid residues, peptides of less than 8 amino acids in length and more than 20 amino acids in length are not enabled for use in tolerization. If they meet the size requirements, the peptides must be demonstrated to have a CD4+ T cell epitopes.
The specification is not enabled for the use of polypeptides comprising these “hyposensitization polypeptides” and which further comprise an unlimited number of additional amino acids added onto the N- and/or C-terminus of the recited sequences.
Furthermore, the peptides used in an immunotherapy must be CD4+ T-cell epitopes and from the previous claim recitations it would appear that the peptides are supposed to be antibody binding epitopes. Antibody binding epitopes are necessary for the method of detecting antibodies, but would not be useful in a hyposensitization method. Peptides of more than 20 amino acids have an increased chance of having antibody binding epitopes.
In view of the absence of a specific and detailed description in Applicant's specification of how to effectively use the genus of hyposensitization polypeptides claimed, absence of working examples providing evidence which is reasonably predictive that the genus of claimed agents are effective for in vivo use for hyposensitization of disease, and the lack of predictability in the art at the time the invention was made, an undue amount of experimentation would be required to practice the claimed hyposensitization compositions with a reasonable expectation of success.
Substantiating evidence may be in the form of animal tests, which constitute recognizedscreening procedures with clear relevance to efficacy in humans. See Ex parte Krepelka, 231USPQ 746 (Board of Patent Appeals and Interferences 1986) and cases cited therein. Ex parteMaas, 9 USPQ2d 1746.
Reasonable correlation must exist between the scope of the claims and scope of the enablement set forth. In view on the quantity of experimentation necessary the limited working examples, the nature of the invention, the state of the prior art, the unpredictability of the art and the breadth of the claims, it would take undue trials and errors to practice the claimed invention.
8. Claim 13 is 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
Applicant is not in possession of:
a “hyposensitization polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 697, 702, 703, 917, 921, 923, 928, 929, 931, 933, 934, 442-453,455-479 and 481-484.”
The specification has not adequately described the genus of recited sequences that be used in hyposensitization therapy. The claim recites administering a “hyposensitization polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 697, 702, 703, 917, 921, 923, 928, 929, 931, 933, 934, 442-453,455-479 and 481-484.” This group of “hyposensitization polypeptides encompasses peptides which ranges from 6 amino acids to 42 amino acids in length. There are many peptides with X residues within these peptides. For example, SEQ ID NOs: 934 is an 8 amino acid long peptide with only 4 amino acids specified. The art of Prickett et al (PTO-982; Reference U) teaches that “identifying CD4+ T cell epitopes within allergens is mandatory for the design of T cell targeted therapeutics.” and “To identify all potential T cell epitopes, allergen-specific T cell lines and clones generated from a large patient cohort are screened for reactivity against overlapping synthetic peptides spanning the entire sequence of the allergen molecule, each usually 15–20 amino acids in length with overlaps ranging from five amino acids upwards. Following identification of T cell reactive peptides, precise core epitope sequences are mapped utilizing peptide sets truncated from the N- and C-termini, for example as demonstrated in early studies for a rye grass pollen allergen Lol p 5 T cell epitope. Minimal core CD4+ T cell epitopes are typically eight or nine residues long, but lengths for optimal T cell stimulation may be longer and vary between subjects. This likely reflects varied requirements for flanking residues in stabilizing different HLA-peptide-TCR complexes and increasing persistence of the peptide at the APC surface. Peptides selected for immunotherapy tend to range from 12 to 20 residues, consistent with naturally processed peptides eluted from HLA class II molecules.” (In particular, last paragraph of page 1016 to end of first paragraph of page 1018, whole document).
As such, peptides for use in a hyposensitization must be at a minimum 8-9 amino acids in length, no longer than 20 amino acids in length and have been confirmed to comprise a CD4+ T cell epitope. The specification has not described any hyposensitization peptides which do not meet these standards. As such all peptides comprising undefined “X” amino acid residues, peptides of less than 8 amino acids in length and more than 20 amino acids in length are adequately described for use in tolerization. If they meet the size requirements, the peptides must be demonstrated to have a CD4+ T cell epitopes.
The specification has not adequately described the use of polypeptides comprising these “hyposensitization polypeptides” and which further comprise an unlimited number of additional amino acids added onto the N- and/or C-terminus of the recited sequences.
Furthermore, the peptides used in an immunotherapy must be CD4+ T-cell epitopes and from the previous claim recitations it would appear that the peptides are supposed to be antibody binding epitopes. Antibody binding epitopes are necessary for the method of detecting antibodies, but would not be useful in a hyposensitization method. Peptides of more than 20 amino acids have an increased chance of having antibody binding epitopes.
Conception cannot be achieved until a representative description of the structural and functional properties of the claimed invention has occurred, regardless of the complexity or simplicity of the method.
The specification has neither demonstrated a structure function relationship nor provided a representative number of species of peptides with the recited hyposensitization function.
The specification must set forth the structural features that allow one of ordinary skill in the art to identify and produce the recited peptides . In the instant case, definition by function does not suffice to define the genus because it is only an indication of what the peptides do, rather than what they are.
The specification does not disclose a correlation between the peptide structure and the function of being able to be used for hyposensitization such that a skilled artisan would have known what peptide variants possess the claimed function. "Possession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features" Ex parte Kubin (83 U.S.P.Q.2d 1410 (BPAI 2007)), at page 16. In this instant case, Applicants have not provided the requisite identifying structural features of the peptides encompassed. "Without a correlation between structure and function, the claim does little more than define the claimed invention by function" supra, at page 17.
The specification does not provide adequate written description of the claimed invention.
The legal standard for sufficiency of a patent's (or a specification's) written description is whether that description "reasonably conveys to the artisan that the inventor had possession at that time of the. . .claimed subject matter", Vas-Cath, Inc. V. Mahurkar, 19 U.S.P.Q.2d 1111
(Fed. Cir. 1991). In the instant case, the specification does not convey to the artisan that the applicant had possession at the time of invention of the claimed invention.
Adequate written description requires more than a mere statement that it is part of the invention and a reference to a potential method of isolating it. In the instant application, the amino acid sequence itself or isolated protein is required. See Fiers v. Revel, 25 USPQ 2d 1601 at 1606 (CAFC 1993) and Amgen Inc. V. Chugai Pharmaceutical Co. Lts., 18 USPQ2d 1016. In view of the aforementioned problems regarding description of the claimed invention, the specification does not provide an adequate written description of the invention claimed herein.
See The Regents of the University of California v. Eli Lilly and Company, 43 USPQ2d 1398,
1404-7 (Fed. Cir. 1997). In University of California v. Eli Lilly and Co., 39 U.S.P.Q.2d 1225
(Fed. Cir. 1995) the inventors claimed a genus of DNA species encoding insulin in different vertebrates or mammals, but had only described a single species of cDNA which encoded rat insulin. The court held that only the nucleic acids species described in the specification (i.e. nucleic acids encoding rat insulin) met the description requirement and that the inventors were not entitled to a claim encompassing a genus of nucleic acids encoding insulin from other vertebrates, mammals or humans, id. at 1240. The Federal Circuit has held that if an inventor is "unable to envision the detailed constitution of a gene so as to distinguish it from other materials.
. .conception has not been achieved until reduction to practice has occurred", Amgen, Inc. v.
Chugai Pharmaceutical Co, Ltd., 18 U.S.P.Q.2d 016 (Fed. Cir. 1991). Attention is also directed to the decision of The Regents of the University of California v. Eli Lilly and Company (CAFC,
July 1997) wherein is stated: "The description requirement of the patent statute requires a description of an invention, not an indication of a result that one might achieve if one made that invention. See In re Wilder, 736 F.2d 1516, 222 USPQ 369, 372-373 (Fed. Cir. 1984) (affirming rejection because the specification does "little more than outlin[e] goals appellants hope the claimed invention achieves and the problems the invention will hopefully ameliorate.").
Accordingly, naming a type of material generally known to exist, in the absence of knowledge as to what that material consists of, is not a description of that material. Thus, as we have previously held, a cDNA is not defined or described by the mere name "cDNA," even if accompanied by the name of the protein that it encodes, but requires a kind of specificity usually achieved by means of the recitation of the sequence of nucleotides that make up the cDNA." See
Fiers, 984 F.2d at 1171, 25 USPQ2d at 1606.
As such, there is insufficient written description of the required kind of structure identifying information about the corresponding makeup of the claimed peptides to demonstrate possession.
9. 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.
10. 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.
11. Claims 12 and 18 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Sahabudin et al. (PTO-892; Reference V) as evidenced by Yang et al. (PTO-892; Reference W) and the attached sequence alignment.
Sahabudin et al. performs SDS-PAGE analysis on a raw extract from Penaeus monodon (black tiger prawn). They probed the SDS-PAGE with sera from patients with histories of prawn allergy and demonstrated positive skin prick tests to raw extracts of black tiger prawn. As shown in Figure 1, immunoblotting of the raw black tiger prawn extracts identified 14 IgE-binding proteins at various molecular weights between 15 and 200 kDa. Four major IgE-binding components at the molecular masses of 36, 42, 49, and 75 kDa were detected in black tiger prawn extracts (In particular, page 29, whole document). The protein at 49 kDa was identified as a major allergen. (In particular, final paragraph on page 31).
Yang et al. is being used an evidentiary reference. Yang teaches the specific IgE binding characteristics of different shrimp proteins of Penaeus monodon (black tiger shrimp) to the sera of eight shrimp-allergic patients from China were studied by SDS-PAGE and nanoliquid chromatography time-of-flight mass spectrometry. According to the PLGS scores (>2000) and the sequence coverage (>40%), eight proteins with sIgE binding activity were identified, including myosin heavy chain tyре 1 (K4Q4N8), hemocyanin (G1AP69 and Q95V28), phosphopyruvate hydratase (O96656), arginine kinase (C7E3T4), tropomyosin (A1KYZ2), sarcoplasmic calcium binding protein (H7CHW2) and glyceraldehyde-3-phosphate dehydrogenase (A0A097BQP2). Among these eight proteins, phosphopyruvate hydratase was a prevalent IgE binding protein among these Chinese patients with binding observed in 100% of sera. phosphopyruvate hydratase (O96656) was located in a 47 kDa band on the SDS-PAGE gel (In particular, Figure 1, Table 2, page 3461, whole document).
Phosphopyruvate hydratase (O96656) is 100% identical to instant SEQ ID NO:455 as evidenced by the attached sequence alignment.
Absent evidence to the contrary, the 49 kDa polypeptide allergen in Penaeus monodon (black tiger shrimp) identified in Sahabudin et al. is phosphopyruvate hydratase of Uniprot Accession number O96656 which is 100% sequence identical to instant SEQ ID NO:455. Since the office does not have a laboratory to test the reference allergen, it is applicant's burden to show that the reference allergen is not SEQ ID NO:455 recited in the claim. See In re Best, 195 USPQ 430, 433 (CCPA 1977); In re Marosi, 218 USPQ 289, 292-293 (Fed. Cir. 1983); and In re Fitzgerald et al., 205 USPQ 594 (CCPA 1980).
Claims 12 and 18 are included in this rejection because determining the sequence of the reference allergen is merely further characterization of a known compound. Atlas Powder Co. V. IRECO, 51 USPQ2d 1943 (Fed. Cir. 1999) “Artisans of ordinary skill may not recognize the inherent characteristics or functioning of the prior art... However, the discovery of a previously unappreciated property of a prior art composition, or of a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer. “ The Court further held that “this same reasoning holds true when it is not a property but an ingredient which is inherently contained in the prior art”. The reference teachings anticipate the claimed invention.
The reference teachings anticipate the claimed invention.
12. Claims 12 and 18 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Tomm et al. (PTO-892; Reference X) as evidenced by the attached sequence alignment.
Tomm et al. teaches identification of allergenic proteins from Marsupenaeus japonicus using 2D gel with extracts from M japonicus and corresponding western blots; 200 μg of protein from M japonicus extracts were applied to a small (7-cm) strip for the first dimension followed by sodium dodecyl sulphate polyacrylamide gel electrophoresis using a 12% gel in the second dimension. Gels were blotted onto nitrocellulose membranes. After incubation with sera from prawn allergic patients, the blots were developed with an anti-IgE antibody conjugated with alkaline phosphatase. Preparative gels were stained with Coomassie after electrophoresis. The identified proteins are listed with the spot number taken from Figure B. Three IgE-reactive proteins were detected upon Western blot incubation and mass-spectrometric identification of protein spots (Figure B, spots 1-5 and Figure C). Phosphopyruvate hydratase, also called enolase, is a cytosolic protein of about 50 kDa involved in glycolysis and was one of the most abundant proteins in the sample (Figure B, spots 3 and 4). Strong IgE reactivity was found towards the 47 kDa protein phosphopyruvate hydratase (In particular Figure C).
Phosphopyruvate hydratase of A0A0S1LKK8 from Marsupenaeus japonicus is 100% identical to instant SEQ ID NO:481 as evidenced by the attached sequence alignment.
Absent evidence to the contrary, the 47 kDa polypeptide allergen in Marsupenaeus japonicus identified in Tomm et al. is phosphopyruvate hydratase of A0A0S1LKK8 which is 100% sequence identical to instant SEQ ID NO:481. Since the office does not have a laboratory to test the reference allergen, it is applicant's burden to show that the reference allergen is not SEQ ID NO:481 recited in the claim. See In re Best, 195 USPQ 430, 433 (CCPA 1977); In re Marosi, 218 USPQ 289, 292-293 (Fed. Cir. 1983); and In re Fitzgerald et al., 205 USPQ 594 (CCPA 1980).
Claims 12 and 18 are included in this rejection because determining the sequence of the reference allergen is merely further characterization of a known compound. Atlas Powder Co. V. IRECO, 51 USPQ2d 1943 (Fed. Cir. 1999) “Artisans of ordinary skill may not recognize the inherent characteristics or functioning of the prior art... However, the discovery of a previously unappreciated property of a prior art composition, or of a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer. “ The Court further held that “this same reasoning holds true when it is not a property but an ingredient which is inherently contained in the prior art”. The reference teachings anticipate the claimed invention.
The reference teachings anticipate the claimed invention.
13. 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.
14. Claim 13 is rejected under 35 U.S.C. 103 as being unpatentable over Tomm et al. (PTO-892; Reference X) as evidenced by the attached sequence alignment and further in view of U.S. Patent Application Publication 2006/0210590 (PTO-892; Reference A).
Tomm et al. has been discussed supra.
The claimed invention differs from the prior art in the recitation of administering the polypeptide of SEQ ID NO:481.
U.S. Patent Application Publication 2006/0210590 teaches a method for inducing tolerance in a subject who is allergic to an allergenic agent, the method comprising obtaining the allergen sensitisation profile of said subject or of the allergenic population to which the subject belongs, selecting a standardized allergen extract or allergen composition which matches the allergens to which the subject is allergic or which matches the major allergens reactive in the allergenic population, and subsequently administering repeated single dosage forms isolated from the standardized allergen extract or allergen composition to induce tolerance to the allergenic agent, wherein the standardized allergen extract and allergen composition are ones wherein 1) one single dosage form thereof comprises a total amount of major allergen found in said population not exceeding the maximum acceptable amount of any one single major allergen of said allergenic agent and/or the concentrations of major and minor allergens in the standardized allergen extract and allergen composition are controlled quantitatively, and 2) that one single dosage form thereof comprises an immunogenically effective amount of each of said major and optionally minor allergens. (In particular, claim 10, whole document).
It would have been obvious to one of ordinary skill in the art at the time of invention to have administered the 47 kDa Phosphopyruvate hydratase polypeptide which demonstrated strong IgE reactivity of Tomm et al. to a patient demonstrating IgE reactivity to the polypeptide to treat shrimp allergies. Absent evidence to the contrary, the 47 kDa polypeptide allergen in Marsupenaeus japonicus identified in Tomm et al. is phosphopyruvate hydratase of A0A0S1LKK8 which is 100% sequence identical to instant SEQ ID NO:481. Since the office does not have a laboratory to test the reference allergen, it is applicant's burden to show that the reference allergen is not SEQ ID NO:481 recited in the claim. See In re Best, 195 USPQ 430, 433 (CCPA 1977); In re Marosi, 218 USPQ 289, 292-293 (Fed. Cir. 1983); and In re Fitzgerald et al., 205 USPQ 594 (CCPA 1980).
From the reference teachings, it is apparent that one of ordinary skill in the art would have had a reasonable expectation of success in producing the claimed invention. Therefore, the invention as a whole was prima facie obvious to one of ordinary skill in the art at the time the invention was made, as evidenced by the reference, especially in the absence of evidence to the contrary.
15. Claim 13 is rejected under 35 U.S.C. 103 as being unpatentable over Sahabudin et al. (PTO-892; Reference V) as evidenced by Yang et al. (PTO-892; Reference W) and the sequence alignment and further in view of U.S. Patent Application Publication 2006/0210590 (PTO-892; Reference A).
Sahabudin et al. and Yang et al. have been discussed supra.
The claimed invention differs from the prior art in the recitation of administering the polypeptide of SEQ ID NO:455.
U.S. Patent Application Publication 2006/0210590 teaches a method for inducing tolerance in a subject who is allergic to an allergenic agent, the method comprising obtaining the allergen sensitisation profile of said subject or of the allergenic population to which the subject belongs, selecting a standardized allergen extract or allergen composition which matches the allergens to which the subject is allergic or which matches the major allergens reactive in the allergenic population, and subsequently administering repeated single dosage forms isolated from the standardized allergen extract or allergen composition to induce tolerance to the allergenic agent, wherein the standardized allergen extract and allergen composition are ones wherein 1) one single dosage form thereof comprises a total amount of major allergen found in said population not exceeding the maximum acceptable amount of any one single major allergen of said allergenic agent and/or the concentrations of major and minor allergens in the standardized allergen extract and allergen composition are controlled quantitatively, and 2) that one single dosage form thereof comprises an immunogenically effective amount of each of said major and optionally minor allergens. (In particular, claim 10, whole document).
It would have been obvious to one of ordinary skill in the art at the time of invention to have administered the 49 kDa polypeptide allergen from Penaeus monodon identified in Sahabudin et al. to treat shrimp allergies. Absent evidence to the contrary, the 49 kDa polypeptide allergen in Penaeus monodon (black tiger shrimp) identified in Sahabudin et al. is phosphopyruvate hydratase of Uniprot Accession number O96656 which is 100% sequence identical to instant SEQ ID NO:455. Since the office does not have a laboratory to test the reference allergen, it is applicant's burden to show that the reference allergen is not SEQ ID NO:455 recited in the claim. See In re Best, 195 USPQ 430, 433 (CCPA 1977); In re Marosi, 218 USPQ 289, 292-293 (Fed. Cir. 1983); and In re Fitzgerald et al., 205 USPQ 594 (CCPA 1980).
From the reference teachings, it is apparent that one of ordinary skill in the art would have had a reasonable expectation of success in producing the claimed invention. Therefore, the invention as a whole was prima facie obvious to one of ordinary skill in the art at the time the invention was made, as evidenced by the reference, especially in the absence of evidence to the contrary.
16. No claim is allowed.
17. Any inquiry concerning this communication or earlier communications from the examiner should be directed to NORA MAUREEN ROONEY whose telephone number is (571)272-9937. The examiner can normally be reached on M-F from 8:00am to 4:30pm.
If attempts to reach the examiner by telephone are unsuccessful, the examiner' s supervisor, Misook Yu, can be reached at telephone number (571) 272-0839. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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September 27, 2025
/Nora M Rooney/
Primary Examiner, Art Unit 1641