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 .
The amendment filed 12/12/25 has been entered. Claims 1-84, 90, 92 and 95 have been cancelled. Claims 85-89 and 91 have been cancelled. Claims 85-89, 91, 93-94 and 96-104 are pending and are under examination.
Claim Rejections Withdrawn
The rejection of claim 90 under 35 U.S.C. 101 because the claimed invention is directed to a composition of matter without significantly more is withdrawn in view of the cancellation of the claim.
The rejection of claim(s) 90 under 35 U.S.C. 102(a)(1) as being anticipated by Matsuda et al. US 6,372,225 4/16/2002 cited in IDS is withdrawn in view of the cancellation of the claim.
The rejection of claims 91-97 and 101-104 under 35 U.S.C. 102 (a)(1) as being anticipated by Yu et al. Mediators of Inflammation, vol. 2020, Article ID 9596129, 11 pages, cited in IDS as evidenced by Wolfe et al. US 8,703,733 B2 2/22/2014 is withdrawn in view of the cancellation of the claims.
The rejection of claim(s) 91-97 and 101-104 under 35 U.S.C. 103 as being unpatentable over Yu et al. Mediators of Inflammation, vol. 2020, Article ID 9596129, 11 pages, cited in IDS in view of Matsuda et al. US 6,372,225 4/16/22 cited in IDS and Wolfe et al. US 8,703,733 B2 2/22/2014 is withdrawn in view of the amendment to the claims.
The rejection of claim(s) 91 and 93 under 35 U.S.C. 103 as being unpatentable over Matsuda et al. US 6,372,225 cited in IDS 4/16/22 in view of by Wolfe et al. US 8,703,733 B2 2/22/2014 is withdrawn in view of the amendment to the claims.
Claim Rejections - 35 USC § 101 Maintained
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
The rejection of claims 85-89 under 35 U.S.C. 101 because the claimed invention is directed to a composition of matter without significantly more.
The claim(s) recite(s) an isolated tetanus toxin protein variant, comprising the segment C of the tetanus toxin protein and the partial segment of the translocation region of the tetanus toxin protein, wherein the variant is N-terminally truncated compared to the wild-type tetanus toxin protein and comprises the amino acid sequence set forth in SEQ ID NO: 1 or SEQ ID NO: 2.
Tetanus toxin protein comprises 3 domains A, B, and C. The translocation domain is the B domain. The A segment of the N-terminal of the tetanus toxin is toxic. See p. 17 of the specification first paragraph and p. 32 paragraph 4.
The claimed tetanus toxin protein variant does not exist in nature and thus it is compared to its closest counter-part which is the tetanus toxin protein.
“N-terminally truncated compared to wild-type” is recited at a high level of generality and this encompasses removal of one to a few amino acids at the N-terminal. There is no evidence that removal of one or two or three amino acids, at the N-terminal of the tetanus toxin changes its structure and function as tetanus toxin.
The claimed tetanus toxin protein variant is not markedly different from the tetanus toxin protein variant even though the bonds have been broken by removal of one or two amino acids at the N-terminal end, for example. Such a variant would reasonably still maintain structure and some function even though one or two amino acids at the N-terminal end have been removed.
For this reason, the claims are still drawn to a judicial exception i.e. a nature based product without significantly more.
Response to Applicants Argument
Applicants argue that the claimed protein is man-made, structurally engineered and functionally distinct and does not exist in nature.
Applicants point to TTD variant in the application SEQ ID NO: 1-2 which lacks the N-terminal sequence while retaining the C-terminal sequence.
Applicants argument is not persuasive because the isolated tetanus toxin protein variant comprises SEQ ID NO: 1 or 2.
In the claims, “N-terminally truncated compared to wild-type” is recited at a high level of generality and this encompasses removal of one to a few amino acids at the N-terminal. “N-terminally truncated” is not limited to the interpretation which means the removal of fragment A of tetanus toxin.
Applicants argument that the claimed variant lacks toxicity of the tetanus toxin protein is not persuasive. There is no evidence that removal of one or two or three amino acids, at the N-terminal end of the tetanus toxin changes its structure and function as tetanus toxin.
Applicant’s argument that absence of N-terminal domain is the result of intentional sequence engineering is not persuasive. The specification while showing that TTD1 and TTD2 variants maintains correct folded structure, stability and binding function while lacking toxicity, this is not what is being claimed. This is because “N-terminally truncated” is more broadly interpreted to encompass as little as one amino acid removed from the N terminal end.
For this reason, the rejection is maintained.
Claim Rejections - 35 USC § 102 Maintained
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
The rejection of claim(s) 85-88 and 98-100 under 35 U.S.C. 102(a)(1) as being anticipated by Matsuda et al. US 6,372,225 4/16/2002 cited in IDS is maintained.
Claim 85: Matsuda et al disclose a tetanus toxin protein variant (a tetanus toxin functional fragment antigen -FFA), comprising the segment C (fragment C) of the tetanus toxin protein and the partial segment of the translocation region (fragment B) of the tetanus toxin protein, wherein the variant is N-terminally truncated compared to the wild -type. See figure 1C showing the structure of tetanus toxin and the location of the disulfide bonds, column 5 lines 35-56 disclosing splitting the disulfide bonds to obtain the light chain (fragment A) and heavy chain comprising fragment B and C (see column 8 lines 24-36).
Said tetanus toxin protein variant is SEQ ID NO: 17 or SEQ ID NO: 16 which comprises the segment C (fragment C) of the tetanus toxin protein and the partial segment of the translocation region (fragment B) and comprises the amino acid sequence shown in SEQ ID NO: 1 and SEQ ID NO: 2.
SEQ ID NO: 17 and SEQ ID NO: 16 of Matsuda et al are both N-terminally truncated as compared to the wild-type tetanus toxin protein sequence SEQ ID NO: 1 of Matsuda et al. See sequence annotation below showing that SEQ ID NO: 17 corresponds to amino acids 463-1315 of the full length tetanus toxin protein sequence and SEQ ID NO: 16 corresponds to amino acids 458-1315 of the full length tetanus toxin protein sequence.
Claim 86: the partial segment of the translocation region comprises the T cell epitope P2 (amino acids 830-844) of the translocation region of the tetanus toxin protein. See sequence alignment below.
Claim 87: the partial segment of the translocation region comprises amino acids 829-864 of the tetanus toxin protein. See sequence alignment below.
Claim 88: the toxin protein variant of Matsuda et al, wherein the partial segment of the translocation region comprises the amino acid sequence shown in SEQ ID NO: 7 or 8. See sequence alignment below.
Alignment with SEQ ID NO: 1:
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901
629
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900
611
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Alignment with SEQ ID NO: 2
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829
682
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889
686
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Alignment with SEQ ID NO: 7:
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870
608
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Alignment with SEQ ID NO: 8:
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882
657
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Claim 98-100: Matsuda et al disclose a nucleic acid molecule (DNA), comprising a sequence encoding the tetanus toxin protein variant (a tetanus toxin functional fragment antigen -FFA); a vector comprising the DNA; and a host cell comprising the nucleic acid molecule. See column 6 lines 38-46.
Response to Applicant’s Argument
Applicant’s argue that the protein variant set forth in the present claims lacks the N-terminal sequence while retaining the C-terminal sequence and that Matsuda et al does not disclose such a protein which is truncated.
Applicant’s argument has been carefully considered but is not found persuasive. The instant claims state that the tetanus toxin protein variant is N-terminally truncated compared to wild-type tetanus toxin protein.
SEQ ID NO: 17 and SEQ ID NO: 16 are both N-terminally truncated and comprise the amino acid sequence set forth in SEQ ID NO: 1 or SEQ ID NO: 2. See sequence alignments above.
The sequence annotation for the sequences of Matsuda et al disclose that SEQ ID NO: 17 corresponds to amino acids 463-1315 of the full length tetanus toxin protein sequence thus lacking the N-terminal amino acids 1-462 and SEQ ID NO: 16 corresponds to amino acids 458-1315 of the full length tetanus toxin protein sequence thus lacking the N-terminal amino acids 1-457. Thus, the proteins of Matsuda et al are N terminally truncated compared to wild-type tetanus toxin protein.
Claim Rejections - 35 USC § 103 Maintained
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.
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.
Claim(s) 85 and 89 is/are rejected under 35 U.S.C. 103 as being unpatentable over Matsuda et al. US 6,372,225 4/16/22 cited in IDS in view of as evidenced by Wolfe et al. US 8,703,733 B2 2/22/2014.
Claim 85: Matsuda et al disclose a tetanus toxin protein variant (a tetanus toxin functional fragment antigen -FFA), comprising the segment C (fragment C) of the tetanus toxin protein and the partial segment of the translocation region (fragment B) of the tetanus toxin protein. See figure 1C showing the structure of tetanus toxin and the location of the disulfide bonds, column 5 lines 35-56 disclosing splitting the disulfide bonds to obtain the light chain (fragment A) and heavy chain comprising fragment B and C (see column 8 lines 24-36).
Said tetanus toxin protein variant is SEQ ID NO: 17 or SEQID NO: 16 which comprises comprising the segment C (fragment C) of the tetanus toxin protein and the partial segment of the translocation region (fragment B) and comprises the amino acid sequence shown in SEQ ID NO: 1 and SEQ ID NO: 2.
SEQ ID NO: 17 and SEQ ID NO: 16 are both N-terminally truncated and comprise the amino acid sequence set forth in SEQ ID NO: 1 or SEQ ID NO: 2. See sequence alignments above.
The sequence annotation for the sequences of Matsuda et al disclose that SEQ ID NO: 17 corresponds to amino acids 463-1315 of the full length tetanus toxin protein sequence thus lacking the N-terminal amino acids 1-462 and SEQ ID NO: 16 corresponds to amino acids 458-1315 of the full length tetanus toxin protein sequence thus lacking the N-terminal amino acids 1-457.
See sequence alignments above.
Matsuda et al does not disclose the segment/fragment C of the tetanus toxin variant FFA comprises the amino acid sequence shown in SEQ ID NO:3.
Wolfe et al discloses a humanized C fragment of tetanus toxin comprising the amino acid sequence shown in SEQ ID NO: 3. See sequence alignment below. Wolfe et al disclose the humanized C fragment of tetanus toxin is a result of using codons that are more abundantly utilized in humans results in order to increase expression in human cells and the amino acid sequence remains the same. See column 3 lines 21-45.
It would have been prima facie obvious to a person of ordinary skill in the art as of the effective filing date to have modified Matsuda et al by substituting the C fragment of the tetanus toxin functional fragment antigen -FFA with the C fragment of Wolfe et al, thus resulting in the instant invention with a reasonable expectation of success.
The C fragment of Matsuda and the C fragment of Wolfe et al are known in the art and one of ordinary skill in the art could have substituted the C fragment of Matsuda with the C fragment of Wolfe et al, while still maintaining the binding activity of the C fragment, thus yielding predictable results. KSR Int'l Co. v. Teleflex Inc., 550 U.S. 398, 415-421, 82 USPQ2d 1385, 1395-97 (2007) – simple substitution of one known element for another to obtain predictable results.
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Response to Applicant’s Argument
Applicant’s argue that the protein variant set forth in the present claims lacks the N-terminal sequence while retaining the C-terminal sequence and that Matsuda et al does not disclose such a protein which is truncated.
Applicant’s argument has been carefully considered but is not found persuasive. The instant claims state that the tetanus toxin protein variant is N-terminally truncated compared to wild-type tetanus toxin protein.
SEQ ID NO: 17 and SEQ ID NO: 16 are both N-terminally truncated and comprise the amino acid sequence set forth in SEQ ID NO: 1 or SEQ ID NO: 2. See sequence alignments above.
The sequence annotation for the sequences of Matsuda et al disclose that SEQ ID NO: 17 corresponds to amino acids 463-1315 of the full length tetanus toxin protein sequence thus lacking the N-terminal amino acids 1-462 and SEQ ID NO: 16 corresponds to amino acids 458-1315 of the full length tetanus toxin protein sequence thus lacking the N-terminal amino acids 1-457.
Applicants argue that the sequence of the tetanus toxin protein variant in the present application is substantially different from the sequences disclosed in Matsuda et al and thus the structure, function, stability and practical performance of the tetanus toxin protein variant of the present application are not predictable from Matsuda or Wolfe alone or in combination and that the structure and stability and its expression was verified by electrophoretic analysis is not taught or suggested by Matsuda et al and/or Wolfe et al.
This argument has been carefully considered but is not found persuasive. As stated above, Matsuda et al discloses the isolated tetanus toxin protein variant comprising the segment C and the partial segment of the translocation region and the variant is N-terminally truncated compared to wild type and comprises SEQ ID NO: 1 and SEQ ID NO:2.
Limitations of the truncated tetanus toxin protein variants disclosed in the specification are not read into the claims. The claimed isolated tetanus toxin variant is not limited to the variants taught in the specification. Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993).
New Claim Rejections Based on Amendment
Claim(s) 91, 93-94, 96-97 and 101-104 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Shin et al. WO 2021/021729 2/4/2021 as evidenced by Wolfe et al. US 8,703,733 B2 2/22/2014.
Shin et al disclose a polysaccharide-protein conjugate comprising a polysaccharide from S. pneumoniae and a carrier protein such as fragment C of tetanus toxin or tetanus toxoid, wherein the polysaccharide is selected from S. pneumoniae serotypes 1, 3, 4, 5, 6A, 6B, 7F, 8, 9N, 10A, 11A, 12F, 15B, 18C, 19A, 19F, 22F and 33F. See paragraph 8, 148, 149 and 150.
As evidenced by Wolfe et al the segment/fragment C of tetanus toxin protein comprises the amino acid sequence show in SEQ ID NO: 3. See sequence alignment below of SEQ ID NO: 4 of Wolf et al with SEQ ID NO: 3 of the instant application below. See Wolfe et al figure 4, column 3 lines 1-2.
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Claim 96: Shin et al disclose the mass ratio of the polysaccharide to the truncated tetanus toxin protein fragment C is 0.4 to 2.3 or about 2.3 or about 2.5. see paragraph 194-195.
Claim 97: Shin et al discloses the step of providing the polysaccharide protein conjugate. See paragraph 8, 148, 149, 150 and 174-190.
Claims 101-102 and 104: Shin et al disclose a pharmaceutical composition or vaccine or kit comprising the conjugate and optionally a pharmaceutically acceptable adjuvant. See paragraph 8, 174-190.
Claim 103: Shin et al disclose a method for preventing a disease caused by S. pneumoniae infection, comprising administering the vaccine to a subject in need thereof. See paragraphs 190 and 203.
Claim(s) 91, 93-94, 96, 97 and 101-104 is/are rejected under 35 U.S.C. 103 as being unpatentable over Shin et al. WO 2021/021729 2/4/2021 in view of Wolfe et al. US 8,703,733 B2 2/22/2014.
Shin et al disclose a polysaccharide-protein conjugate comprising a polysaccharide from S. pneumoniae and a carrier protein such as fragment C of tetanus toxin or tetanus toxoid, wherein the polysaccharide is selected from S. pneumoniae serotypes 1, 3, 4, 5, 6A, 6B, 7F, 8, 9N, 10A, 11A, 12F, 15B, 18C, 19A, 19F, 22F and 33F. See paragraph 8, 148, 149 and 150.
Claim 96: Shin et al disclose the mass ration of the polysaccharide to the truncated tetanus toxin protein fragment C is 0.4 to 2.3 or about 2.3 or about 2.5. see paragraph 194-195.
Claim 97: Shin et al discloses the step of providing the polysaccharide protein conjugate. See paragraph 8, 148, 149, 150 and 174-190.
Claims 101-102 and 104: Shin et al disclose a pharmaceutical composition or vaccine or kit comprising the conjugate and optionally a pharmaceutically acceptable adjuvant. See paragraph 8, 174-190.
Claim 103: Shin et al disclose a method for preventing a disease caused by S. pneumoniae infection, comprising administering the vaccine to a subject in need thereof. See paragraphs 190 and 203.
Shin et al does not disclose that the fragment C of tetanus toxin comprises the amino acid sequence shown in SEQ ID NO: 3.
Wolfe et al discloses a humanized C fragment of tetanus toxin comprising the amino acid sequence shown in SEQ ID NO: 3. See sequence alignment below. Wolfe et al disclose the humanized C fragment of tetanus toxin is a result of using codons that are more abundantly utilized in humans results in order to increase expression in human cells and the amino acid sequence remains the same. See column 3 lines 21-45.
It would have been prima facie obvious to a person of ordinary skill in the art as of the effective filing date to have modified Shin et al by substituting the C fragment of the tetanus toxin with the C fragment of tetanus toxin Wolfe et al, thus resulting in the instant invention with a reasonable expectation of success.
The C fragment of tetanus toxin of Shin et al and the C fragment of the tetanus toxin of Wolfe et al are known in the art and one of ordinary skill in the art would have been able to substitute the C fragments, while still maintaining the binding activity of the C fragment, thus yielding predictable results. KSR Int'l Co. v. Teleflex Inc., 550 U.S. 398, 415-421, 82 USPQ2d 1385, 1395-97 (2007) – simple substitution of one known element for another to obtain predictable results.
Claim(s) 91, 93, 96, 97 and 101-104 is/are rejected under 35 U.S.C. 103 as being unpatentable over Shin et al. WO 2021/021729 2/4/2021 in view of Matsuda et al. US 6,372,225 4/16/2002.
Shin et al disclose a polysaccharide-protein conjugate comprising a polysaccharide from S. pneumoniae and a carrier protein such as a tetanus toxoid, wherein the polysaccharide is selected from S. pneumoniae serotypes 1, 3, 4, 5, 6A, 6B, 7F, 8, 9N, 10A, 11A, 12F, 15B, 18C, 19A, 19F, 22F and 33F. See paragraph 8, 148, 149 and 150.
Claim 96: Shin et al disclose the mass ration of the polysaccharide to the truncated tetanus toxin protein fragment C is 0.4 to 2.3 or about 2.3 or about 2.5. see paragraph 194-195.
Claim 97: Shin et al discloses the step of providing the polysaccharide protein conjugate. See paragraph 8, 148, 149, 150 and 174-190.
Claims 101-102 and 104: Shin et al disclose a pharmaceutical composition or vaccine or kit comprising the conjugate and optionally a pharmaceutically acceptable adjuvant. See paragraph 8, 174-190.
Claim 103: Shin et al disclose a method for preventing a disease caused by S. pneumoniae infection, comprising administering the vaccine to a subject in need thereof. See paragraphs 190 and 203.
Shin et al does not disclose that the tetanus toxoid is a truncated tetanus toxin protein comprising the amino acid sequence shown in SEQ ID NO: 1-2.
Matsuda et al disclose a tetanus toxin protein variant (a tetanus toxin functional fragment antigen -FFA), comprising the segment C (fragment C) of the tetanus toxin protein and the partial segment of the translocation region (fragment B) of the tetanus toxin protein, wherein the variant is N-terminally truncated compared to the wild -type. See figure 1C showing the structure of tetanus toxin and the location of the disulfide bonds, column 5 lines 35-56 disclosing splitting the disulfide bonds to obtain the light chain (fragment A) and heavy chain comprising fragment B and C (see column 8 lines 24-36).
Said tetanus toxin protein variant is SEQ ID NO: 17 or SEQ ID NO: 16 which comprises comprising the segment C (fragment C) of the tetanus toxin protein and the partial segment of the translocation region (fragment B) and comprises the amino acid sequence shown in SEQ ID NO: 1 and SEQ ID NO: 2.
SEQ ID NO: 17 and SEQ ID NO: 16 of Matsuda et al are both N-terminally truncated as compared to the wild-type tetanus toxin protein sequence SEQ ID NO: 1 of Matsuda et al. See sequence annotation below showing that SEQ ID NO: 17 corresponds to amino acids 463-1315 of the full length tetanus toxin protein sequence and SEQ ID NO: 16 corresponds to amino acids 458-1315 of the full length tetanus toxin protein sequence.
The partial segment of the translocation region comprises the T cell epitope P2 (amino acids 830-844) of the translocation region of the tetanus toxin protein. See sequence alignment above for Matsuda et al
See sequence alignment for SEQ ID NO: 1-2 above for Matsuda et al.
Matsuda et al disclose that tetanus toxoid is normally detoxified with formalin. However, formalin detoxified tetanus toxin has disadvantages in that there are various adverse side effects, the product quality is uneven among different manufacturers, that the retention of immunity is limited to only approximately 5 to 10 years and, therefore, repeated vaccinations are necessary to keep the antitoxin level sufficient to prevent tetanus infection. Thus, the conventional tetanus toxoid has problems to be solved with respect to safety, control of quality, retention of immunity, and ease, labor saving and economy in administration. See column 2.
Matsuda et al disclose that fragments of the tetanus toxin can be used to avoid the adverse effects of the conventional tetanus toxoid. See column 3.
Matsuda et al disclose that the functional fragment antigen (FFA) of tetanus toxin disclosed therein has an immunopotency which is substantially the same as that of the whole tetanus toxin toxoid. In addition, the tetanus toxin functional fragment antigen (FFA) of the present invention is extremely excellent with respect to the diminution of adverse side effects, as compared to conventional whole tetanus toxin toxoids. See under Definition of "FFA" of the Present Invention. Matsuda et al disclose that the FFA can be used without detoxification but can be stabilized by fixation using a fixative. See under stabilization of FFA.
It would have been prima facie obvious to a person of ordinary skill in the art as of the effective filing date to have modified Shin et al by substituting the tetanus toxoid of the conjugate with the tetanus toxin fragments of Matsuda et al i.e. the FFA or FFA toxoid al, thus resulting in the instant invention with a reasonable expectation of success.
The motivation to do so is that Matsuda et al disclose that conventional tetanus toxoid as many disadvantages as disclosed above, and that the FFA or FFA toxoids has an immunopotency which is substantially the same as that of the whole tetanus toxin toxoid and the tetanus toxin functional fragment antigen (FFA) is extremely excellent with respect to the diminution of adverse side effects, as compared to conventional whole tetanus toxin toxoids.
Status of Claims
Claims 85-89, 91, 93-94 and 96-104 are rejected.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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/OLUWATOSIN A OGUNBIYI/ Primary Examiner, Art Unit 1645