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 .
Election/Restrictions
Applicant’s election without traverse of Group I, claims 1-15, in the reply filed on 2/12/2026 is acknowledged. Claims 16-19 and 20 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 2/12/2026.
Priority
Priority to US 63/104,196, filed 10/22/2020, is acknowledged.
Information Disclosure Statement
The information disclosure statements (IDS) were submitted on 4/21/2023 and 9/16/2024, before the mailing of a first office action. The submissions are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Claim Status
Claims 1-20, filed 2/12/2026, are pending. Claims 1-15 are under examination. Claim 16-20 are withdrawn.
Claim Interpretation
Regarding claim 1, for purposes of compact prosecution, the sequence SEQ ID NO: 18 shall be interpreted in such a way to be consistent with the specification and the sequence listing. That is to say, the eighth position is interpreted to be a histidine (His) and the fourteenth position is tyrosine (Tyr).
Claim Objections
Claim 3 is objected to because of the following informalities. Claim 3 uses the term “comprised”. For consistency, using the term “comprises” would be better. “Comprised” is past tense, and the rest of the verbs in the claim are in the present tense. Appropriate correction is required.
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 1-15 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.
Regarding claim 1, claim 1 recites the sequence R-GIVEQCCESICSLEQLENYCN (SEQ ID NO:18), but SEQ ID NO: 18 is listed as GIVEQCCHSICSLYQLENYCN. These two sequences do not match. It is not clear which sequence is actually being claimed by claim 1.
Furthermore, R is described as an N-terminal extension of SEQ ID NO: 18. It is not clear whether R represents more amino acids or is another kind of molecule entirely.
Claim 1 is rejected.
Regarding claim 2-4, these claims fail to resolve the indefiniteness of claim 1.
Claims 2-4 are rejected.
Regarding claim 5, the scope of claim 5 is indefinite because the Thr-ol is a 1,3 diol and not a 1, 2 diol. Claim 5 is dependent upon claim 2 which in turn is dependent upon claim 1. Claim 1 requires that the B chain ends with Thr-ol, because Thr-ol cannot extend the polypeptide chain further.
Thr-ol cannot extend the polypeptide chain because Thr-ol, depicted below:
PNG
media_image1.png
138
180
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Greyscale
(Specification, Fig. 8)
lacks a C-terminal carboxyl group to react with an amine from another amino acid in polypeptide formation.
Furthermore, Thr-ol is a 1,3 diol, not a 1,2 diol. It is unclear how the B chain C-terminus can be a 1,2 diol given the constraints of claim 1.
This claim also fails to resolve the indefiniteness of claim 1 and does not further limit claim 1.
Claim 5 is rejected.
Regarding claim 6, claim 6 depends from claim 2, which in turn depends from claim 1. This claim fails to resolve the indefiniteness of claim 1 that is also present in claim 2. Furthermore, this claim fails to further limit claim 2 or claim 1 because claim 1 requires a Thr-ol at the C-terminus which is a 1,3 diol already.
Claim 6 is rejected.
Regarding claim 7, claim 7 fails to resolve the indefiniteness of claim 1.
Claim 7 is rejected.
Regarding claim 8, claim 7 is rejected as described above. Claim further recites the case wherein the modified amino acid is thiol-containing. This does not resolve the indefiniteness generated by claim 7.
This claim also fails to resolve the indefiniteness of claim 1.
Claim 8 is rejected.
Regarding claims 9 and 10, these claim fails to resolve the indefiniteness of claim 1.
Claims 9-10 are rejected.
Regarding claim 11, claim 11 recites the case wherein the B chain is extended by two amino acids positions GluB31 and LysB32. It is not clear how the B chain of claim 1 can be extended past B28 because Thr-ol precludes extension of the polypeptide chain.
This claim also fails to resolve the indefiniteness of claim 1.
Claim 11 is rejected.
Regarding claim 12, claim 12 recites the case wherein the B chain is extended by two amino acids positions and X30 is a diol bearing amino acid. It is not clear how the B chain of claim 1 can be extended past B28 because Thr-ol precludes extension of the polypeptide chain.
This claim also fails to resolve the indefiniteness of claim 1.
Claim 12 is rejected.
Regarding claim 13, claim 13 recites the case wherein the B chain is FVNQHLCGSHLVEALYLVCGERGFF[Sar][APD] (SEQ ID NO: 37). Is not clear how the B chain can comprise FVNQHLCGSHLVEALYLVCGERGFFYT[Thr-ol] and simultaneously consist of FVNQHLCGSHLVEALYLVCGERGFF[Sar][APD].
This claim also fails to resolve the indefiniteness of claim 1.
Claim 13 is rejected.
Regarding claim 14, claim 14 recites the case wherein the B chain is FVNQHLCGSHLVEALYLVCGERGFFYTKPX31X30 (SEQ ID NO: 12). Is not clear how the B chain can comprise FVNQHLCGSHLVEALYLVCGERGFFYT[Thr-ol] and simultaneously consist of FVNQHLCGSHLVEALYLVCGERGFFYTKPX31X30.
Furthermore, it is not clear with X31 is in the B30 location and why X30 is in the B31 location.
This claim also fails to resolve the indefiniteness of claim 1.
Claim 14 is rejected.
Regarding claim 15, claim 15 further defines the R group of the A chain. This claim does, resolves the indefiniteness of claim 1 above. However, this does not resolve the indefiniteness of claim 12 or claim 13.
Claim 15 is rejected.
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, 2, 6, 7, and 10 are rejected under 35 U.S.C. 103 as being unpatentable over UniProt Entry P01308 (https://www.uniprot.org/uniprotkb/P01308/entry, accessed 3/12/2026, published 11/1/1988) over Weiss et al. (Weiss, et al. Journal of Biological Chemistry 276.43: 40018-40024. (2001)), Ciszak et al. (Ciszak, et al. Structure 3.6: 615-622 (1995)), Weiss et al. 2 US20180057559, published 3/1/2018, Slieker et al. (Slieker, et al. Diabetologia 40.Suppl 2: S54-S61 (1997)), Kashida, et al. (Kashida et al., Organic & Biomolecular Chemistry 6.16: 2892-2899 (2008)), and Reddy et al. (Reddy, et al., International Journal of Peptides 2012.1: 323907 (2012)).
Regarding claim 1, claim 1 recites: “An insulin analogue consisting of an A chain modified by a glucose-binding element at or near its N terminus and a variant B chain comprising a diol group at the C terminus of the B chain such that the polypeptide chain ends with a hydroxyl group rather than with a carboxylate group, wherein in the A chain comprises a polypeptide sequence of R-GIVEQCCESICSLEQLENYCN (SEQ ID NO:18) where R indicates an N-terminal extension of the A chain comprising the glucose-binding element, and the B chain comprises a polypeptide sequence of FVNQHLCGSHLVEALYLVCGERGFFYT[Thr-ol] (SEQ ID NO: 9).
Uniprot discloses Insulin A chain as having the sequence GIVEQCCTSICSLYQLENYCN and Insulin B chain as having the sequence FVNQHLCGSHLVEALYLVCGERGFFYTPKT.
Uniprot does not disclose the A chain sequence R-GIVEQCCHSICSLEQLENYCN or the B chain sequence FVNQHLCGSHLVEALYLVCGERGFFYT[Thr-ol].
However, with respect to the A chain, Weiss et al. discloses that: “Previous studies have demonstrated that the potency and thermodynamic stability of human insulin are enhanced in concert by substitution of ThrA8 by arginine or histidine. These surface substitutions stabilize the N-terminal α-helix of the A chain, a key element of hormone-receptor recognition.” (Weiss et al., page 40018, Abstract).
Weiss et al. 2 discloses the usage of an A chain with a glucose-binding moiety at or within 5 residues of the N-terminus: “ An insulin analogue containing a modified A-chain polypeptide and a modified B-chain polypeptide, wherein the A-chain is modified with a monomeric glucose-binding moiety at or within 5 residues of the A-chain N-terminus, and wherein the B-chain is modified with a diol-containing modification or an alpha-hydroxycarboxylate modification at or within 6 residues of the B-chain C terminus.” (Weiss et al. 2, claim 1).
With respect to the B chain, Ciszak et al. discloses that: “Although removal of B29 and B30 does not significantly reduce association, the removal or replacement of ProB28 does alter these properties, which strongly suggests that ProB28 is critical to dimer stabilization and hence hexamer formation.” (Ciszak et al., page 615, col. 2, para. 1).
With respect to the Pro -> Thr-ol substitution, Weiss et al. 2 discloses the incorporation of diols at the C-terminus of the B chain: “The second element is a N-linked or O-linked monosaccharide, disaccharide, or oligosaccharide at one or near the C-terminus of the B-chain polypeptide, that is at one or more of the positions B27, B28, B29, B30, or as attached to a peptide extension of the B-chain containing one residue (B31) or two residues (B31-B32). Alternatively, a nonstandard diol-containing amino acid such as L-DOPA or D-DOPA may be substituted at any of B27-B30.” (Weiss et al. 2, para. [0011]).
Weiss et al. 2 does not disclose the usage of Threoninol; however, Slieker et al. discloses that a Pro -> Thr substitution is well-tolerated at position 28, with the Thr mutant having a potency of 1.09. (Slieker, et al., page S56, Table 1). Kashida et al. discloses that Thr-ol is an obvious variant of Thr: ” Threoninol is an amino acid derivative that can be synthesized by one-step reduction from threonine.” (Kashida et al., page 2892, col. 2, para. 2).
In addition to the efficacy of Thr-ol in the disclosure of Weiss et al. 2, Thr-ol also is useful for anchoring of a synthetic peptide synthesis product: “It was found that Fmoc-Thr-OL gives better loading than Fmoc-Thr(tBu)-OL.” (Reddy et al., page 2, col. 2, para. 2).
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to make the modifications to the sequences disclosed by UniProt as disclosed by Weiss et al., Ciszak et al., Weiss et al. 2, Slieker et al., Kahshida et al., and Reddy et al. to arrive at the claimed invention.
A person of ordinary skill in the art would be motivated to make such modifications to achieve an A chain and a B chain capable of performing glucose-responsive binding as described by Weiss et al. 2: “It is, therefore, an aspect of the present invention to provide insulin analogues that provide glucose-responsive binding to the insulin receptor and hence glucose-regulated bioactivity. The analogues of the present invention contain two essential elements.” (Weiss et al. 2, para. [0011]). These elements are “The first element is a phenylboronic acid derivative (including a spacer element) at the α-amino group of Glycine at position A1 (GlyA1) or optionally at either the ε-amino group of D-Lysine as an amino-acid substitution well tolerated at position A1 (D-LysA1) or the ε-amino group of L-Lysine as a substitution at position A4 (L-LysA4)” (Weiss et al. 2, para. [0011]) and the previously mentioned “…a nonstandard diol-containing amino acid such as L-DOPA or D-DOPA may be substituted at any of B27-B30.” (Weiss et al. 2, para. [0011]).
For this usage, a person of ordinary skill in the art would use the A chain with a glucose binding moiety to fulfill the first element. The second element would be the Thr-ol, which is a nonstandard diol-containing amino acid. A person of ordinary skill in the art would be motivated to substitute at the B28 position because Slieker et al. discloses that a Thr is well-tolerated in this position.
Based off the teachings of Slieker et al., serinol would also be a viable choice, but no other amino acid disclosed by Slieker as being well-tolerated is easily converted into a diol via the teachings of Kashida et al. Therefore, a finite number of choices exist and Thr-ol would be obvious to try based off this teaching.
A person of ordinary skill in the art would truncate the sequence of Uniprot to take advantage of having a Thr-ol available for diol interactions as described in Weiss et al. 2 (Weiss et al. 2, para. [0011]) and Ciszak et al. discloses that such a truncation is well-tolerated.
A person of ordinary skill in the art would also be motivated to utilize Thr-ol in the event of FMOC synthesis of the claimed peptides to take advantage of the loading properties discussed by Reddy above. A person of ordinary skill in the art would truncate the sequence of Uniprot to take advantage of having a Thr-ol available for loading and Ciszak et al. discloses that such a truncation is well-tolerated.
A person of ordinary art would have a reasonable expectation of success because Ciszak describes the truncation as well-tolerated. Slieker et al. discloses that Thr is well-tolerated at the B28 position. The modifications described above would also fulfill the two required elements of the glucose-responsive binding to the insulin receptor and hence glucose-regulated bioactivity as described by Weiss et al. 2, the use the A chain with a glucose binding moiety and a B chain with a nonstandard diol-containing amino acid at any of B27-B30.
Consequently, claim 1 is obvious over Uniprot in view of Weiss et al., Ciszak et al., Weiss et al. 2, Slieker et al., Kashida, et al., and Reddy et al. and rejected.
Regarding claim 2, claim 1 is obvious as described above. Claim 2 further recites the case wherein the A chain contains a substitution at position A8 that enhances affinity of the insulin analogue for the insulin receptor, wherein the substitution at position A8 is histidine.
As currently interpreted, position A8 is already histidine and described above: Weiss et al. discloses that: “Previous studies have demonstrated that the potency and thermodynamic stability of human insulin are enhanced in concert by substitution of ThrA8 by arginine or histidine. These surface substitutions stabilize the N-terminal α-helix of the A chain, a key element of hormone-receptor recognition.” (Weiss et al., page 40018, Abstract).
Consequently, claim 2 is obvious over Uniprot in view of Weiss et al., Ciszak et al., Weiss et al. 2, Slieker et al., Kashida, et al., and Reddy et al. and rejected.
Regarding claim 6, claim 2 is obvious as described above. Claim 6 further recites the case wherein the C-terminus of the B chain is an aliphatic (1,3) diol. Thr-ol is an aliphatic (1,3) diol.
Consequently, claim 6 is obvious over Uniprot in view of Weiss et al., Ciszak et al., Weiss et al. 2, Slieker et al., Kashida, et al., and Reddy et al. and rejected.
Regarding claim 7, claim 1 is obvious as described above. Claim 7 recites the case wherein position 28 is substituted for a diol-bearing ornithine residue.
Weiss discloses the substitution of a diol-bearing ornithine at or within 6 residues of the C-terminal of the B chain:
“1. An insulin analogue containing a modified A-chain polypeptide and a modified B-chain polypeptide, wherein the A-chain is modified with a monomeric glucose-binding moiety at or within 5 residues of the A-chain N-terminus, and wherein the B-chain is modified with a diol-containing modification or an alpha-hydroxycarboxylate modification at or within 6 residues of the B-chain C terminus.
2. The insulin analogue of claim 1, wherein the diol-containing modification is conjugated through the side chain of a D-amino acid containing a thiol group or containing an amino group.
3. The insulin analogue of claim 2, wherein the D-amino acid is D-Cysteine, D-Homocysteine, D-Lysine, D-Ornithine, D-diaminobutyric acid, or D-diaminopropionic acid.”
(Weiss et al., claims 1-3).
Slieker et al. discloses that ornithine is well-tolerated in position 28, yielding a slightly better EC50 than lysine or cysteine.
It would have been obvious to a person of ordinary skill in the art to substitute a diol-bearing ornithine as disclosed by Weiss at position 28 as disclosed by Slieker to arrive at the claimed invention.
A person of ordinary skill in the art would be motivated to use a diol-bearing ornithine residue in place of Thr-ol in order to retain an free carboxyl group so the resulting peptide could still be extended in the future while still retaining the beneficial activity of the diol group. Furthermore, ornithine is slightly better tolerated at position 28 than at least two of the other residues recited by Weiss.
A person of ordinary skill in the art would have a reasonable expectation of success because Slieker discloses that ornithine is well-tolerated at that position and Weiss has made use of diol-bearing ornithine previously as disclosed above.
Consequently, claim 7 is obvious over Uniprot in view of Weiss et al., Ciszak et al., Weiss et al. 2, Slieker et al., Kashida, et al., and Reddy et al. and rejected.
Regarding claim 10, claim 1 is obvious as described above. Claim 10 further recites the case wherein B29 and B30 are removed and a diol group is located at the C-terminus of the B chain. Claim 1 already requires Thr-ol at position B28, which precludes the presence of a B29 or B30. Thr-ol also has a diol group.
Consequently, claim 10 is obvious over Uniprot in view of Weiss et al., Ciszak et al., Weiss et al. 2, Slieker et al., Kashida, et al., and Reddy et al. and rejected.
Claim 3 is rejected under 35 U.S.C. 103 as being unpatentable over UniProt Entry P01308 (https://www.uniprot.org/uniprotkb/P01308/entry, accessed 3/12/2026, published 11/1/1988) over Weiss et al. (Weiss, et al. Journal of Biological Chemistry 276.43: 40018-40024. (2001)), Ciszak et al. (Ciszak, et al. Structure 3.6: 615-622 (1995)), Weiss et al. 2 US20180057559, published 3/1/2018, Slieker et al. (Slieker, et al. Diabetologia 40.Suppl 2: S54-S61 (1997)), Kashida, et al. (Kashida et al., Organic & Biomolecular Chemistry 6.16: 2892-2899 (2008)), and Reddy et al. (Reddy, et al., International Journal of Peptides 2012.1: 323907 (2012)) as applied to claim 1 above, and further in view of Chu et al. (Chu, et al. Journal of protein chemistry 11.5: 571-577 (1992)).
Regarding claim 3, claim 1 is obvious as described above. Claim 3 further recites the case wherein the A chain contains a substitution at position A8 and position A14 that enhances thermodynamic stability of the insulin analogue for the insulin receptor, wherein the substitution at position A8 and A14 comprises GluA8 and GluA14.
Regarding GluA8, Weiss et al. discloses that: “Surprisingly, the extent of stabilization conferred by GluA8(ΔΔG u = 1.1 ± 0.2 kcal/mol) is greater than that conferred by HisA8 (ΔΔGu = 0.4 ± 0.2 kcal/mol).” (Weiss et al., page 40020, col. 2, para. 2).
Regarding GluA14, Chu et al. discloses that this substitution results in higher lipogenesis as compared to the wild-type tyrosine. (Chu et al. page 574, Table I).
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to modify the A chain of insulin as disclosed by UniProt, Weiss et al., Ciszak et al., Weiss et al. 2, Slieker et al., Kashida, et al., and Reddy et al. with the substitutions of Weiss et al. and Chu et al. to arrive at the claimed invention.
A person of ordinary skill in the art would be motivated to make these substitutions to create a variant with greater stability and greater lipogenicity.
A person of ordinary skill in the art would have a reasonable expectation of success because both substitutions result in an active variant as disclosed by Weiss et al. Weiss et al., page 40020, Table II) and Chu et al. (Chu et al. page 574, Table I).
Consequently, claim 3 is obvious over Uniprot in view of Weiss et al., Ciszak et al., Weiss et al. 2, Slieker et al., Kashida, et al., and Reddy et al. as applied to claim 1 above, further in view of Chu et al. and rejected.
Claim 4 is rejected under 35 U.S.C. 103 as being unpatentable over UniProt Entry P01308 (https://www.uniprot.org/uniprotkb/P01308/entry, accessed 3/12/2026, published 11/1/1988) over Weiss et al. (Weiss, et al. Journal of Biological Chemistry 276.43: 40018-40024. (2001)), Ciszak et al. (Ciszak, et al. Structure 3.6: 615-622 (1995)), Weiss et al. 2 US20180057559, published 3/1/2018, Slieker et al. (Slieker, et al. Diabetologia 40.Suppl 2: S54-S61 (1997)), Kashida, et al. (Kashida et al., Organic & Biomolecular Chemistry 6.16: 2892-2899 (2008)), and Reddy et al. (Reddy, et al., International Journal of Peptides 2012.1: 323907 (2012)) as applied to claim 1 above, and further in view of Barnett et al. (Barnett, et al. The Lancet 349.9044: 47-51 (1997)).
Regarding claim 4, claim 1 is obvious as described above. Claim 4 further recites the case wherein the A chain contains a substitution at position A21. Barnett et al. discloses: “Hoechst modified di-arginyl insulin, an intermediate in the bioconversion of proinsulin to insulin, and substituted asparagine with glycine at position A21 to improve stability.” (Barnett et al., page 48, col. 2, para. 1)
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to modify the A Chain of UniProt, Weiss et al., Ciszak et al., Weiss et al. 2, Slieker et al., Kashida, et al., and Reddy et al. with the modification of Barnett et al. to arrive at the claimed invention.
A person of ordinary skill in the art would be motivated to make the A chain more stable as disclosed by Barnett et al. and have a reasonable expectation of success because Barnett reports that this modification has already been tested. (Barnett et al., page 48, col. 2, para. 1).
Consequently, claim 4 is obvious over Uniprot in view of Weiss et al., Ciszak et al., Weiss et al. 2, Slieker et al., Kashida, et al., and Reddy et al. as applied to claim 1 above, further in view of Barnett et al. and rejected.
Free of the Prior Art
Claim 9 is free of the prior art. While L-DOPA at position B26 is not specifically disclosed, Žáková et al. (Žáková, et al. Biological Crystallography 70.10: 2765-2774 (2014)) discloses that PheB6 results in an inactive form of insulin (Žáková, et al., page 2769, Table 2). Phenylalanine is a very close structural analog to L-DOPA and consequently, a person of ordinary skill in the art would be motivated to not make such a substitution based off the results of Žáková. Therefore, the insulin analog of claim 9 is novel and nonobvious.
Conclusion
No claim is allowed.
Claims 3 is objected to.
Claims 1-15 are rejected.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to David Paul Bowles whose telephone number is (571)272-0919. The examiner can normally be reached Monday-Friday 8:30-5:00.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Lianko Garyu can be reached on (571) 270-7367. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/DAVID PAUL BOWLES/ Examiner, Art Unit 1654
/LIANKO G GARYU/ Supervisory Patent Examiner, Art Unit 1654