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 .
Continued Examination Under 37 CFR 1.114
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 10/06/2025 has been entered.
Priority
This application is a CIP of 17/215,476 filed 03/29/2021. Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 10/06/2025 complies with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Status of the Claims
Applicant’s amendment filed on 10/06/2025 is acknowledged.
Claims 1, 6 and 11-27 are pending. Claims 25 and 26 are amended. Claims 2-5 and 7-10 are cancelled. Claim 27 is new. Claims 14-17 were withdrawn.
Claims 1, 6, 11-13 and 18-27 are under examination (claims set filed 10/06/2025).
Withdrawal of Rejections
The response and amendment filed on 10/06/2025 are acknowledged. The Declaration under 37 C.F.R. 1.132 of Dr. Koji Sode is acknowledged. All of the amendment and arguments have been thoroughly reviewed and considered.
For the purposes of clarity of the record, the reasons for the Examiner's withdrawal and/or maintaining if applicable, of the substantive or essential claim rejections are detailed directly below and/or in the Examiner's response to arguments section.
The previous claims 25 and 26 rejection under 35 U.S.C. 112(b) has been withdrawn necessitated by amendment of claims 25 and 26.
Amendment of Claims (1.121)
“Amendments to a claim must be made by rewriting the entire claim with all changes (e.g., additions and deletions) as indicated in this subsection, except when the claim is being canceled. Each amendment document that includes a change to an existing claim, cancellation of an existing claim or addition of a new claim, must include a complete listing of all claims ever presented, including the text of all pending and withdrawn claims, in the application. The claim listing, including the text of the claims, in the amendment document will serve to replace all prior versions of the claims, in the application. In the claim listing, the status of every claim must be indicated after its claim number by using one of the following identifiers in a parenthetical expression: (Original), (Currently amended), (Canceled), (Withdrawn), (Previously presented), (New), and (Not entered).” (MPEP 1.121).
The Applicant has not amended claim 6 but has indicated the status of the claim as “Currently amended”. The amendment: “a second
The claim 6 is not-compliant, however, since this may be inadvertent and in the interest of compact prosecution the Examiner will proceed with the examination of the application.
Maintained/Modified Rejections
Claim Rejections - 35 USC § 112
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.
Claims 1, 6, 11-13, 18, 19, 21 and 23-26 are 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claims 1 recites five alternative combinations of cysteine residues introduced into the catalytic subunit and the electron transfer subunit of mutant FAD-dependent glucose dehydrogenase (FAD-GDH). Only two of those combinations are mentioned in the specification, i.e.: “combination of the proline at position 205 of the catalytic subunit and the aspartic acid at position 383 of the electron transfer subunit, and the combination of the asparagine at position 215 of the catalytic subunit and the threonine at position 336 of electron transfer subunit.” (paragraph 0033). That corresponds to alternatives (a) and (c). However, alternative combination claimed in (b), (d) and (e) are not described.
The prior art of Yoshida (Yoshida et al. Acta Cryst., 2019, D75, 841-851 on record in IDS) teaches the X-ray structure of the FAD-GDH catalytic subunit complexed with a hitchhiker subunit (Abstract). The structure revealed a loop in the catalytic subunit containing cysteine cluster (Cys 212, Cys 213, Cys 218 and Cys 222) from which Cys 213 was shown to form disulfide bond with Cys 152 of the hitchhiker subunit (p. 844, right column, 1st and 4th paragraphs). Although the other Cys residues of the loop were located at the interface between subunits, they did not form the disulfide bonds. The prior art of Yoshida indicates unpredictability of disulfide bond formation between specific residues on the interface of interacting proteins in the absence of the crystal structure of the complex of two proteins. It is noted that the structure of the electron transfer subunit and the whole FAD-GDH was not determined before the effective filing date of the claimed invention and therefore the prior art could not provide guidance for the selection of residues for disulfide bonds between catalytic and electron transfer subunits.
Hirakawa (Hirakawa et al. Biotech. and Bioengin., 2013, 110, 1858-1864 on record in IDS) teaches introduction of intersubunit disulfide bonds into a multienzyme complex of proliferating cell nuclear antigen (PCNA), which is a heterotrimer consisting of PCNA1, PCNA2 and PCNA3 (Abstract). The sites for cysteine introduction were selected based on the structure to identify residues within 5.5 Å or less distance from each other since 5.5 Å was suggested to be a favorable distance between alpha-carbons in disulfide bond (p. 1861, left column, 3rd paragraph). Therefore, the prior art of Yoshida and Hirakawa indicates the importance of the distance between cysteine residues for the formation of the disulfide bond and the necessity to determine that distance based on the crystal structure of the complex of proteins participating in the disulfide bond formation. It is noted that the specification describes residues of the catalytic subunit, 205, 208, 215, 224 and 235, on the interface with the electron transfer subunit (paragraph 0018) and residues of the electron transfer subunit, 385 and 391, on the interface with the catalytic subunit (paragraph 0031). The specification indicates that the residues of the combinations (a) and (c) have “a distance of about 5 Å from each other in the spatial structure of FAD-GDH and are capable of more efficient formation of a disulfide bond” (paragraph 0033). However, the specification does not provide teaching on the distance between residues in combinations (b), (d) and (e) and does not provide any guidance for the importance of the distance between residues necessary to achieve disulfide bond formation for any combinations. The specification does not provide reasonable guidance in the bond formation.
Therefore, the recitations of combinations (b), (d) and (e) are not supported by the specification and hence one of ordinary skill in the art would not conclude that the applicant would have been in possession of the subject matter of claim 1 at the time of filing application.
Claims 6, 11-13, 18, 19, 21 and 23-26, dependent on claim 1, do not resolve the issue mentioned above and are rejected. Claims 20 and 22 recite the combinations supported by the specification.
Response to Arguments
Applicant's arguments filed 10/06/2025 and Declaration under 37 C.F.R. 1.132 of Dr. Koji Sode have been fully considered but they are not persuasive.
Applicant argues (addressing pages 8-10 of the Remarks) that the specification expressly discloses all five claimed positions in SEQ ID NO:3 as exemplary cites at which a cysteine residue can
be introduced in paragraph 0018, all claimed positions in SEQ ID NO:4 in paragraph 0031 and identifies two of the claimed combinations as “examples of preferred combination” in paragraph 0033. Applicant provided the Declaration of Dr. Sode and article of Ikuda-Shimazaki (Sode et al.) referring specifically to Table 1 in the article showing functional activities of the combinations corresponding to claimed alternative combinations in claim 1. Applicant argues that: “These exhibits unequivocally demonstrate that the inventors were in possession of all five combinations in claim 1 as of the filing date including combinations (b), (d), and (e) for which the Examiner alleged a lack of description” and that the fact that the inventors had actually constructed and confirmed the function of these mutants is the strongest possible evidence of possession.
These arguments are not persuasive because: (i) There is no doubt that the inventors are currently in possession of the claimed combination mutants in claim 1, however, the article was published on December 6, 2022 that is after the filing date and the effective filing date of instant application (03/29/2021).
The courts have described the essential question to be addressed in a description requirement issue in a variety of ways. An objective standard for determining compliance with the written description requirement is, "does the description clearly allow persons of ordinary skill in the art to recognize that he or she invented what is claimed." In re Gosteli, 872 F.2d 1008, 1012, 10 USPQ2d 1614, 1618 (Fed. Cir. 1989). Under Vas-Cath, Inc. v. Mahurkar, 935 F.2d 1555, 1563-64, 19 USPQ2d 1111, 1117 (Fed. Cir. 1991), to satisfy the written description requirement, an applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, the inventor was in possession of the invention, and that the invention, in that context, is whatever is now claimed. The test for sufficiency of support in a parent application is whether the disclosure of the application relied upon "reasonably conveys to the artisan that the inventor had possession at that time of the later claimed subject matter." Ralston Purina Co. v. Far-Mar-Co., Inc., 772 F.2d 1570, 1575, 227 USPQ 177, 179 (Fed. Cir. 1985) (quoting In re Kaslow, 707 F.2d 1366, 1375, 217 USPQ 1089, 1096 (Fed. Cir. 1983)).
Hence the article cannot demonstrate that the inventors were in possession of all five combinations in claim 1 as of the filing date and (ii) while the claimed positions for the introduction of cysteine residues on catalytic and electron transfer subunits are described, only two combinations of positions (a) and (c) of claim 1 are described in the specification. It is clear from the prior art that the distance between residues is important for the disulfide bond formation. The specification does not provide guidance on the importance of distance between possible interacting residues and does not discuss the distance between residues of the catalytic and electron transfer subunit which is a critical aspect for selection of the combinations of residues. One of ordinary skill in the art would conclude that it was not known at the time of filing the application whether the cysteine residues introduced in the positions cited in combinations (b), (d) and (e) will form the disulfide bonds and it would not be possible to predict the claimed combination in the absence of the structural information which was not available at the filing time.
In response to Applicant’s argument that the written description is separate from the enablement requirement and that additional experimentation is not a relevant basis for a written description rejection, this argument is not persuasive because the previous written description rejection and the current rejection is not based on the additional experimentation but on the introduction of new matter lacking the description and indicating that the Applicant was not in possession of the subject matter of claim 1 at the time of filing application.
Applicant mentions that the newly introduced claim 27 adopts the language disclosed in the specification and satisfies the written description. The Examiner agrees with that statement and claim 27 is not included in the 112a written description rejection.
Claim Rejections - 35 USC § 112
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.
Claims 1, 6, 11-13, 18, 19, 21 and 23-26 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre- AIA ), first paragraph, because the specification, while being enabling for: (i) a mutant FAD-GDH comprising the catalytic subunit and the electron transfer subunit bound to each other through a disulfide bond between introduced cysteine residues wherein the cysteine residues are introduced in the catalytic subunit at position 205 of SEQ ID NO:3 and in the electron transfer subunit at position 383 of SEQ ID NO:4 and (ii) mutant FAD-GDH comprising the catalytic subunit and the electron transfer subunit bound to each other through a disulfide bond between introduced cysteine residues wherein the cysteine residues are introduced in the catalytic subunit at position 215 of SEQ ID NO:3 and in the electron transfer subunit at position 336 of SEQ ID NO:4; the specification does not reasonably provide enablement for a mutant FAD-GDH comprising the catalytic subunit and the electron transfer subunit bound to each other through a disulfide bond between introduced cysteine residues wherein the combinations of introduced cysteine residues are:
cysteine residue introduced in the catalytic subunit at position 208 of SEQ ID NO:3 and in the electron transfer subunit at position 385 of SEQ ID NO:4 (b);
cysteine residue introduced in the catalytic subunit at position 224 of SEQ ID NO:3 and in the electron transfer subunit at position 336 of SEQ ID NO:4 (d); and
cysteine residue introduced in the catalytic subunit at position 235 of SEQ ID NO:3 and in the electron transfer subunit at position 391 of SEQ ID NO:4 (e).
Claim 27 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre- AIA ), first paragraph, because the specification, while being enabling for a mutant FAD-GDH comprising the catalytic subunit and the electron transfer subunit bound to each other through a disulfide bond between introduced cysteine residues wherein the cysteine residues are at the position 208 of the catalytic subunit and position 385 of the electron transfer subunit or at the position 215 of the catalytic subunit and position 336 of the electron transfer subunit, does not reasonably provide enablement for a mutant FAD-GDH comprising the catalytic subunit and the electron transfer subunit bound to each through a disulfide bond between introduced cysteine residues at any other possible combinations of 5 recited positions for the catalytic subunit and 4 recited positions for the electron transfer subunit (total of 18 combination from 20 combinations without two combinations described in the specification).
The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the invention commensurate in scope with these claims.
Claim 1 is directed to a mutant FAD-GDH comprising the catalytic subunit and the electron transfer subunit bound to each other through a disulfide bond between cysteine residues introduced in the catalytic and electron transfer subunits wherein the five specific combinations of the introduced cysteine residues are claimed as alternatives. Claim 6 is drawn to introduction of a second cysteine residue in the electron transfer subunit of mutant FAD-GDH of claim 1 and a cysteine residue introduced in the hitchhiker subunit wherein the combination of introduced cysteine residues are: at position 345 of SEQ ID NO:4 and at position 154 of SEQ ID NO:2 and at position 349 of SEQ ID NO:4 and at position 155 of SEQ ID NO: 2. Claim 27 is directed to a mutant FAD-GDH comprising the catalytic subunit and the electron transfer subunit bound to each other through a disulfide bond between cysteine residues introduced in the catalytic and electron transfer subunits at positions selected from 5 positions in the catalytic subunit and 4 positions in the electron transfer subunit and thus comprising 20 alternative pair combinations.
The prior art of Yoshida describes that FAD-GDH is composed of catalytic subunit (α subunit), electron transfer subunit (β subunit) and hitchhiker subunit (γ subunit) (p. 842, left column, 3rd paragraph). Yoshida teaches the X-ray structure of the FAD-GDH catalytic subunit complexed with a hitchhiker subunit (Title). Yoshida discloses connection of these molecules through disulfide bond formed at the interface between cysteine residues of two subunits (p. 845, left column) that is important for maintaining thermal stability of FAD-GDH dimer (p. 846, right column, 1st paragraph). However, the structure of the electron transfer subunit and the whole FAD-GDH was not determined before the effective filing date of the claimed invention. Hirakawa teaches introduction of intersubunit disulfide bonds into a multienzyme complex of proliferating cell nuclear antigen (PCNA), which is a heterotrimer consisting of PCNA1, PCNA2 and PCNA3 (Abstract). Hirakawa mentions that disulfide bonds were introduced by cysteine substitution at the sites neighboring the interface for heterotrimerization and that resulted in stabilized multienzyme complex (p. 1859, right column, 2nd paragraph). The sites for cysteine introduction were selected based on the structure to identify residues within 5.5 Å or less distance from each other since 5.5 Å was suggested to be a favorable distance between alpha-carbons in disulfide bond (p. 1861, left column, 3rd paragraph).
Thus, the prior art does not provide information about disulfide bonds between the catalytic subunit and the electron transfer subunit and between the electron transfer subunit and the hitchhiker subunit. The prior art points to necessity to know the spatial position of candidate residues in FAD-GDH structure for substitution with cysteines or interaction to achieve formation of disulfide bonds.
The specification describes residues in the region of the catalytic subunit located on the interface with the electron transfer subunit which can be used for introduction of cysteine residues, i.e. residues at positions 205, 208, 215, 224, and 235 (paragraph 0018). The specification describes residues in the region of the electron transfer subunit located on the interface with the catalytic subunit which can be used for introduction of cysteine residues, i.e. residues at positions 336, 383, 385 and 391 (paragraph 0031) and residues located on the interface with the hitchhiker subunit which can be used for introduction of cysteine residues, i.e. residues at positions 345, 346 and 349 (paragraph 0035). The specification describes residues in the region of the hitchhiker subunit located on the interface with the electron transfer subunit which can be used for introduction of cysteine residues, i.e. residues at positions 145, 154 and 155 (paragraph 0057). The specification mentions that residues were selected based on the crystal structure of FAD-GDH (paragraph 0005). Even though the specification mentions all positions in claims 1, 6 and 27, only two of five combinations of position for cysteine residues introduction into the catalytic and the electron transfer subunit are described in the specification: “combination of the proline at position 205 of the catalytic subunit and the aspartic acid at position 383 of the electron transfer subunit, and the combination of the asparagine at position 215 of the catalytic subunit and the threonine at position 336 of electron transfer subunit. These combinations of residues are combinations of residues having a distance of about 5 Å from each other in the spatial structure of FAD-GDH, and capable of more efficient formation of a disulfide bond” (paragraph 0033). Other combinations (alternatives (b), (d) and (e) in claim 1 and 18 other possible combinations in claim 27) are not mentioned. The specification provides working examples for the mutant FAD-GDH with cysteine introduced in the position 205 of the catalytic subunit and position 383 of the electron transfer subunit which is an alternative (a) in claim 1 (Mutant 3, paragraph 0095) and mutant FAD-GDH with the second cysteine introduced into position 345 of the electron transfer subunit and cysteine introduced in position 154 of the hitchhiker subunit (Mutant 4, paragraph 0095) and mutant FAD-GDH with the second cysteine introduced into position 349 of the electron transfer subunit and cysteine introduced in position 155 of the hitchhiker subunit (Mutant 5, paragraph 0095) which are claimed in claim 6 when using alternative (a) of claim 1. Example 1 describes increase in stability of Mutants 3-5 indicating disulfide bond formation (Fig. 1, Fig. 4, paragraph 0098, 0101). No working examples are provided for alternative combinations of positions for cysteine residues introduction (b), (c), (d) and (e) of claim 1 and possible alternative combinations in claim 27.
Although no working example is provided for combination of cysteine residue introduced at position 215 of the catalytic subunit and at position 336 of the electron transfer subunit, since the specification indicates these residues to be located at a distance of about 5 Å from each other (paragraph 0033) and Hirakawa teaches that 5.5 Å is a favorable distance between alpha-carbons in disulfide bond (p. 1861, left column, 3rd paragraph), the combination of cysteine residues introduced into positions 215 and 336 of the catalytic and electron transfer subunits, respectively, is considered enabled.
Thus, based on the unpredictability taught by the prior art and absence of working examples and directions provided by inventors, one of ordinary skill in the art would have to undergo undue experimentation to practice the full scope of the invention. Therefore, claims 1 and 6 are rejected under 35 U.S.C. 112(a) for failing to disclose sufficient supporting information to enable a person of skill in the art to make and use mutant FAD-GDH with combinations of cysteine residues introduced at position 208 of SEQ ID NO:3 and at position 385 of SEQ ID NO:4, at position 224 of SEQ ID NO:3 and at position 336 of SEQ ID NO:4 and at position 235 of SEQ ID NO:3 and at position 391 of SEQ ID NO:4. Claims 11-13, 18, 19, 21 and 23-26 do not resolve the issue mentioned above and are rejected.
Claims 27 is rejected under 35 U.S.C. 112(a) for failing to disclose sufficient supporting information to enable a person of skill in the art to make and use mutant FAD-GDH with combinations of cysteine residues introduced at position 205 of SEQ ID NO:3 and at any of positions 336, 385 and 391 of SEQ ID NO:4; cysteine residues introduced at position 215 of SEQ ID NO:3 and at any of positions 383, 385 and 391 of SEQ ID NO:4; cysteine residues introduced at position 208 of SEQ ID NO:3 and at any of four recited positions of SEQ ID NO:4; cysteine residues introduced at position 224 of SEQ ID NO:3 and at any of four recited positions of SEQ ID NO:4; and cysteine residues introduced at position 235 of SEQ ID NO:3 and at any of four recited positions of SEQ ID NO:4.
Response to Arguments
Applicant's arguments and Declaration under 37 C.F.R. 1.132 of Dr. Koji Sode filed 10/06/2025 have been fully considered but they are not persuasive.
Applicant argues (addressing pages 10-11 of the Remarks) that Declaration of Dr. Sode and the article by Dr. Sode et al. indicates that five claimed combinations of cysteine introduction sites have been created and demonstrated to be viable enzymes. Regarding new claim 27, Applicant argues that the article demonstrated 5 of possible 20 variants of claim 27 providing sufficient basis to enable the full scope of claim 27 with merely routine experimentation. Applicant further argues that the Declaration and article demonstrate that the invention is based on rational design strategy and the candidate pairs for disulfide bond formation were selected based on the structural information. Therefore, a POSITA, following the rational design strategy disclosed in the specification and in the article could create and test other combinations within the scope of new claim 27 with no more than mere routine experimentation.
These arguments are not persuasive because:
As described above, the article of Dr. Sode et al. was published after the filing date and
the effective filing date of instant application. MPEP 2164.05(a) states: “The state of the art existing at the filing date of the application is used to determine whether a particular disclosure is enabling as of the filing date. Chiron Corp. v. Genentech Inc., 363 F.3d 1247, 1254, 70 USPQ2d 1321, 1325-26 (Fed. Cir. 2004) (Stating that "a patent document cannot enable technology that arises after the date of application."). Information published for the first time after the filing date generally cannot be used to show what was known at the time of filing. In re Gunn, 537 F.2d 1123, 1128, 190 USPQ 402,405-06 (CCPA 1976); In re Budnick, 537 F.2d 535, 538, 190 USPQ 422, 424 (CCPA 1976)”. Therefore, the arguments based on the article published after the filing date are not persuasive for the enablement rejection.
As mentioned in the specification and the article the selection of the pairs of positions
for introduction of cysteine residues is based on the structural information because residues need to be at a close distance (5 Å) from each other. Only two preferred combinations are described in the specification, i.e. position 205 of the catalytic subunit and position 383 of the electron transfer subunit and position 215 of the catalytic subunit and position 336 of the electron transfer subunit, and these positions are described to have distance of about 5 Å from each other in the spatial stricture of FAD-GDH (paragraph 0033). The first combination is supported by the working example (paragraph 0095). The other combinations, i.e. alternatives (b), (d) and (e) in claim 1 and 18 out of 20 possible combinations in claim 27 are not suggested or predicted in the specification and without available structural information would require undue experimentation.
Please note that claim 22 is not currently rejected under 112a enablement requirement
since the specification teaches these residues to be located at a distance of about 5 Å from each other based on the structural information (paragraph 0033) which is a favorable distance for disulfide bond formation based on Hirakawa teaching (p. 1861, left column, 3rd paragraph), and therefore the combination of cysteine residues introduced into positions 215 of the catalytic subunit and 336 of the electron transfer subunit is predicted to be enabled.
Allowable Subject Matter
Claims 20 and 22 are objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims. Claim 20 recites mutant FAD-GDH with cysteine residue introduced at position 205 of SEQ ID NO:3 and a cysteine residue introduced at position 383 of SEQ ID NO: 4 which is free of prior art. Claim 22 recites mutant FAD-GDH with cysteine residue introduced at position 215 of SEQ ID NO:3 and a cysteine residue introduced at position 336 of SEQ ID NO: 4 which is free of prior art.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to LIOUBOV G KOROTCHKINA whose telephone number is (571)270-0911. The examiner can normally be reached Monday-Friday: 8:00-5:30.
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/L.G.K./Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653