DETAILED ACTION
1. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
2. Applicant’s reply filed on 6/2/2026 is acknowledged. New claim 35 has been added. Claims 1-4 and 9-35 are pending. Claims 5-8 are canceled. Claims 15-18 and 21-30 are withdrawn from consideration. Claims 32-34 have been amended.
3. Claims 1-4, 9-14, 19-20 and 31-35 are under examination.
Rejections Maintained
Claim Rejections - 35 USC § 112
4. 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.
5. Claims 1-4, 9-14, 19-20, 31 and 32 remain 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 an immune effector cell comprising a nucleotide sequence encoding a polypeptide comprising the amino acid sequence selected from the group consisting of SEQ ID NOs: 74, 82, 92, 98, 100 and 104 (corresponding to Mut 5, 9, 14, 17, 18 and 20 disclosed in the specification), and a nucleotide sequence encoding a cell-targeting molecule, does not reasonably provide enablement for any mammalian cell comprising a nucleotide sequence encoding a polypeptide comprising an amino acid sequence having at least 95% or 97% sequence identity to at least one sequence set forth in SEQ ID NOs: 74, 82, 92, 98, 100 and 104. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to use the invention commensurate in scope with these claims.
Note: The rejection of claim 34 is withdrawn in view of applicant’s amendment.
Factors to be considered in determining whether a disclosure meets the enablement requirement of 35 USC 112, first paragraph, have been described by the court in In re Wands, 8 USPQ2d 1400 (CA FC 1988). Wands states at page 1404,
''Factors to be considered in determining whether a disclosure would
require undue experimentation have been summarized by the board in Ex
parte Forman. They include (1) the quantity of experimentation necessary,
(2) the amount of direction or guidance presented, (3) the presence or
absence of working examples, (4) the nature of the invention, (5) the state
of the prior art, (6) the relative skill of those in the art, (7) the predictability
or unpredictability of the art, and (8) the breadth of the claims.''
The nature of the invention
Claims 1-4, 9-14, 19-20 and 31 are drawn to a mammalian cell comprising a nucleotide sequence encoding a polypeptide comprising an amino acid sequence having at least 95% sequence identity to at least one sequence set forth in SEQ ID NOs: 74, 82, 92, 98, 100 and 104.
Claim 32 further limit claim 1, wherein the polypeptide comprising an amino acid sequence having at least 97% sequence identity to at least one sequence set forth in SEQ ID NOs: 74, 82, 92, 98, 100 and 104.
The nature of the claims is protein and cell engineering.
The invention is in a class of invention, which the CAFC has characterized as ''the unpredictable arts such as chemistry and biology.'' Mycogen Plant Sci., Inc. v. Monsanto Co., 243 F.3d 1316, 1330 (Fed. Cir. 2001).
The breadth of the claims
The claims recite a polypeptide comprising an amino acid sequence having at least 95% or 97% sequence identity to at least one sequence set forth in SEQ ID NOs: 74, 82, 92, 98, 100 and 104. Each of SEQ ID NOs: 74, 82, 92, 98, 100 and 104 is referred to here as the reference polypeptide.
The claims encompass a genus of variants, wherein the variants share 95% or 97% sequence homology with the reference polypeptide. Up to 5% or 3% of the amino acids in the reference polypeptide may be changed by substitution, addition, deletion or combination thereof at any positions. Note that the claims do not require the variants to have any function.
Quantity of experimentation
The quantity of experimentation in this area is extremely large in view of the breath of claims and unpredictability of protein/cell engineering. The function of each variant must be determined in order to know how to use a mammalian cell comprising the variant.
Working examples
The specification discloses that the function of p13 has not previously been characterized at the amino acid level. To determine which amino acids and domains are critical for fusion, an alanine scan of p13 was performed. The p13 protein was mutated with sequential stretches of 4 alanine residues, beginning at amino acid #1 and proceeding to amino acid #113, excluding the transmembrane domain, for a total of 23 unique proteins (SEQ ID NOs:67-111 and 151). Three mutations ablated fusion: (1) Mut 1, comprising mutations within the consensus myristoylation site (MYR: amino acids #1-#2); and (2) Mut 2 and Mut 3, comprising mutations in the critical N-terminus of p13 (FIG. 5). Six mutants, Mut 5, 9, 14, 17, 18, and 20 (which have SEQ ID NOs: 74, 82, 92, 98, 100 and 104, respectively), showed augmented fusion compared to p13 (WT) when expressed in CD19-targeting human T-cells targeting CD19+ human B-cells (FIG. 5). Two of these mutants comprise mutations in domains important for p13 function, the polybasic (PB) domain and the amphipathic helix (AH) (FIG. 5). Taken together, these data identified regions of p13 necessary for fusion, as well as alanine mutations capable of promoting fusion (e.g., between human T-cells and human B-cells) ([00448]). The specification further disclose testing combinations of two, three, four or all five mutations, six combinations, Mu5 5/17, Mut 5/18, Mut 5/20, Mut 9/17, Mut17/20, and Mut 5/17/20 showed significant augmented fusion compared to p13 (WT) (Example 2, and Fig. 9).
Applicant’s Figs. 5 and 9 (reproduced below) provide evidence of unpredictability of the effects of substitutions on the fusogenic function of a fusogen.
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Furthermore, the disclosure limited to alanine scanning of fusogen p13 is not commensurate in scope with the claims which allows 5% or 3% change in any one of SEQ ID NOs: 74, 82, 92, 98, 100 or 104, such change includes substitution with any amino acids, deletion, addition and/or any combination thereof. The specification does not disclose the function of all the variants. Without knowing the function of the variants, one of ordinary skill in the art would not know how to use the invention as broadly claimed.
Regarding the new limitation “wherein the amino acid sequence differs only by conservative amino acid substitutions” recited in claim 32, the specification does not disclose which amino acid residues can be changed by conservative amino acid substitution without affecting the function of the reference polypeptide.
Guidance in the specification
The specification does not provide guidance on how to use the full scope of the invention.
While one of ordinary skill in the art know how to make all the variants and mammalian cells comprising each of the variants, the specification does not teach how to use the mammalian cells comprising each of the variants. The variants encompass those with no fusogenic function, and those whose functions remain to be determined.
The state of the art
Thalmann et al (Virology 2010, 402:26-40, PTO-892 dated 9/23/2024) teaches a novel fusion associated small transmembrane (FAST protein) identified from Broome virus which is responsible for syncytium formation in BroV-infected cells and comprises an amino acid sequence that is 100% identical to instant SEQ ID NO:3 (see sequence alignment below).
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The prior art does not teach any variants of instant SEQ ID NOs: 74, 82, 92, 98, 100 and 104, which are not 100% identical to instant SEQ ID NO:3.
The unpredictability of the art
Protein chemistry is probably one of the most unpredictable areas of biotechnology. It is known in the art that the relationship between the amino acid sequence of a protein (polypeptide) and its tertiary structure (i.e. its binding activity) are not well understood and are not predictable. There is no recognition in the art that sequence with identity predicts biological function. It is known in the art that even single amino acid changes or differences in a protein's amino acid sequence can have dramatic effects on the protein's function. Duncan et al. (Annu Rev Virol, 2019, 6:341-63, PTO-892 dated 9/23/2024) teaches that the rudimentary FAST protein ectodomains are all small, amphiphilic peptides. These domains in p10, p14, and p15 are sensitive to substitution and in liposome fusion assays induce robust lipid mixing, two characteristics of enveloped virus FPs. They do so, however, using remarkably diverse structures. While structurally distinct, these unusual viral FPs all appear to be dynamic structures, and all three contain a pair of apolar aromatic and beta-branched amino acids (e.g., Phe and Val) (page 352, last para). Proline residues are tolerant of substitution, but multiple substitutions that disrupt the helix structure ablate p15-induced syncytiogenesis (page 13, para 3). Despite the dramatic differences in their structures, the p15 ectodomain can be functionally replaced by that of p14, but the converse substitution is nonfusogenic, evidence that specific combinations of different ecto-, endo-, and TM domain motifs are needed to generate a functional FAST protein (page 13, para 13).
Regarding conservative amino acid substitutions recited in claim 32, it is known in the art that even single amino acid changes or differences in a protein's amino acid sequence can have dramatic effects on the protein's function. For example, conservative replacement of a single “lysine” reside at position 118 of acidic fibroblast growth factor by “glutamic acid” led to the substantial loss of heparin binding, receptor binding and biological activity of the protein (Burgess et al., J of Cell Bio. 111:2129-2138, 1990). Further, Leninger et al. (Elife. 2019;8:e48909. Published 2019 Oct 22) teaches: “a single conservative mutation introduced into an SMR dimer is sufficient to change the resting conformation and function in bacteria…changing a single amino acid (the building blocks that make up proteins) in one of the two subunits to make them minimally different from each other, dramatically modified the transporter’s structure and function”(Abstract).
Level of skill in the art
The level of skill in the art is deemed to be high.
Conclusion
Thus given the unpredictability of the art, the unpredictability of the function of the broadly encompassed variants, the lack of correlation between a function and a structure of the variants, the presence of working examples and guidance which are not commensurate in scope of the claims, balanced only against the high skill level in the art, it is the position of the examiner that it would require undue experimentation for one of skill in the art to perform the claimed invention.
Applicant’s Arguments
The response states that the Office Action improperly reads a functional "fusogenic activity" limitation into claim 1. Claim 1 does not require any particular level of fusogenic activity, nor does claim 1 require that every polypeptide encompassed by the recited sequence identity limitation necessarily mediate membrane fusion. The Office Action further conflates enablement of biological function with enablement of
structurally defined compositions. Claims directed to structurally defined polypeptides and cells expressing such polypeptides are enabled where the specification teaches how to make and express the claimed molecules, even if particular embodiments exhibit varying biological activity. The pending claims are not method-of-use claims and do not require any minimum level of fusogenic activity. Moreover, the pending amended claims are structurally constrained and do not encompass unrestricted sequence variation. In particular, amended claim 32 limits permissible sequence variation to conservative amino acid substitutions and no longer encompasses unrestricted insertions, deletions, or arbitrary amino acid substitutions across the recited sequences.
Even assuming that fusogenic activity were required for the pending claims, which it is not, the specification provides extensive guidance enabling a POSITA to identify and evaluate functional variants without undue experimentation. The specification discloses numerous working examples, specific substitutions, sequence variants, structure-function relationships, and experimental assays for evaluating fusion activity. The experimental results cited by the Office, including FIGs. 5 and 9, do not demonstrate lack of enablement. The alanine scanning data provide a detailed structure-function map identifying regions important for fusion activity, regions that are tolerant of substitution, and variants exhibiting enhanced activity. Such guidance substantially reduces the amount of experimentation required.
Practicing the claimed invention would not require "extremely large" experimentation. The claims are limited to six specifically disclosed and experimentally characterized reference sequences and limited by defined sequence identity thresholds. The disclosed polypeptides are relatively small, and the specification identifies regions that tolerate modification versus regions important for activity, therefore substantially reducing the amount of experimentation required.
First, the quantity of experimentation required to practice the claimed invention would have been limited and routine. Routine substitution mutagenesis, recombinant expression, and co-culture fusion assays were well established in the art as of the filing date. Second, the specification provides substantial guidance and direction regarding the claimed subject matter. The disclosure identifies structurally conserved regions, provides experimentally validated fusogen sequences, and teaches methods for evaluating membrane fusion activity. The specification does not require a POSITA to engage in undue trial-and-error experimentation in order to identify operative embodiments. Third, the disclosure contains representative working examples demonstrating successful construction and use of fusogens in mammalian cells. These examples provide concrete guidance regarding construct design, expression systems, and functional characterization assays relevant to the claimed subject matter.
Fourth, while the Applicant acknowledges that protein engineering may involve some
degree of biological variability, the claimed subject matter is not an unpredictable genus. The claims are structurally constrained by specific sequence identity thresholds and expressly recited sequence limitations. The specification further provides experimentally validated examples and screening methodologies sufficient to permit a POSITA to identify functional variants without undue experimentation.
Response to Arguments
Applicant’s arguments have been carefully considered but are not persuasive.
In the previous office action mailed on 03/02/2026, the examiner stated “The claims encompass a genus of variants of a reference polypeptide, wherein the variants share 95% or 97% sequence homology with the reference polypeptide. Up to 5% or 3% of the amino acids in the reference polypeptide may be changed by substitution, addition, deletion or combination thereof at any positions. Note that the claims do not require the variants to have any function.” (emphasis added) (page 5 of the office action, under subheading The breadth of the claims). The function of the broadly encompassed variants is not disclosed in the instant specification. Because neither the specification nor the prior art discloses the function of the broadly encompassed variants, one of ordinary skill in the art would not know how to use mammalian cells comprising these variants.
Applicant’s arguments regarding the breadth of the claims and quantity of experimentation are not persuasive. Each of SEQ ID NOs: 74, 82, 92, 98, 100 and 104 consists of 113 amino acids.
The limitation “at least 95% identical” allows a change of up to 5 amino acids. The number of ways to choose 5 positions from 113 is 113!/5!108!, which equals to 140,257,566 (i.e. there are 140,257,566 different sets of five positions that could be mutated). For each of the 5 chosen positions, there are 19 possible amino acid (anything except the original one). For 5 chosen positions, the number of substitutions is 195=2,476,099. The number of unique variants is 140,257,566 x 2,476,099, which equals to approximately 3.47x1014.
The limitation “at least 97% identical” allows a change of up to 3 amino acids. The number of ways to choose 3 positions from 113 is 113!/3!110!, which equals to 234,136 (i.e. there are 234,136 different sets of three positions that could be mutated). For each of the 3 chosen positions, there are 19 possible amino acid (anything except the original one). For 3 chosen positions, the number of substitutions is 193=6,859. The number of unique variants is 234,136 x 6,859, which equals to approximately 1.6x109.
Regarding the new limitation “conservative amino acid substitutions” recited in claim 32, many amino acids have roughly 2-3 conservative alternative. Using an average of 3 substitution per position, for a 113 amino acid protein with exactly 3 conservative substitution, three conservative choices at each position is 33 =27. The number of unique variants is 234,136 x 27 =6,321,672 (6.3 x106).
As one can see, the breadth of the claims is enormous. Therefore, the quantity of experimentation is extremely large. The function of each variant must be determined in order to know how to use a mammalian cell comprising the variant. Without knowing the function of each variant, one would not know how to use them.
New Grounds of Rejections
Claim Rejections - 35 USC § 112
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. Amended claims 34 and new claim 35 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.
“[T]he purpose of the written description requirement is to ‘ensure that the scope of the right to exclude, as set forth in the claims, does not overreach the scope of the inventor’s contribution to the field of art as described in the patent specification.’” Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1353-54 (Fed. Cir. 2010) (en banc) (quoting Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 920 (Fed. Cir. 2004)). To satisfy the written description requirement, the specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. Vas-Cath, Inc. v. Mahurkar, 935 F.2d 1555, 1562-63, 19 USPQ2d 1111 (Fed. Cir. 1991). See also MPEP 2163.04.
For a claim to a genus, a generic statement that defines a genus of substances by only their functional activity does not provide an adequate written description of the genus. Reagents of the University of California v. Eli Lilly, 43 USPQ2d 1398 (CAFC 1997). The recitation of a functional property alone, which must be shared by the members of the genus, is merely descriptive of what the members of the genus must be capable of doing, not of the substance and structure of the members.
“[A] sufficient description of a genus . . . requires the disclosure of either a representative number of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can ‘visualize or recognize’ the members of the genus.” Ariad, 598 F.3d at 1350 (quoting Eli Lilly, 119 F.3d at 1568-69). A “representative number of species” means that those species that are adequately described are representative of the entire genus. AbbVie Deutschland GMBH v. Janssen Biotech, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014). Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus to provide a "representative number” of species.
The “structural features common to the members of the genus” needed for one of skill in the art to ‘visualize or recognize’ the members of the genus takes into account the state of the art at the time of the invention.
Lastly, even if a selection procedure is disclosed that was, at the time of the invention, sufficient to enable the skilled artisan to identify members with the recited functional properties, the written description provision of 35 U.S.C § 112 is severable from its enablement provision.
Claim 35 recites “wherein the polypeptide comprises an amino acid sequence having at least 95% sequence identity to at least one sequence set forth in SEQ ID NOs: 74, 82, 92, 98, 100 and 10, and wherein the polypeptide induces fusion between the mammalian cell and a target cell in a co-culture assay (emphasis added). The limitation “95% sequence identity” allows a change of up to 5% of the amino acids in each SEQ ID NO. The specification does not disclose which 5% of the amino acids can be changed by substitution, addition, and/or deletion such that the resulting sequences still have the function (inducing fusion between the mammalian cell and a target cell in a co-culture assay). The claims are rejected because the specification does not adequately describe all the variants encompassed by the genus.
Regarding amended claim 34, the limitation “the amino acid sequence comprises MGSGPSNFVNKVDGASA (which is amino acid residues 1-17 of SEQ ID NO: 3) and TEDKLVNPFI (which is amino acid residues 104-113 of SEQ ID NO:3) is insufficient to provide the function (capable of inducing membrane fusion). This is evidenced by Mut13 and Mut 15. Both Mut13 (SEQ ID NO: 90) and Mut 15 (SEQ ID NO: 94) comprise amino acid residues 1-17 and 104-113 of SEQ ID NO: 3 ([00675]-[00676], [00681]-[00682]). However, they did not induce cell fusion (see Fig. 5) (i.e. they are not fusogenic).
The specification does not disclose which 5% of the amino acids in each of SEQ ID NOs: 74, 82, 92, 98, 100 and 104 can be changed by substitution, addition, and/or deletion such that the resulting sequences which comprise MGSGPSNFVNKVDGASA and TEDKLVNPFI still have the function of being capable of inducing membrane fusion. Therefore, the specification does not adequately describe all the species encompassed by the genus.
The specification discloses that the function of p13 has not previously been characterized at the amino acid level. To determine which amino acids and domains are critical for fusion, an alanine scan of p13 was performed. The p13 protein was mutated with sequential stretches of 4 alanine residues, beginning at amino acid #1 and proceeding to amino acid #113, excluding the transmembrane domain, for a total of 23 unique proteins (SEQ ID NOs:67-111 and 151). Three mutations ablated fusion: (1) Mut 1, comprising mutations within the consensus myristoylation site (MYR: amino acids #1-#2); and (2) Mut 2 and Mut 3, comprising mutations in the critical N-terminus of p13 (FIG. 5). Six mutants, Mut 5, 9, 14, 17, 18, and 20 (which have SEQ ID NOs: 74, 82, 92, 98, 100 and 104, respectively), showed augmented fusion compared to p13 (WT) when expressed in CD19-targeting human T-cells targeting CD19+ human B-cells (FIG. 5). Two of these mutants comprise mutations in domains important for p13 function, the polybasic (PB) domain and the amphipathic helix (AH) (FIG. 5). Taken together, these data identified regions of p13 necessary for fusion, as well as alanine mutations capable of promoting fusion (e.g., between human T-cells and human B-cells) ([00448]). The specification further disclose testing combinations of two, three, four or all five mutations, six combinations, Mu5 5/17, Mut 5/18, Mut 5/20, Mut 9/17, Mut17/20, and Mut 5/17/20 showed significant augmented fusion compared to p13 (WT) (Example 2, and Fig. 9). However the disclosure limited to alanine scanning of fusogen p13 is not commensurate in scope with the claims which allows 5% change at any positions including conservative substitution. Applicant’s Figs. 5 and 9 (see above) provide evidence of unpredictability of the effects of substitutions on the fusogenic function of a fusogen.
Protein chemistry is probably one of the most unpredictable areas of biotechnology. It is known in the art that the relationship between the amino acid sequence of a protein (polypeptide) and its tertiary structure (i.e. its binding activity) are not well understood and are not predictable). There is no recognition in the art that sequence with identity predicts biological function. It is known in the art that even single amino acid changes or differences in a protein's amino acid sequence can have dramatic effects on the protein's function. Duncan et al. (Annu Rev Virol, 2019, 6:341-63, form 892 dated 9/23/2024ezmartine) teaches that the rudimentary FAST protein ectodomains are all small, amphiphilic peptides. These domains in p10, p14, and p15 are sensitive to substitution and in liposome fusion assays induce robust lipid mixing, two characteristics of enveloped virus FPs. They do so, however, using remarkably diverse structures. While structurally distinct, these unusual viral FPs all appear to be dynamic structures, and all three contain a pair of apolar aromatic and beta-branched amino acids (e.g., Phe and Val) (page 352, last para). Proline residues are tolerant of substitution, but multiple substitutions that disrupt the helix structure ablate p15-induced syncytiogenesis (page 13, para 3). Despite the dramatic differences in their structures, the p15 ectodomain can be functionally replaced by that of p14, but the converse substitution is nonfusogenic, evidence that specific combinations of different ecto-, endo-, and TM domain motifs are needed to generate a functional FAST protein (page 13, para 13).
In view of the unpredictability of the functions of the variants, there is no basis by which the artisan would expect that the disclosed alanine substituted sequences are representative number of species for the genus. Neither does the specification provide a structure and function correlation for the variants. The disclosure therefore does not show that applicant was in possession of the genus.
It is noted that, “[r]egardless whether a compound is claimed per se or a method is claimed that entails the use of the compound, the inventor cannot lay claim to the subject matter unless he can provide a description of the compound sufficient to distinguish infringing compounds from non-infringing compounds, or infringing methods from non-infringing methods.” University of Rochester v. G.D. Searle Co., 69 USPQ2d 1886 1984 (CAFC 2004) (emphasis added).
Conclusion
8. Claims 1-4, 9-14, 19-20, 31-32 and 34-35 are rejected. Claim 33 is allowable.
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.
9. Any inquiry concerning this communication or earlier communications from the examiner should be directed to HONG SANG whose telephone number is (571)272-8145. The examiner can normally be reached Monday-Friday 8am-5pm.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Gregory Emch can be reached on 571-272-8149. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/HONG SANG/Primary Examiner, Art Unit 1643
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