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 .
Claim Status
Claims 1-4, 6, 8-11, 14-17, 22, 25, and 29 are pending (claim set as filed on 02/24/2026). Claims 14-17, 22, 25, 29 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Claim 8 is withdrawn as being drawn to a non-elected species. Applicant previously elected invention Group I, claims 1-11 and 13, sequence species ‘SEQ ID NO: 7’, and the condition or disease species ‘inflammatory bowel disease’, in the reply filed on 10/14/2025.
Claims 1-4, 6, 9-11 are currently under examination and were examined on their merits.
Withdrawn Objections/Rejections
The objections to the drawings, Figures 9a-c and 12c set forth in the previous Office action are withdrawn in light of the amended drawings filed on 02/24/2026.
The rejection of claims 5 and 13 under 35 U.S.C. 112(d) set forth in the previous Office action is withdrawn in light of the amendment filed on 02/24/2026.
Claim Rejections - 35 USC § 112(a)
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 6 and 9 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 claims contain subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
As stated in MPEP 2111.01, during examination, the claims must be interpreted as broadly as their terms reasonably allow. Claim 6 is directed in part to a genus of autolysin variants that have at least 90% sequence identity to the polypeptide of SEQ ID NO: 1, and claim 9 is directed to a genus of proteins that comprise variants of the polypeptide of SEQ ID NO: 7 having at least 90% sequence identity with the polypeptide of SEQ ID NO: 7.
In University of California v. Eli Lilly & Co., 43 USPQ2d 1938, the Court of Appeals for the Federal Circuit has held that “A written description of an invention involving a chemical genus, like a description of a chemical species, ‘requires a precise definition, such as by structure, formula, [or] chemical name,’ of the claimed subject matter sufficient to distinguish it from other materials”. As indicated in MPEP § 2163, the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show that Applicant was in possession of the claimed genus. In addition, MPEP § 2163 states that a representative number of species means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
There is either (a) no structural limitation, or (b) a significant amount of structural variability with respect to variants of the polypeptide of SEQ ID NO: 1 or variants of the polypeptide of SEQ ID NO: 7 required by the claims. While the specification in the instant application discloses the basic structure of the autolysin Lys2 (SEQ ID NO: 1) from Lactobacillus plantarum and of the polypeptide of SEQ ID NO: 7, wherein Lys2 comprises a cell wall targeting region comprising a SH3 type 5 domain (see Figure 2a, see Example 1 on pages 23-24), and wherein the polypeptide of SEQ ID NO: 7 corresponds to a truncated version of the cell wall targeting region (see Figure 2a), it provides no clue as to the structural elements required in any autolysin protein, nor does it teach which specific structural elements within SEQ ID NO: 1 or SEQ ID NO: 7 are required. No disclosure of a structure/function correlation on an amino acid sequence level has been provided which would allow one of skill in the art to recognize which variants of the polypeptide of SEQ ID NO: 1 or SEQ ID NO: 7 having the recited % sequence identity have the desired cell wall targeting activity.
The claims encompass a large genus of proteins which are structurally unrelated or substantially unrelated in structure. A polypeptide having 90% sequence identity with the polypeptide of SEQ ID NO: 1 allows for any combination of 86 amino acid modifications within SEQ ID NO: 1 (86 = 0.1x860; SEQ ID NO: 1 has 860 amino acids). The total number of variants of a polypeptide having a specific number of amino acid substitutions can be calculated from the formula N!x19A/(N-A)!/A!, where N is the length in amino acids of the reference polypeptide and A is the number of allowed substitutions. Thus, the total number of variants of the polypeptide of SEQ ID NO: 1 having 90% sequence identity to the polypeptide of SEQ ID NO: 1 that result from amino acid substitutions is 860!x1986/(860-86)!/86! (SEQ ID NO: 1 has 860 amino acids) or 1.1x10230 variants. A similar calculation 228!x1922.8/(228-22.8)!/22.8! for variants of the polypeptide of SEQ ID NO: 7 having 90% sequence identity to the polypeptide of SEQ ID NO: 7 yields 1.9x1060 variants (SEQ ID NO: 7 has 228 amino acids). A sufficient written description of a genus of polypeptides may be achieved by a recitation of a representative number of polypeptides defined by their amino acid sequence or a recitation of structural features common to members of the genus, which features constitute a substantial portion of the genus. However, in the instant case, there is either no recited structural feature which is representative of all the members of the genus of proteins recited, or the recited structural feature, i.e., 90% sequence identity to SEQ ID NO: 1 or SEQ ID NO: 7, is not representative of all the members of the genus of autolysin Lys2 recited since there is no information as to which are the structural elements within the polypeptide of SEQ ID NO: 1 or SEQ ID NO: 7 that are essential for the recited cell targeting activity, which are the remaining structural elements required in the recited polypeptides in addition to those recited in the claims such that the desired cell wall targeting activity is displayed, or a correlation between structure and function which would provide those unknown structural features.
Due to the fact that the specification discloses no variants of SEQ ID NO: 1 and a limited number of variants of SEQ ID NO: 7 required by the claims, and the lack of description of any additional species by any relevant, identifying characteristics or properties, one of skill in the art would not recognize from the disclosure that Applicant was in possession of the claimed invention.
Claim Rejections - 35 USC § 112 (b)
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 1-4, 6, and 9-11 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.
Claim 1 recites “wherein the second polypeptide comprises two to four repeats of the
SH3_5 domain from the cell wall targeting region” which renders the claim indefinite since the comprising language makes it unclear if the second polypeptide could comprise further repeats of the SH3_5 domain in addition to the recited two to four repeats, or if the polypeptide contains at least two but no more than four repeats of the SH3_5 domain. One of ordinary skill in the art would not be able to determine the metes and bounds of the claim, and thus, could not clearly determine how to avoid infringement of claim 1.
Dependent claims 2-4, 6, and 9-11 are rejected since they do not remedy the deficiency of claim 1.
In the interest of compact prosecution, claim 1 is interpreted to the broadest embodiment claimed.
Claim Rejections 35 USC § 103
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.
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 factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
Determining the scope and contents of the prior art.
Ascertaining the differences between the prior art and the claims at issue.
Resolving the level of ordinary skill in the pertinent art.
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.
Claims 1-4, 6, 9, and 11 are newly rejected as necessitated by amendment under 35 U.S.C. 103 as being unpatentable over Mathiesen et al. (“Anchoring of heterologous proteins in multiple Lactobacillus species using anchors derived from Lactobacillus plantarum”, published on 06/15/2020, Scientific Reports, 10(1): 9640, pages 1-10), hereinafter ‘Mathiesen’, in view of Rolain et al. (“Identification of key peptidoglycan hydrolases for morphogenesis, autolysis, and peptidoglycan composition of Lactobacillus plantarum WCFS1”, published on 10/15/2012, Microbial Cell Factories, Vol. 11:137, pages 1-15), hereinafter ‘Rolain’, as evidenced by Kleerebezem et al. (“lysozyme/muramidase, glycoside hydrolase family 25 [Lactiplantibacillus plantarum WCFS1]”, published on 02/27/2015, NCBI, Genbank: CCC80137, downloaded from https://www.ncbi.nlm.nih.gov/protein/CCC80137.1, pages 1-2), hereinafter ‘CCC80137’.
Mathiesen’s general disclosure relates to “multiple surface anchors derived from Lactobacillus plantarum for protein surface display in multiple Lactobacillus species, using a Mycobacterium tuberculosis hybrid antigen as test protein” (see entire document, including abstract).
Regarding claim 1, please not the rejection under Claim Rejections - 35 USC § 112(b) above. Pertaining to an expression construct, Mathiesen teaches an expression construct encoding a fusion protein (“plasmids for expression of surface-anchored antigen”, “pCwa2 … pSIP401 derivative, encoding signal peptide Lp_3050 fused to DC binding sequence followed by the AgE6 hybrid protein and a subsequent LPXTG anchor sequence”, “pLysM … pSIP401 derivative, encoding a signal peptide followed by a LysM domain, derived from Lp_3014, fused to AgE6-DC“; see Table 1, Figure 5, and fusion proteins in Figure 1), the expression construct comprising a nucleic acid encoding a first polypeptide for expression (see AgE6 hybrid protein encoded by plasmid pCwa2 and AgE6-DC encoded by plasmid pLysM in Table 1), and a second polypeptide derived from the cell wall targeting region of a Lactobacillus plantarum (“We have assessed multiple surface anchors derived from Lactobacillus plantarum for protein surface display … two cell wall anchors, one non-covalent (LysM domain) and one covalent (sortase-based anchoring using the LPXTG motif)”; see LPXTG anchor sequence encoded by pCwa2 and LysM domain encoded by pLysM in Table 1), wherein the first and second polypeptides are joined to form a fusion protein (see abstract and pCwa2 plasmid and pLysM plasmid in Table 1; see fusion proteins in Figure 1).
Regarding claim 2, pertaining to the polypeptides, Mathiesen teaches wherein the first and second polypeptides are separated by a linker polypeptide (“the black color indicates the linker regions between the anchor and the fused antigen”; see Figure 1).
Regarding claim 3, pertaining to the polypeptides, Mathiesen teaches wherein the first polypeptide is positioned upstream of the second polypeptide (“AgE6 hybrid protein and a subsequent LPXTG anchor sequence”; see pCwa2 in Table 1; see fusion protein comprising LPXTG anchor sequence in Figure 1).
Regarding claim 4, pertaining to the polypeptides, Mathiesen teaches wherein the first polypeptide is positioned downstream of the second polypeptide (“signal peptide followed by a LysM domain, derived from Lp_3014, fused to AgE6-DC”; see plasmid pLysM in Table 1).
Regarding claim 11, pertaining to a recombinant host cell, Mathiesen teaches wherein the expression construct is comprised in a recombinant host cell (“Thus, three different expression vectors for surface-anchoring were tested in eight Lactobacillus species”, “Lactobacillus strains were made electro-competent and transformed”, “Growth of the recombinant Lactobacillus strains. The growth curves are for lactobacilli harbouring plasmids for expression of intracellular (cyt) or surface-displayed (lipo, cwa2, LysM) AgE6-DC”; page 8, paragraph 2; see abstract and Figure 3).
Additionally, Mathiesen teaches that “surface anchors derived from L. plantarum are promising candidates for efficient anchoring of medically interesting proteins in other food grade Lactobacillus species” (see abstract), wherein L. plantarum is L. plantarum strain WCFS1 (page 6, paragraph 3), and that “[b]ecause lactobacilli are safe and may have immune-stimulating adjuvant effects 3–8, they are promising delivery vectors for antigens and other medical molecules.” (page 1, paragraph 2).
Mathiesen does not teach wherein the second polypeptide is derived from the cell wall targeting region of a Lactobacillus plantarum Lys2 autolysin, wherein the second polypeptide comprises two to four repeats of the SH3_5 domain from the cell wall targeting region (instant claim 1), wherein the Lactobacillus autolysin comprises or consists of an amino acid sequence having at least 90% sequence identity to an amino acid sequence of SEQ ID NO: 1 (instant claim 6), and wherein the second polypeptide comprises or consists of an amino acid sequence having at least 90% sequence identity to an amino acid sequence of SEQ ID NO: 7 (instant claim 9)
Rolain’s general disclosure relates to “the functional role of the predicted peptidoglycan hydrolase (PGH) complement encoded in the genome of L. plantarum by systematic gene deletion” (see entire document, including abstract).
Regarding claim 1, please note the rejection under Claim Rejections - 35 USC § 112 (b) above. Pertaining to the cell wall targeting region, Rolain teaches the cell wall targeting region of a Lactobacillus plantarum Lys2 autolysin (“Bacteria produce a variety of enzymes that are able to degrade PG. These enzymes are collectively called peptidoglycan hydrolases (PGH) or autolysins”, “4 PGHs (Acm2, Lys2, LytA, and LytH) play important roles either in the cell cycle or in the autolysis process of L. plantarum.”, “Most of the PGHs display a modular organization composed of different domains usually associated with functions related to cell wall binding (e.g. LysM, SH3 domains)”, “8 of the 12 PGHs show a modular organization where their catalytic domain is associated with at least one PG binding domain (SH3_3, SH3_5, or LysM)”, “peptidoglycan (PG)”; page 2, left column, paragraph 1; page 2, right column, paragraph 2; and page 5, right column, paragraph 1; see SH3_5 domain in the modular organization of Lys2 in Figure 1),
wherein the second polypeptide comprises five repeats of the SH3_5 domain from the cell wall targeting region (see Fig. 1; please note the five repeats of the SH3_5 domain in the modular organization of Lys2).
Regarding claim 6, pertaining to the Lactobacillus autolysin sequence, Rolain teaches wherein Lys2 is a protein in Lactobacillus plantarum strain WCFS1 (“Identification of key peptidoglycan hydrolases for morphogenesis, autolysis, and peptidoglycan composition of Lactobacillus plantarum WCFS1”, “In this study, we investigate the functional role of the 12 more probable candidates of the PGH complement of L. plantarum WCFS1 by a systematic gene deletion strategy. Characterization of mutant cell morphology, growth, and autolytic behavior, in a range of conditions showed that 4 PGHs (Acm2, Lys2, LytA, and LytH) play important roles either in the cell cycle or in the autolysis process of L. plantarum”; see title and page 2, right column, paragraph 2).
Rolain teaches wherein Lys2 is protein Lp_3093 (see “Lys2 (Lp_3093)” in Figure 1), wherein the amino acid sequence of Lys2 (Lp_3093) has 100% sequence identity to an amino acid sequence of instant SEQ ID NO: 1, as evidenced by CCC80137 (see CCC80137 for amino acid sequence of Lp_3093; see sequence alignment A attached to the previous Office action).
Regarding claim 9, pertaining to the second polypeptide, Rolain teaches the cell wall binding region SH3 type 5 motif polypeptide in Lys2 (Lp_3903) (“Cell-wall binding domains SH3_3, SH3_5”; see Figure 1, especially the SH3_5 domain in the modular organization of Lys2 (Lp_3093) in Figure 1), wherein the SH3 type 5 motif polypeptide extends from position 472 and to position 857 in Lp_3093, as evidenced by CCC80137 (“Region 472..530 / region name “SH3” … Region 800..857 /region_name=”SH3”; see page 2), said region having 99.7% sequence identity to an amino acid sequence of SEQ ID NO: 7, as shown in sequence alignment B attached to the previous Office action.
While Mathiesen does not teach wherein the second polypeptide is derived from the cell wall targeting region of a Lactobacillus plantarum Lys2 autolysin, wherein the second polypeptide comprises two to four repeats of the SH3_5 domain from the cell wall targeting region (instant claim 1), wherein the Lactobacillus autolysin comprises or consists of an amino acid sequence having at least 90% sequence identity to an amino acid sequence of SEQ ID NO: 1 (instant claim 6), and wherein the second polypeptide comprises or consists of an amino acid sequence having at least 90% sequence identity to an amino acid sequence of SEQ ID NO: 7 (instant claim 9), it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have combined Mathiesen’s teachings on an expression construct encoding an antigen fusion protein comprising a L. plantarum derived cell wall targeting region with Rolain’s teachings on the cell wall targeting region from the autolysin Lys2 from Lactobacillus plantarum, in order to have created an expression construct encoding a fusion protein, wherein the second polypeptide of the fusion protein is derived from the cell wall targeting region of a Lactobacillus plantarum Lys2 autolysin, wherein the second polypeptide comprises five repeats of the SH3_5 domain from the cell wall targeting region, wherein the Lactobacillus autolysin comprises or consists of an amino acid sequence having 100% sequence identity to an amino acid sequence of SEQ ID NO: 1, and wherein the second polypeptide comprises or consists of an amino acid sequence having 99.7% sequence identity to an amino acid sequence of SEQ ID NO: 7. One would have been motivated to do so, in order to create a fusion protein with increased cell wall binding to Lactobacillus bacteria for improved delivery of medically interesting proteins by food grade Lactobacillus species (see Mathiesen; abstract and page 1, paragraph 2). A skilled artisan would have reasonably expected success in combining Mathiesen’s and Rolain’s teachings since both references are directed to cell-wall targeting regions of Lactobacillus plantarum (see above).
Claims 1 and 10 are newly rejected as necessitated by amendment under 35 U.S.C. 103 as being unpatentable over Mathiesen et al. (“Anchoring of heterologous proteins in multiple Lactobacillus species using anchors derived from Lactobacillus plantarum”, published on 06/15/2020, Scientific Reports, 10(1): 9640, pages 1-10), hereinafter ‘Mathiesen’, in view of Rolain et al. (“Identification of key peptidoglycan hydrolases for morphogenesis, autolysis, and peptidoglycan composition of Lactobacillus plantarum WCFS1”, published on 10/15/2012, Microbial Cell Factories, Vol. 11:137, pages 1-15), hereinafter ‘Rolain’, as evidenced by Kleerebezem et al. (“lysozyme/muramidase, glycoside hydrolase family 25 [Lactiplantibacillus plantarum WCFS1]”, published on 02/27/2015, NCBI, Genbank: CCC80137, downloaded from https://www.ncbi.nlm.nih.gov/protein/CCC80137.1, pages 1-2), hereinafter ‘CCC80137’, in view of Han et al. (“Improvement of an Experimental Colitis in Rats by Lactic Acid Bacteria Producing Superoxide Dismutase”, published in Nov 2006, Inflamm Bowel Dis, Vol. 12, No. 11, pages 1044-1052), hereinafter ‘Han’.
Mathiesen’s and Rolain’s teachings have been set forth above.
Modified Mathiesen does not teach wherein the first polypeptide is superoxide dismutase (SOD) (instant claim 10).
Han’s general disclosure relates to “the effects of oral treatment with live recombinant lactic acid bacteria producing different amounts of SOD” (see entire document, including abstract).
Regarding claim 10, pertaining to the first polypeptide, Han teaches that “oral administration of LAB expressing SOD improves a TNBS experimental colitis in rats” (page 1051, left column, paragraph 1; note, lactic acid bacteria (LAB) (page 1044, right column, paragraph 2) and 2,4,6-trinitrobenzenesulphonic acid (TNBS) (page 1045, left column, paragraph 2)), and that “SOD-producing lactic acid bacteria open a novel approach in inflammatory bowel disease treatment” (see abstract). Additionally, Han teaches wherein “The use of superoxide dismutases (SODs) in inflammatory diseases is hampered by their short circulatory half-life” (see abstract).
While modified Mathiesen does not teach wherein the first polypeptide is superoxide dismutase (SOD) (instant claim 10), it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have combined modified Mathiesen’s expression construct with Han’s teachings on superoxide dismutase, to have created an expression construct wherein the first polypeptide is superoxide dismutase (SOD). One would have been motivated to do so to increase the half-life and delivery of SOD by incorporating it into a fusion protein that binds to a Lactobacillus cell wall, wherein the Lactobacillus is used for delivery of SOD, thereby resulting in improved treatment of inflammatory diseases such as inflammatory bowel disease (see Han, abstract). A skilled artisan would have reasonably expected success in combining modified Mathiesen’s and Han’s teachings since both are directed to the delivery of medically interesting proteins using lactic acid bacteria.
Response to Arguments
Applicant has traversed the previous rejections of claims 1-7, 9-11, and 13 under 35 U.S.C. 103 in the reply filed on 02/24/2026 (remarks, pages 7-9). Applicant's arguments have been fully considered but they are not persuasive.
Applicant describes that “[a] person skilled in the art following the teachings of the combinations of the cited documents would not have considered or been motivated to truncate anchoring domains to improve surface display of heterologous proteins” (remarks, page 9).
In response to Applicant's argument that the references fail to show certain features, i.e. truncation of anchoring domains of the invention, please note the rejection under Claim Rejections - 35 USC § 112 (b) above. The feature upon which Applicant relies, truncation of anchoring domains, is not recited in the rejected claim(s). 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).
Applicant discusses the experimental results obtained with the instant fusion proteins.
The Examiner responds that in light of Mathiesen’s teachings on anchoring of heterologous proteins in Lactobacillus species using anchors derived from Lactobacillus plantarum and in light of Rolain’s teachings on autolysin Lys2 from Lactobacillus plantarum, a skilled artisan would have reasonably expected that a fusion protein comprising cell wall binding domains from Lys2 would bind to the cell wall of a Lactobaclllus.
Conclusion
No claims are allowed.
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.
Correspondence Information
Any inquiry concerning this communication or earlier communications from the examiner should be directed to SANDRA ZINGARELLI whose telephone number is (703)756-1799. The examiner can normally be reached M-F 9-5.
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/SANDRA ZINGARELLI/Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653