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 .
Following office action is formulated as second non-final rejection since claims 4 and 29 in step (f) is analyzed with introduction of new art of Goldman et al. (Published: 2017, Journal: Front. Immunol. 8:865. doi: 10.3389/fimmu.2017.00865) and Khan et al. (Published: 2014, Journal: Saudi Journal of Biological Sciences 21: 173–177), see below.
Election/Restrictions
Applicant's amendment of claims submitted on 03/19/2026 has been acknowledged. Claims 4, 14-15, 17, 26-29, 33, 36-42 are pending.
Claim 36-42 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a claim reciting nonelected species by original presentation, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on 07/08/2025.
Therefore, claims 4, 14-15, 17, 26-29 and 33 along with the elected species of SEQ ID NO:17 is examined in this office action.
Rejection that are withdrawn
Objection to specification is withdrawn in light of applicant’s amendment of specification by include a proper symbol indicating use in commerce.
Objection to claims 4, 15 and 29 are withdrawn in light of applicant’s amendment of the claims by deleting the terms “identify” and “which”.
35 USC § 112 – Indefiniteness rejection has been withdrawn in light of applicant’s amendment of the claims 4, 29 by deleting the terms “which”, “about”, deletion of claims 10 and 19.
Claim Interpretation
In claims 4 and 29 last lines, the recitation of phrase “heavy chain variable domain of an antibody” is interpreted as applicant defines "Heavy chain variable domain of an antibody or a functional fragment thereof', as used herein, means (i) the variable domain of the heavy chain of a heavy chain antibody, which is naturally devoid of light chains (also indicated hereafter as VHH), including but not limited to the variable domain of the heavy chain of heavy chain antibodies of camelids or sharks or (ii) the variable domain of the heavy chain of a conventional four-chain antibody (also indicated hereafter as VH), including but not limited to a camelized (as further defined herein) variable domain of the heavy chain of a conventional four-chain antibody (also indicated hereafter as camelized VH).” (page 20, lines 26-32). Thus, it is interpreted as include heavy chain antibodies of camelids, sharks or camelized VHH.
Claim Rejections - 35 USC § 112 - Indefiniteness
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.
Claim 28 is 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 28 recites the limitation “inhibiting” which renders the claim indefinite. Is it 100% inhibition for every plant all the time? Or inhibits a certain percentage? Or a reduced frequency of infection? Or a reduced severity of symptoms? It is unclear what effects would be encompassed by the claimed “inhibiting”.
Response to Argument for Rejection
Applicant's arguments 03/19/2026 have been fully considered but they are not persuasive.
Applicant argues in the context of "inhibiting the growth of a plant pathogenic fungus", the skilled person would readily understand that inhibiting refers to any reduction and/or prevention of fungal growth. Applicant argues this understanding is also explicitly supported by the application as filed. For example, page 14, lines 22-31, states (emphasis added):
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Applicant's arguments have been fully considered but they are not persuasive since the definition is open ended with comprising the uncertain term “may mean”. Furthermore, claim does not have any standard or control to compare. Therefore, the rejection has been maintained.
Claim Rejections - 35 USC § 112 – Written Description Requirements
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 4, 14-15, 17, 26-29, 33 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.
The claim is drawn to a polypeptide comprising an amino acid sequence of SEQ ID NO: 17 or its complementary determining regions (CDRs), wherein said polypeptide is capable of binding to a fungus. Wherein the polypeptide is a heavy chain variable domain of an antibody.
Analysis of Breadth of Claims
Claims encompasses large variants of polypeptides that comprises an amino acid sequence having the CDR1, CDR2 and CDR3 of SEQ ID NO: 17.
Applicant has not described polypeptide binding to any plasma membrane component of any fungus (claim 12).
Claim 28 encompass inhibiting growth of a plant pathogenic fungus compared to any control or standard plant.
Claims encompass the polypeptide binds to large genus of fungal species (claims, 17 and 26-28).
Claims encompass variants of SEQ ID NO:17 comprising any substitutions resulting in increased positive charge that would bind to the large genus of fungus or the lipid containing fraction of the plasma membrane of Botrytis cinerea.
What is Described in the Specification
Applicant describes the following:
VHHs were generated from llamas immunized with a Folch lower phase extract from Fusarium oxysporum (page 77, lines 1-8).
positively charged variants were designed based on the structural analysis as described in Example 10 as Mutant 11: S27K, I28K and S30K substitutions in CDR1 and W100aK and T1 00bK substitutions in CDR3 (See Figure 8) (SEQ ID NO: 17) (page 80, lines 30-42).
Figure 6 shows mutant 11 (i.e. SEQ ID NO:17) show a significant increase in antifungal activity, with mutant 11 reaching up to 5-fold increase in anti-fungal activity over 10G11.
performing a prolonged incubation antifungal assay over a period of 14 days, showed a sustained effect on preventing spore outgrowth by Mutant 11 over the assessed time, as opposed to 10G11 which, although highly potent, allowed spore outgrowth to partly reinitiate after 3 days (Figure 9) (page 81, lines 1-5).
The antifungal acidity was assessed in vitro against the plant pathogenic fungus Botrytis cinerea R16 (page 78, lines 10-12, page 81, lines 1-5).
Difference Between What was Reduced to Practice and What is Claimed
Applicant has not described inhibiting growth of any plant pathogenic fungus compared to any control or standard plant (claim 28).
Applicant has not described the variants of polypeptide sequence comprising SEQ ID NO: 17 that encompass CDR1, CDR2 and CDR3 of SEQ ID NO:17 which are SEQ ID NOs: 57, 68 and 89 (see page 11, Table 9) respectively would has any effect against the claimed pathogenic fungal species (claims 4 and 29 (b)).
Applicant has not described any embodiments wherein the VHH SEQ ID NO: 17 capable binding to any of the plant pathogenic fungus of genera Alternaria, Ascochyta, Botrytis, etc. (17 and 26-28).
Applicant has not described variants of SEQ ID NO:17 comprising any substitutions resulting in increased positive charge that would bind to the large genus of fungus or the lipid containing fraction of the plasma membrane of Botrytis cinerea.
Analysis
The purpose of the written description is to ensure that the inventor had possession at the time the invention was made, of the specific subject claimed. For a broad generic claim, the specification must provide adequate written description to identify the genus of the claim.
Given the many variants of polypeptides associated with the claimed genus, one would not be able to predict their effects to specifically bind to any of a fungus and it is impossible to predict such a broad sequence variation of at least having any of the CDR1, CDR1 and CDR3 of SEQ ID NO: 17 which are SEQ ID NOs: 57, 68 and 89 (see page 11, Table 9) respectively would has any effect against the claimed pathogenic fungal species. Since applicant has not described any sequence with CDR1, CDR1 and CDR3 of SEQ ID NO: 17 which are SEQ ID NOs: 57, 68 and 89 (see page 11, Table 9, see below figure for location in sequence) in any other sequence other than SEQ ID NO:17 (claims 4 and 29 (b)).
CDR1/SEQ ID NO:57 CDR2/ SEQ ID NO: 68
DVQLVESGGGLVQAGGSLRLSCAASRKKFKINAMDWYRQAPGKQREWVAGITRGGTTKYADSVK
CDR3/ SEQ ID NO: 89
GRFTISRDNAKKKVYLQMNSLKPEDTAVYYCNVLRGEQPKKRDYWGQGTQVTVSS
Applicant has not described any polypeptide of any size and composition (i.e. with any structure of framework regions (see page 36, lines 1418) comprising the CDR1, CDR1 and CDR3 would be capable to bind to the diverse species of fungus including binding to the plasma membrane of B. cinera that would be useful as treating fungal infected plant or inhibit or kill the growth of the plant pathogenic fungus other than the SEQ ID NO:17 itself. For example, applicant teaches different domains are important for specific property of the polypeptides (page 32, lines 1-24). Therefore, it is not clear whether grafting of these CDRs would cause loss of antigen-binding affinity or cause structural instability to the recited any structure of the framework regions of the VH or VHH. For example, Guo et al. (Published: 2004, Journal: Proceedings of the National Academy of Sciences, 101(25), 9205-9210) describes that while proteins are fairly tolerant to mutations resulting in single amino acid changes, increasing the number of substitutions additively increases the probability that the protein will be inactivated (page 9205, right. col., Paragraph 2).
Applicant has not described any embodiments wherein the VHH SEQ ID NO: 17 capable binding to any of the plant pathogenic fungus of genera Alternaria, Ascochyta, Botrytis, etc. (claims 17 and 26-28). VHH are specific for example Coninck et al. (Published: 2017, Journal: Frontiers in Microbiology, 8, 1059) teaches VHH that bind to fungal glucosylceramides (fGLcCer) and not the mammalian or plant-derived glucosylceramides and those were shown to inhibit growth of B. cinerea (page 1, Abstract) and binding capacity of the VHHs towards fGLcCer varied strongly (Figure 3A). Thus, there is a dearth of description of structure of antigen with the fungus that bind to the disclosed VHH. Since applicant specifically defines the VHH are antigen specific and if it binds to one antigen could not bind to another antigen. Thus, the genus of capable of binding to any fungus is not described well. The limited species described by Applicant are insufficient to describe the large recited genus by virtue of example (claims 17 and 26-28).
Recited genus of any species of the plant pathogenic fungus of species Alternaria, Ascochyta, Botrytis, etc.(as in claim 17), encompass large number of species and strains that may not be effected by the SEQ ID NO: 17. Applicant has only reduced to practice that has reduced growth of the plant pathogenic fungus Botrytis cinerea R16 (page 78, lines 10-12, page 81, lines 1-5) with SEQ ID NO:17 as Mutant 11.Thus there is dearth of description of whether any peptides comprising SEQ ID NO:17 or the CDRs of SEQ ID NO:17 would be effective to control all the recited pathogen genus of fungus. The limited species described by Applicant are insufficient to describe the large recited genus by virtue of example.
Furthermore, Applicant has not described variants of SEQ ID NO:17 comprising any substitutions resulting in increased positive charge that would bind to the large genus of fungus or the lipid containing fraction of the plasma membrane of Botrytis cinerea.
Applicant has not described the method of protecting or treating a plant or a part from any plant pathogenic fungus (claims 26-28) other than for the plant pathogenic fungus Botrytis cinerea R16 (page 78, lines 10-12, page 81, lines 1-5) with SEQ ID NO:17 as Mutant 11. For example, Goldman et al. (Published: 2017, Journal: Front. Immunol. 8:865. doi: 10.3389/fimmu.2017.00865) teaches specific position for example 44 would be useful to enhance the electrostatic interaction with negatively charged molecules in the medium to create stability (page 7, left paragraph 1).
Applicant although showed the 10G11 (i.e. SEQ ID NO:1, Spec, page 9, lines 11-12) has effect on controlling soybean rust (Phakopsora pachyrhizi, Colletotrichum orbiculare, Uncinula necator, Oidium neolycopersici etc. (Spec, page 82) however 10G11 as SEQ ID NO:1 has only 78% identity to the recited sequence of SEQ ID NO:17 (see alignment below), therefore applicant has not described any of the sequence having at least 80% sequence identity to SEQ ID NO: 17 would bind to any fungus or fungus recited in claim 17 and would be used in method for protecting or treating plant from infection of the plant pathogenic fungus other than for Botrytis cinerea.
Furthermore, Applicant has not described a transgenic plant, plant part, seed, or plant cell comprising a nucleic acid sequence encoding a polypeptide of SEQ ID NO:17 without the sequence operably linked to heterologous region. SEQ ID NO: 17 is an engineered VHH, the expression of the SEQ ID NO:17 would require an heterologous promoter or expression element operably linked to the sequence to express in the transgenic plant cell.
“A patentee will not be deemed to have invented species sufficient to constitute the genus by virtue of having disclosed a single species when … the evidence indicates ordinary artisans could not predict the operability in the invention of any species other than the one disclosed.” In re Curtis, 354 F.3d 1347, 1358, 69 USPQ2d 1274, 1282 (Fed. Cir. 2004). For inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus. See, e.g., Eli Lilly.
Further, it is not sufficient to define it solely by its principal biological property, because an alleged conception having no more specificity than that is simply a wish to know the identity of any material with that biological property. Per the Enzo court’s example, (Enzo Biochem, Inc. v. Gen-Probe Inc., 63 USPQ2d 1609 (CA FC 2002) at 1616) of a description of an anti-inflammatory steroid, i.e., a steroid (a generic structural term) couched “in terms of its function of lessening inflammation of tissues” which, the court stated, “fails to distinguish any steroid from others having the same activity or function” and the expression “an antibiotic penicillin” fails to distinguish a particular penicillin molecule from others possessing the same activity and which therefore, fails to satisfy the written description requirement. Applicant has not disclosed any relevant, identifying characteristics, such as structure or other physical and/or chemical properties, sufficient to show possession of the claimed genus. Mere idea or function is insufficient for written description; isolation and characterization at a minimum are required. A description of what a material does, rather than what it is, usually does not suffice. Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406.
No common structural attributes identify the members of the genus. The general knowledge and level of skill in the art do not supplement the omitted description, because specific, not general guidance is needed. Since the disclosure does not describe the common attributes or structural characteristics that identify members of the genus, and because the genus is highly variant without function is insufficient to describe the genus of “pathogenic plant pests to protect or treat a plant or a harvested part of a plant, a human or animal, or an object” of that function equivalently. One of skill in the art would reasonably conclude that the disclosure of a treating or preventing a plant or a harvested part of a plant against Botrytis cinerea infection does not provide a representative number of fungal pests to protect or treat a plant or a harvested part of a plant, a human or animal or an object to describe the claimed genus. As such, the specification lacks written description for the highly variant genus and one skilled in the art would not recognize that applicants had possession of the genus of claimed fungal pests to protect or treat a plant or a harvested part of a plant, a human, animal, or an object as instantly claimed.
Therefore, only treating or preventing a plant or a harvested part of a plant against Botrytis cinerea infection but not the full breadth of the claim meets the written description provision of 35 U.S.C. §112, first paragraph. Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. §112 is severable from its enablement provision (see page 1115).
Given the virtually infinite structural variable associated with these embodiments, the claims read on an extremely broad and highly diverse structures that needs to have specific function of inhibiting growth of multiple genus of plant pathogenic fungus and have ability to bind to the different structures of fungal antigens. Thus, in view of the analysis presented above, a skilled artisan would appreciate that the claims are directed to extremely broad and highly diverge genus of sequence variants.
Given the large size and structural diversity associated with the claimed genus, Applicant’s disclosure is not representative of the claimed genus as a whole. This point is particularly relevant because, as discussed above, the experiment results in specification and prior art speaks to the disconnection between the structure of the broadly claimed variants in any agrochemical composition and the recited specific function of binding to the multiple genus of fungi and inhibiting their growth.
"The test for sufficiency is whether the disclosure of the application relied upon reasonably conveys to one skilled in the art that the inventor had possession of the claimed subject matter as of the filing date." Ariad Pharm., Inc, v EH Lilly & Co., 598 F.3d 1336, 1351 (Fed. Cir. 2010). To satisfy the written description requirement, a patent 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. Lockwood v. Amer. Airlines, ina, 107 F.3d 1565, 1572, 41 USPQ2d 1961, 1966 (Fed. Cir. 1997). "An applicant shows possession of the claimed invention by describing the claimed invention with all of its limitations. Lockwood, 107 F.3d at 1572, 41 USPG2d at 1966". While the written description requirement does not demand either examples or an actual reduction, actual "possession" or reduction to practice outside of the specification is not enough. Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F,3d 1336,1352 (Fed. Cir. 2010). Rather, it is the specification itself that must demonstrate possession. Id.
Thus, based on the analysis above, Applicant has not met either of the two elements of the written description requirement as set forth in the court's decision in Eli Lilly. As a result, it is not clear that Applicant was in possession of the claimed genus at the time this application was filed.
Response to Argument for Rejection
Applicant's arguments 03/19/2026 have been fully considered but they are not persuasive.
Applicant argues regarding claims 17 and 26-28 claims specify that the polypeptides are VHHs capable of binding to a lipid-containing fraction of the plasma membrane of Botrytis cinerea. Applicant argues the claims further define this lipid-containing fraction by reference to the method used to obtain it, namely fractionating hyphae of Botrytis cinerea by total lipid extract thin-layer chromatography and selecting the fraction with a Retention Factor (Rf) higher than the ceramide fraction and lower than the non-polar phospholipids fraction (Response to Rejection, page 14, first paragraph).
Applicant argues the application as-filed provides extensive support for VHHs having this property. Applicant argues in particular; the application describes a class of VHHs that bind to the lipid fraction referred to in the application as "Fraction 3". Applicant argues this fraction is specifically defined and characterized in the Examples section of the application (Response to Rejection, page 14, second paragraph).
Applicant argues throughout the application, numerous VHHs capable of binding to this lipid fraction are disclosed and experimentally characterized. Applicant argues the application further demonstrates that these VHHs exhibit antifungal activity against several plant pathogenic fungi. For example:
In examples 5, 6, 17, and 21 the antifungal activity against Botrytis cinerea is shown;
• In example 15 the antifungal activity against Phakopsora pachyrhizi is shown;
• In example 16 the antifungal activity against Colletotrichum orbiculare is shown;
• In example 19 the antifungal activity against Oidium neolycopersici is shown;
• In example 20 the antifungal activity against Podosphaera aphanis is shown; and
• In example 22 the antifungal activity against Podosphaera xanthii is shown.
Applicant argues antifungal activity is not only demonstrated for a single VHH, but also for numerous related VHH variants. For example:
• Examples 5 and 6 demonstrate the antifungal activity of lOGllQ (Full sequence SEQ ID NO: l; CDRl SEQ ID NO: 52; CDR2 SEQ ID NO: 68; CDR3 SEQ ID NO: 84);
• Examples 12, 15, 17, 18, and 19-22 demonstrate the antifungal activity of lOGll (Full sequence SEQ ID NO: 2; CDRl SEQ ID NO: 52; CDR2 SEQ ID NO: 68; CDR3 SEQ ID NO: 84);
• Example 13 demonstrates the antifungal activity of lOEllQ, lOEll, 12C03Q, and 12C03 (Full sequence SEQ ID NOs: 3-6; CDRl SEQ ID NOs: 53-54; CDR2 SEQ ID NOs: 69-70; CDR3 SEQ ID NOs: 85-86); (Response to Rejection, page 14, last 5 paragraphs).
Example 11 demonstrates the antifungal activity of mutant 6-11 VHHs (Full sequence SEQ ID NOs: 12-17; CDR1 SEQ ID NOs: 52, 56-57; CDR2 SEQ ID NO: 68; CDR3 SEQ ID NOs: 84, 88-89); and
• Example 8 demonstrates the antifungal activity of single-ALA mutant 1-34 VHHs (Full sequence SEQ ID NOs: 18-51; CDR1 SEQ ID NOs: 52, 58-67; CDR2 SEQ ID NOs: 68, 72-83; CDR3 SEQ ID NOs: 84, 90-100).
Applicant argues these examples demonstrate that the application provides a substantial number of representative VHHs sharing the same functional property, namely binding to the lipid fraction referred to as "Fraction 3" (Response to Rejection, page 14, paragraphs 1-3).
Applicant argues the VHHs recited in the amended claims share common structural features, including specific CDR regions and full-length sequences that are explicitly disclosed in the application. Applicant argues the amended claims are therefore directly supported by the sequence disclosures and experimental data provided throughout the application (Response to Rejection, page 14, paragraph 4).
Applicant argues Accordingly, the amended claims are fully supported by the description and comply with the written description requirement under 35 U.S.C. §l 12(a).
Applicant's arguments have been fully considered but they are not persuasive since:
Regarding argument on application further demonstrates that these VHHs exhibit antifungal activity against several plant pathogenic fungi was not found persuasive since the example of 10G11 (i.e. SEQ ID NO:1, Spec, page 9, lines 11-12) has effect on controlling soybean rust (Phakopsora pachyrhizi, Colletotrichum orbiculare, Uncinula necator, Oidium neolycopersici etc. (Spec, page 82) however 10G11 as SEQ ID NO:1 has only 78% identity to the recited sequence of SEQ ID NO:17 (see alignment below), therefore applicant has not described any of the sequence having SEQ ID NO: 17 or its CDRs would bind to any fungus or fungus recited in claim 17 and would be used in method for protecting or treating plant from infection of the plant pathogenic fungus other than for Botrytis cinerea.
Furthermore, Applicant has not described the variants of polypeptide sequence comprising SEQ ID NO: 17 that encompass CDR1, CDR2 and CDR3 of SEQ ID NO:17 which are SEQ ID NOs: 57, 68 and 89 (see page 11, Table 9) respectively would has any effect against the claimed pathogenic fungal species (claims 4 and 29 (b)). Therefore, the rejection has been maintained.
In following analysis previous 102 rejection has been modified to 102/103 rejection since applicant has recite the sequence having 100% identity to SEQ ID NO:17.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Anticipated by Patent No. 10400033
Claims 4, 14-15, 17, 26-29, 33, 36-42 are rejected under 35 U.S.C. 102 (a) (1) and/or (a)(2) as anticipated by Verheesen’33 (US Patent No.: US 10,400,033 B2, Date of Patent: Sep. 3,2019) or, in the alternative, under 35 U.S.C. 103 as obvious over Goldman et al. (Published: 2017, Journal: Front. Immunol. 8:865. doi: 10.3389/fimmu.2017.00865), and further in view of Khan et al. (Published: 2014, Journal: Saudi Journal of Biological Sciences 21: 173–177).
Claims are drawn to ta composition or a polypeptide comprising SEQ ID NO:17 wherein the polypeptide bind to the lipid-containing fraction of the plasma membrane of a B. cinerea, Alternaria etc.
Following analysis is based on the recitation of claim 4 and 29 and their step (f) where claim recite polypeptide comprises one or more (i.e. any numbers) substitutions resulting in increased positive charge. Furthermore, since the newly added limitation recite “at least one polypeptide as set out in a)-f)” the limitation would not need to apply to any of the steps. For example, a polypeptide of step c, d, e recites CDRs not found in SEQ ID NO:17.
Following analysis based on the In re Thorpe, 777 F.2d 695, 698, 227 USPQ 964, 966 (Fed. Cir. 1985) which teaches “[E]ven though product-by-process claims are limited by and defined by the process, determination of patentability is based on the product itself. The patentability of a product does not depend on its method of production. If the product in the product-by-process claim is the same as or obvious from a product of the prior art, the claim is unpatentable even though the prior product was made by a different process.” Thus, a product-by-process claim may be properly rejectable over prior art teaching the same product produced by a different process, if the process of making the product fails to distinguish the two products.
Claims are directed to a polypeptide which has any substitutions in SEQ ID NO:17 that result in increase in positive charge that are capable binding to a fungus (claims 4 and 29 (f)). Claims are drawn to a method of protecting or treating a plant, a part of post-harvest part by applying the composition. Claims are drawn to a transgenic plant comprising the nucleic acid sequence encoding the polypeptide.
Regarding claims 4 and 29, alignment of SEQ ID NO: 17 to Verheesen’33.’s SEQ ID NO:79 identified as VHH sequence (col. 167) showed the fragments are present which has 100% local similarity for example in position 6-25 (see alignment below) as taught by Verheesen’33. The sequence has 81% identity to applicant’s recited SEQ ID NO:17 which comprises various substitution with positive, neutral amino acid substitutions. Applicant showed the positively charged amino acid on page 40 lines 40-43 and page 41-42 wherein the Verheesen’33’s SEQ ID NO: 79 has similar positively charged amino acid substitutions such as S, T, C, P, N, Q, K, R or H, therefore the VHH would have increased positive charge compared to SEQ ID NO:17 (see alignment below).
Furthermore, Verheesen’33 teaches an antifungal composition (i.e. agrochemical composition) comprising a polypeptide that is a VHH or a functional fragment thereof (col. 255, claim 1, lines 15-34) that bind to a glucosylceramide of a fungal plant pest. Verheesen’33 teaches binding of VHH 41D01 to lipid extracts and their different effect on fungal pathogens (Figure 5).
Alignment of Applicant’s SEQ ID NO: 17 to Verheesen’33’s SEQ ID NO: 79
Query: unnamed protein product Query ID: lcl|Query_4609115 Length: 119
>unnamed protein product
Sequence ID: Query_4609117 Length: 120
Range 1: 2 to 120
Score:184 bits(468), Expect:6e-67,
Method:Compositional matrix adjust.,
Identities:94/119(79%), Positives:97/119(81%), Gaps:1/119(0%)
Query 2 VQLVESGGGLVQAGGSLRLSCAASRKKFKINAMDWYRQAPGKQREWVAGITRGGTTKYAD 61
VQL ESGGGLVQAGGSLRLSCAAS F IN M WYRQAPGKQR+ VA ITR G+T Y D
Sbjct 2 VQLQESGGGLVQAGGSLRLSCAASGSIFGINDMGWYRQAPGKQRDLVADITRSGSTHYVD 61
Query 62 SVKGRFTISRDNAKKKVYLQMNSLKPEDTAVYYCNVLRGEQ-PKKRDYWGQGTQVTVSS 119
SVKGRFTISRDNAK VYLQMNSLKPEDTAVYYCN G +RDYWGQGTQVTVSS
Sbjct 62 SVKGRFTISRDNAKNTVYLQMNSLKPEDTAVYYCNADSGSHWWNRRDYWGQGTQVTVSS 120
The Examiner does not have a laboratory for measuring the positive charge of Verheesen’33’s SEQ ID NO: 79, however it appears to be there will be some increase in positive charge since the substitutions are appear to be of positive amino acids in Verheesen’33’s SEQ ID NO: 79 compared to applicant’s SEQ ID NO:17 (see alignment above).
The Office does not have the facilities and resources to provide the factual evidence needed in order to establish that the product of the prior art does not possess the same, material, structural and functional characteristics of the claimed product. In the absence of evidence to the contrary, the burden is on the Applicant to provide that the claimed product is different from those taught by the prior art and to establish patentable differences. See In re Best 562F.2d 1252 USPQ 430 (CCPA 1977) and Ex parte Gray 10 USPQ 2d 1922 (PTO Bd. Pat. App. & Int. 1989).
Or in alternative the Goldman et al. teaches the mutation to a positively charged residue at certain position would increase the VHH binding to the fungus Malassezia furfur, a fungus responsible for the formation of dandruff.
Furthermore, Verheesen’33’ teaches thin layer chromatography (THC) glucosylceramide (GLcCer) from Pleurotus citrinopileatus (col. 91, lines 45-50). Verheesen’33’ teaches the pest target to which their disclosed polypeptide would be plasma membrane component as phospholipid bilayer or any other protein therein. The plasma membrane component could be phospholipid, a glycoprotein, a carbohydrate or cholesterol (col. 59, lines 8-18). Furthermore Khan et al. teaches that the THC is used for separation and detection of non- polar and polar lipids from the skin tissue samples using retention factor (rf) values to separate specific lipids for example ceramide. Khan et al. teaches phospholipid comprise about 45% of total lipid in basal layers fraction of the THC. Khan et al. teaches THC is simple method of separation and quantification of skin lipids (page173, Abstract). Therefore, someone skilled in the art would choose the fraction with a Retention Factor (Rf) higher than the ceramide fraction and lower than the non-polar phospholipids fraction to find lipids that bind to the polypeptide.
Therefore someone skilled in the art before the effective date of filling of the invention from teaching suggestion and motivation of Verheesen’33 would use the polypeptide of SEQ ID NO: 79 of Verheesen’33 that is used in antifungal composition (i.e. agrochemical composition) which would comprise many of the positively charged amino acids, and someone would increase the positive charge since Goldman et al. suggested that the increase in positive charged residue would increase VHH binding to the lipid bin containing fraction of fungus B. cinerea. Furthermore, it would have been obvious to try from different fragment taught by Khan et al. and choose the fraction with a Retention Factor (Rf) higher than the ceramide fraction and lower than the non-polar phospholipids fraction.
Regarding claim 14, Verheesen’33 discloses claim 4 teaches the polypeptide is from 0.0001% to 50% by wight of the composition.
Regarding claim 15, Verheesen’33 discloses the composition further comprises suitable carrier and adjuvants (col. 256, lines 24-26).
Regarding claims 17, Verheesen’33 discloses a method where in protecting against or treating an infection or biological interaction with a fungal pest or of killing or inhibiting the growth of a fungal plant pest such as Alternaria, Ascochyta etc. (col. 255, lines 15-34). Wherein Verheesen’33 measures inhibiting fungal growth by growth of fungal spores (see Figure 8B, 8C, 8D, col. 11, lines 8).
Regarding claims 26 and 28, Verheesen’33 discloses a method of applying antifungal composition comprising VHH that binds to fungal plant pest (page 255, lines 15-34).
Regarding claim 27, Verheesen’33 discloses treatment to the harvested part of the plant i.e. post-harvest treatment.
Regarding claim 33, Verheesen’33 statements 12-13, col.12, lines 45-49 discloses their disclosed sequence comprises plant expressible promoter operably linked and statement 15 discloses a plant comprising the chimeric gene of statement 12-13 (col. 12, lines 45-53).
Thus Verheesen’33 anticipates the claims.
Response to Argument for Rejection
Applicant's arguments 03/19/2026 have been fully considered but they are not persuasive.
Applicant argues Applicant has amended claim 4 (from which claims 14, 15, 17, 26, 27, and 28 depend) and claim 29 (from which claim 33 depends) to be restricted to the specific sequences recited therein. Applicant argues claims 4 and 29 no longer encompass sequences having about 80% sequence identity (Response to Rejection, page 17, first paragraph).
Applicant argues Verheesen does not teach each and every element of the amended claims as Verheesen does not teach or suggest the specific recited sequences of the amended claims. Applicant argues the instant claims differ from the teachings of Verheesen with respect to the target to which the claimed VHHs bind. Applicant argues the VHHs according to the present invention do not bind glucosylceramide. Applicant argues rather, the claimed VHHs bind to a lipid-containing fraction of the plasma membrane of Botrytis cinerea obtained by fractionating hyphae by total lipid extract thin-layer chromatography and selecting the fraction having a Retention Factor (Rf) higher than the ceramide fraction and lower than the non-polar phospholipids fraction.
Applicant argues as described in Example 12 (page 80, lines 22-25), four fractions were identified:
(i) Fraction 1: the fraction of polar lipids;
(ii) Fraction 2: with a Retention Factor (Rf) similar to the glucosylceramide reference standard (GlcCer from Tamogitake), likely representing ceramides;
(iii) Fraction 3: having a slightly higher Rf than the reference standard; and
(iv) Fraction 4: the fraction of non-polar phospholipids.
Applicant argues Fraction 3 corresponds to the lipid fraction recited in the amended claims. Applicant argus importantly, the application demonstrates that the VHHs of the present invention do not bind Fraction 2 (see e.g., Figure 11), which is the fraction comprising glucosylceramide (GlcCer) (Response to Rejection, page 17, paragraphs 2-3).
Applicant argues unlike the VHH disclosed in Verheesen, the VHHs of the present invention do not bind glucosylceramide but instead bind a distinct lipid fraction.
Applicant's arguments have been fully considered but they are not persuasive since claims 4 and 29 step (f) does not require specific structure of the polypeptide and would require SEQ ID NO:17 with any number of substitutions resulting in increase in positive charge. Verheesen’33’s disclosed polypeptide comprises such positive charge and/or in alternative Goldman et al. teaches the mutation to a positively charged residue at certain position would increase the VHH binding to the fungus, see analysis above. Regarding argument on specific fragments Khan et al. teaches identifiable alternative fragment that comprise retention factor higher than a ceramide fraction and lower than non-polar phospholipid fraction therefore it would have been obvious to screen the variants of Verheesen’33’’s polypeptide for binding to the lipid containing fraction. Therefore, the rejection has been converted to 102 and/or 103 rejection, see analysis above.
Following analysis is added since applicant claims broader species of fungus than the dependent claim of claim 4 in the instant amendment.
Claim Rejections - 35 USC § 112 - improper dependent form
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claim 17 rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claim 17 recite the fungus is any of the fungus from genera Alternaria, Achocyta, Botrytis etc. which are broader than on the dependent claim 4 which recite binding to the specific of species of Botrytis cinerea.
Claims 26-28 recite any plant pathogenic fungus which is broader than the specific of species of Botrytis cinerea.
Therefore, the claims are in improper dependent form for failing to further limit the subject matter of the claim upon which it depends.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Obviousness type Nonstatutory Double Patenting over copending Application no. 18007317 and further in view of Goldman et al. and Khan et al.
Claims 4, 15, 17 and 29 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 6, 7 and 10 of copending Application No. 18007317 (Hereafter ‘317) (reference application) and further in view of Goldman et al. and Khan et al. Although the claims at issue are not identical, they are not patentably distinct from each other because:
Regarding claims 4 and 29, copending Application ‘317 claims 1, 6, 7 and 10 teaches a microbial host cell as VHH comprising or consisting of SEQ ID NO:43 (claim 10) wherein SEQ ID NO:43 and SEQ ID NO:44 has 96% and 95% sequence identity respectively to Applicant’s SEQ ID NO: 17. copending Application ‘317 claim 1 teaches the polypeptide is modified.
Therefore, copending Application ‘317 teaches the composition in the microbial host cell comprising SEQ ID NO:17. The capability to binding to a fungus would be the inherent property of the disclosed VHH.
Application ‘317 does not specifically teach the polypeptide comprise one or more substitutions leading to increased positive charge in comparison to SEQ ID NO:17.
Furthermore, Goldman et al. teaches the mutation to a positively charged residue at certain position would increase the VHH binding to the fungus Malassezia furfur, a fungus responsible for the formation of dandruff.
Furthermore, Verheesen’33’ teaches thin layer chromatography (THC) glucosylceramide (GLcCer) from Pleurotus citrinopileatus (col. 91, lines 45-50). Verheesen’33’ teaches the pest target to which their disclosed polypeptide would be plasma membrane component as phospholipid bilayer or any other protein therein. The plasma membrane component could be phospholipid, a glycoprotein, a carbohydrate or cholesterol (col. 59, lines 8-18). Furthermore Khan et al. teaches that the THC is used for separation and detection of non- polar and polar lipids from the skin tissue samples using retention factor (rf) values to separate specific lipids for example ceramide. Khan et al. teaches phospholipid comprise about 45% of total lipid in basal layers fraction of the THC. Khan et al. teaches THC is simple method of separation and quantification of skin lipids (page173, Abstract). Therefore, someone skilled in the art would choose the fraction with a Retention Factor (Rf) higher than the ceramide fraction and lower than the non-polar phospholipids fraction to find lipids that bind to the polypeptide.
Therefore someone skilled in the art before the effective date of filling of the invention from teaching suggestion and motivation of copending Application ‘317 would use the polypeptide of that is used in antifungal composition (i.e. antimicrobial) which would comprise many of the positively charged amino acids, and someone would create further variants that increase the positive charge since Goldman et al. suggested that the increase in positive charged residue would increase VHH binding to the lipid bin containing fraction of fungus B. cinerea. . Furthermore, it would have been obvious to try from different fraction t taught by Khan et al. and choose the fraction with a Retention Factor (Rf) higher than the ceramide fraction and lower than the non-polar phospholipids fraction.
Regarding claim 17, the binding to plasma membrane of B. cinerea would have been identified among the variants of SEQ ID NOs :43 or 44 of copending Application ‘317.
Regarding claims 15, Applicant defines " An "agrochemical composition" as used herein means a composition for agrochemical use, as further defined, comprising at least one active substance” (page 17, lines 18-21). Furthermore, applicant defines "Active substance", "active ingredient" or "active principle", as used interchangeably herein, means any biological, biochemical or chemical element and its derivatives, fragments or compounds based thereon, including micro-organisms, having general or specific action against harmful organisms on a subject, and in particular on plants, parts of plants or on plant products, as they occur naturally or by manufacture, including any impurity inevitably resulting from the manufacturing process (page 16, lines 18-22), therefore the SEQ ID NO:17 is an active substance that act against Botrytis cinerea as inherent property (see Figure 9).
Therefore, microbial host cell comprising SEQ ID NO:44 or 43 comprises the agrochemical composition.
Nonstatutory Double Patenting over copending Application no. 18007340 and further in view of Goldman et al. and Khan et al.
Claims 4, 15, 17 and 29 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 13, 16-18 of copending Application No. 18007340 (Hereafter ‘340) (reference application) and further in view of Goldman et al. and Khan et al. Although the claims at issue are not identical, they are not patentably distinct from each other because:
Regarding claims 4 and 29, copending Application ‘340 claims 13, 16-18 teaches a microbial host cell as VHH comprising or consisting of SEQ ID NO:1 wherein SEQ ID NO:1 and SEQ ID NO:2 has 96% and 96% sequence identity respectively to Applicant’s SEQ ID NO: 17.
Application ‘340 does not specifically teach the polypeptide comprise one or more substitutions leading to increased positive charge in comparison to SEQ ID NO:17.
Furthermore, Goldman et al. teaches the mutation to a positively charged residue at certain position would increase the VHH binding to the fungus Malassezia furfur, a fungus responsible for the formation of dandruff.
Furthermore, Verheesen’33’ teaches thin layer chromatography (THC) glucosylceramide (GLcCer) from Pleurotus citrinopileatus (col. 91, lines 45-50). Verheesen’33’ teaches the pest target to which their disclosed polypeptide bound would be plasma membrane component as phospholipid bilayer or any other protein therein. The plasma membrane component could be phospholipid, a glycoprotein, a carbohydrate or cholesterol (col. 59, lines 8-18). Furthermore Khan et al. teaches that the THC is used for separation and detection of non- polar and polar lipids from the skin tissue samples using retention factor (rf) values to separate specific lipids for example ceramide. Khan et al. teaches phospholipid comprise about 45% of total lipid in basal layers fraction of the THC. Khan et al. teaches THC is simple method of separation and quantification of skin lipids (page173, Abstract). Therefore, someone skilled in the art would choose the fraction with a Retention Factor (Rf) higher than the ceramide fraction and lower than the non-polar phospholipids fraction to find lipids that bind to the polypeptide.
Therefore someone skilled in the art before the effective date of filling of the invention from teaching suggestion and motivation of copending Application ‘340 would use the polypeptide of that is used in antifungal composition (i.e. antimicrobial) which would comprise many of the positively charged amino acids, and someone would create further variants that increase the positive charge since Goldman et al. suggested that the increase in positive charged residue would increase VHH binding to the lipid bin containing fraction of fungus B. cinerea. Furthermore, it would have been obvious to try from different fraction t taught by Khan et al. and choose the fraction with a Retention Factor (Rf) higher than the ceramide fraction and lower than the non-polar phospholipids fraction.
Regarding claim 17, , the binding to plasma membrane of Botrytis cinerea would have been identified among the variants of SEQ ID NOs :1 or 2 of copending Application ‘340.
Regarding claims 15, Applicant defines " An "agrochemical composition" as used herein means a composition for agrochemical use, as further defined, comprising at least one active substance” (page 17, lines 18-21). Furthermore, applicant defines "Active substance", "active ingredient" or "active principle", as used interchangeably herein, means any biological, biochemical or chemical element and its derivatives, fragments or compounds based thereon, including micro-organisms, having general or specific action against harmful organisms on a subject, and in particular on plants, parts of plants or on plant products, as they occur naturally or by manufacture, including any impurity inevitably resulting from the manufacturing process (page 16, lines 18-22), therefore the SEQ ID NO:17 is an active substance that act against Botrytis cinerea as inherent property (see Figure 9).
Therefore, microbial host cell comprising SEQ ID NOs: 1 or 2 would comprise the agrochemical composition.
Response to Argument for Rejection
Applicant's arguments 03/19/2026 have been fully considered but they are not persuasive.
Applicant argues the nonstatutory double patenting rejection be placed in abeyance until claims have actually issued or are deemed allowable in this application.
Applicant's arguments have been fully considered but they are not persuasive since it is not proper to hold any double patenting rejection in abeyance, and disagreeing with the analysis without providing any rationale for the disagreement is not an adequate response. Any future responses must include a terminal disclaimer or a proper traversal for each of the rejections or the response will be found non-responsive. See PTAB decision for application no. 12/089,270, mailed on April 19, 2018, which states that Applicant has an obligation to address double-patenting rejections before a Final Rejection, and the APJ points to 37 CFR 1.111(b) (PTAB Dec. p. 3, footnote).
Conclusion
No claim is 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.
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/SANTOSH SHARMA/Examiner, Art Unit 1663
/DAVID H KRUSE/Primary Examiner, Art Unit 1663
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