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 .
DETAILED ACTION
Application Status
This application is 371 of PCT/US2023/060731, filed on 07/17/2024.
Claims 1-2, 7-8, 13-30, and 32 are currently pending in the instant application.
The preliminary amendment filed on 02/14/2025, amending claims 7, 13-15, 17, 19, 21, 24-27, 29-3, and 32, and canceling claims 3-6, 9-12, and 32 is acknowledged.
Election/Restriction
Applicant's election without traverse of Group I, Claims 1-2, 7-8, 13-19-20, 25-27 and 28, drawn to a recombinant polypeptide comprising a prodomain polypeptide linked to a catalytic polypeptide, wherein the catalytic polypeptide, or a biologically active fragment thereof, has an activity of proteolytic cleavage of SNAP25, VAMP2, VAMP7, and/or VAMP8, and composition comprising the same in the response filed on 07/23/2026 is acknowledged.
Claims 21-24, 29-30, and 32 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention, there being no allowable generic or linking claim.
Applicants request for rejoinder is noted. However, current claims of elected Group I are not allowable at this time. When Group I would be allowable, rejoinder request would be evaluated at that time.
The requirement is still deemed proper and is therefore made FINAL.
Claims 1-2, 7-8, 13-19-20, 25-27 and 28 are present for examination.
Priority
Acknowledgement is made of applicants claim for priority of US Provisional application 63/300,458, filed on 01/18/2022.
Information Disclosure Statement
The information disclosure statements (IDSs) submitted on 07/17/2024, 12/29/2025, and 04/01/2026 are acknowledged. The submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are considered by the examiner. The signed copies of 1449 are enclosed herewith.
Drawings
There is no Drawing with this application.
Claim Objections
Claim 1 is objected to in the recitation “SNAP25, VAMP2, VAMP7 and VAMP8” as abbreviations should not be used without at least once fully setting forth what they are used for. Appropriate correction is required.
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.
Claims 19 (depends on claim 1) and 20 are rejected under 35 U.S.C. 112(b), as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor, or for pre-AIA the applicant regards as the invention.
Claim 19 (depends on non-elected claim 1) recites the phrase “e.g.” renders the claim(s) indefinite because the claim(s) include(s) elements not actually disclosed (those encompassed by “e.g.”), thereby rendering the scope of the claim(s) unascertainable. See MPEP § 2173.05(d).
Claims 2, 8, 17, 18, and 20 are rejected under 35 U.S.C. 112(b), as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor, or for pre-AIA the applicant regards as the invention.
Claims 2, 8, 17, 18, and 20 are indefinite and vague in the recitation “an amino acid sequence” in the context various proteins, domains, and referred to respective SEQ ID NOs:”, which are confusing because “an amino acid sequence” under broadest reasonable interpretation (BRI), could be interpreted as “a fragment of the “polypeptide sequences”, which are unknown, rendering the metes and bounds of the term unclear. This rejection could be overcome by replacing “an amino acid sequence” with “the amino acid sequence” but will be withdrawn if the recitation “an amino acid sequence” is changed to “the amino acid sequence”. Clarification is required.
Claims 1-2, 7-8, 13-19-20, 25-27 and 28 are rejected under 35 U.S.C. 112(b), as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor, or for pre-AIA the applicant regards as the invention.
Claims 1 and 2 are indefinite in the recitation of “biologically active fragments” in the context of SNAP25, VAMP2, VAMP7 and VAMP8, or SEQ ID NO: 1, …… SEQ ID NO: 52, or SEQ ID NO: 2 ……SEQ ID NO: 53, as it is unclear what the scope of activities that is encompassed by this term “biologically active fragments”. On page 7 of the specification, applicants define the term “biologically active fragments” as “having similar proteolytic cleavage of SNARE protein as “SNARE -cleaving activity”. As the number of naturally occurring molecules is vast, and the scope of possible s biochemical functions is even broader with no clear boundaries of what these terms include, the scope of “biologically active fragments” of SNAP25, VAMP2, VAMP7 and VAMP8, or SEQ ID NO: 1, …… SEQ ID NO: 52, or SEQ ID NO: 2 ……SEQ ID NO: 53 is vague and indefinite. Applicants are advised to look at other claims for similar limitations as of claims 1 and 2.
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.
A. Written Description
Claims 1-2, 7-8, 13-19-20, 25-27 and 28 are rejected under 35 U.S.C. 112(a), 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claims 1 and 25, are directed to a recombinant polypeptide comprising a prodomain polypeptide linked to a catalytic polypeptide, wherein the catalytic polypeptide, or a biologically active fragment thereof, has an activity of proteolytic cleavage of SNAP25, VAMP2, VAMP7, and/or VAMP8, and composition comprising the same.
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.” University of California v. Eli Lilly and Co., 1997 U.S. App. LEXIS 18221, at *23, quoting Fiers v. Revel, 25 USPQ2d 1601, 1606 (Fed. Cir. 1993). To fully describe a genus of genetic material, which is a chemical compound, applicants must (1) fully describe at least one species of the claimed genus sufficient to represent said genus whereby a skilled artisan, in view of the prior art, could predict the structure of other species encompassed by the claimed genus and (2) identify the common characteristics of the claimed molecules, e.g., structure, physical and/or chemical characteristics, functional characteristics when coupled with a known or disclosed correlation between function and structure, or a combination of these (paraphrased from Enzo Biochemical).
Thus, Claims are drawn to any recombinant polypeptide derived from any unknown sources having no structural feature, comprising any prodomain polypeptide derived from any unknown sources having no structural feature, linked to any catalytic polypeptide, wherein the catalytic polypeptide, or a biologically active fragment thereof, derived from any unknown sources having no structural feature, has an activity of proteolytic cleavage of SNAP25, VAMP2, VAMP7, and/or VAMP8, and a composition comprising the same, i.e., claimed any recombinant polypeptide or any prodomain polypeptide derived from any unknown sources having no structural feature, that encompasses many recombinant polypeptide or any prodomain polypeptide derived from many unknown sources and many mutants, variants, and fragments thereof, which can have wide variety of unknown structures, i.e. No Structure-Function correlation, which is required to fulfill the Written Description (WD) requirement.
As discussed in the written description guidelines 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 the applicant was in possession of the claimed genus. 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.
Furthermore, the genus of polypeptides required in the claimed invention is an extremely large structurally and functionally variable genus. While the argument can be made that the recited genus of polypeptides is adequately described by the disclosure of the structures of prior art. However, the art clearly teaches the “Practical Limits of Function Prediction”: Whisstock et al., (2003) highlight the difficulties associated with “Prediction of protein function from protein sequence and structure”; “To reason from sequence and structure to function is to step onto much shakier ground”, closely related proteins can change function, either through divergence to a related function or by recruitment for a very different function, in such cases, assignment of function on the basis of homology, in the absence of direct experimental evidence, will give the wrong answer, it is difficult to state criteria for successful prediction of function, since function is a vague concept. This finding is reinforced in the following scientific teachings for specific proteins in the art that suggest, even highly structurally homologous polypeptides do not necessarily share the same function, and many functionally similar proteins will have little or no structural homology to disclose proteins. For example, proteins having similar structures have different activities (structure does not always correlate to function); Witkowski et al., (1999) teaches that one conservative amino acid substitution transforms a -ketoacyl synthase into a malonyl decarboxylase and celiminates-ketoacyl synthase activity. Similarly, the art also teaches that functionally similar molecules have different structures; Kisselev L. (2002) teaches that polypeptide release factors in prokaryotes and eukaryotes have same function but different structures.
Claims are drawn to very broadly any recombinant polypeptide derived from any unknown sources having no structural feature, comprising any prodomain polypeptide derived from any unknown sources having no structural feature, linked to any catalytic polypeptide, wherein the catalytic polypeptide, or a biologically active fragment thereof, derived from any unknown sources having no structural feature, has an activity of proteolytic cleavage of SNAP25, VAMP2, VAMP7, and/or VAMP8, and a composition comprising the same, i.e., claimed any recombinant polypeptide or any prodomain polypeptide derived from any unknown sources having no structural feature, that encompasses many recombinant polypeptide or any prodomain polypeptide derived from many unknown sources and many mutants, variants, and fragments thereof, which can have wide variety of unknown structures, whose structures are not fully described in the specification. No information, beyond the characterization of few recombinant polypeptides and prodomain polypeptide has been provided, which would indicate that applicants had possession of the claimed genus. The specification does not contain sufficient disclosure of the structure with function of all the recombinant polypeptide, and prodomain polypeptide, within the scope of the claimed genus. The genus of polypeptides claimed is a large variable genus including many mutants, variant and fragments thereof, which can have wide variety of structures. Therefore, many structurally unrelated polypeptides within the scope of these claims. The specification discloses the structure of only few representative species of the claimed genus, which is insufficient to put one of skill in the art in possession of the attributes and features of all species within the claimed genus. Therefore, one skilled in the art cannot reasonably conclude that applicant had possession of the claimed invention at the time the instant application was filed.
Claims 2, 8, 17, 18, and 20 are also included in this rejection because of the recitation “an amino acid sequence” (see, 112(b) rejection) but will be withdrawn if the recitation “an amino acid sequence” is changed to “the amino acid sequence”.
Applicant is referred to the revised guidelines concerning compliance with the written description requirement of U.S.C. 112, first paragraph, published in the Official Gazette and available at www.uspto.gov.
Claim Rejections - 35 USC § 102
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 for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 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 names another inventor and was effectively filed before the effective filing date of the claimed invention.
MPEP-2131 Anticipation — Application of 35 U.S.C. 102 [R-08.2017]
A claimed invention may be rejected under 35 U.S.C. 102 when the invention is anticipated (or is "not novel") over a disclosure that is available as prior art. To reject a claim as anticipated by a reference, the disclosure must teach every element required by the claim under its broadest reasonable interpretation. See, e.g., MPEP § 2114, subsections II and IV.
"A claim is anticipated only if each and every element as set forth in the claim is found, either expressly or inherently described, in a single prior art reference." Verdegaal Bros. v. Union Oil Co. of California, 814 F.2d 628, 631, 2 USPQ2d 1051, 1053 (Fed. Cir. 1987). "When a claim covers several structures or compositions, either generically or as alternatives, the claim is deemed anticipated if any of the structures or compositions within the scope of the claim is known in the prior art." Brown v. 3M, 265 F.3d 1349, 1351, 60 USPQ2d 1375, 1376 (Fed. Cir. 2001) Note that, in some circumstances, it is permissible to use multiple references in a 35 U.S.C. 102 rejection. See MPEP § 2131.01.
MPEP-2131.01 Multiple Reference 35 U.S.C. 102 Rejections [R-11.2013]
Normally, only one reference should be used in making a rejection under 35 U.S.C. 102. However, a 35 U.S.C. 102 rejection over multiple references has been held to be proper when the extra references are cited to:
(A) Prove the primary reference contains an "enabled disclosure;"
(B) Explain the meaning of a term used in the primary reference; or
(C) Show that a characteristic not disclosed in the reference is inherent.
Claims 1-2, 7, 8, 13, 14, 15, 16, 17, 18-19-20, 25-27 and 28 are rejected under 35 U.S.C. 102(a)(1) based upon a public use or sale or other public availability of the invention as anticipated by Fetcher et al. (Fast acting snare-cleaving enzymes. US 2012/0225049A1, publication 09/06/2012, see IDS).
The Broadest Reasonable Interpretation (BRI) of claims 1 and 25, which are directed to a recombinant polypeptide comprising a prodomain polypeptide linked to a catalytic polypeptide, wherein the catalytic polypeptide, or a biologically active fragment thereof, has an activity of proteolytic cleavage of SNAP25, VAMP2, VAMP7, and/or VAMP8, and composition comprising the same.
Regarding claims 1-2, 7, 8, 13, 14, 15, 16, 17, 18-19-20, 25-27 and 28, Fletcher et al. teach metalloprotease enzymes isolated from scorpion venom, which is 49.3% (upper image) amino acid identity to SEQ ID NO: 1 and 41.3% (lower image) identity to SEQ ID NO: 6 of the instant application, see sequence alignment as SnagIt image as shown below), that cleave SNARE complex proteins, their nucleic acid and amino acid sequences, and methods of use thereof in the treatment of various diseases, disorders and cosmetic conditions, wherein said metalloprotease enzymes inherently comprises N-terminal signal sequence, and pro-domain , N-terminal signal sequence in front of pro-domain (see, Sternlicht et al._2001, whole document, as evidence), wherein the SNARE proteins incudes SNAP25, VAMP2, VAMP3, and VAMP8, wherein said metalloprotease comprises three catalytic sites or centers for catalysis for cleaving SNARE proteins, wherein said metalloprotease is overexpressed in a E. coli bacterial cell by plasmid or vector for overexpression, and said metalloprotease was isolated and purified for SNARE cleaving functions. Fletcher et al. also teach composition comprising the metalloprotease enzyme in pyrogen-free water with pharmaceutically acceptable carrier, wherein the carrier is also creams (abstract, para 2, 3-5, 10-11, 16, 43, 59, 65, 81, 87, 92, 94, 141, 168, 169).
Claims 2, 8, 17, 18, and 20 are also included in this rejection because of the recitation “an amino acid sequence” (see, 112(b) rejection), but the rejection will be withdrawn if the recitation “an amino acid sequence” is changed to “the amino acid sequence”.
While claims 13-15, 19, recite products (metalloprotease) in product by process form, patentability of a product by process claim is determined by the characteristics of the product only. As there is no evidence that the degraded starch molecules product as recited in claims 13-15, 19 would be any different from the degraded starch molecules recited by the Fletcher et al. see, MPEP 2113:
2113 Product-by-Process Claims [R-08.2017]
I. PRODUCT-BY-PROCESS CLAIMS ARE NOT LIMITED TO THE MANIPULATIONS OF THE RECITED STEPS, ONLY THE STRUCTURE IMPLIED BY THE STEPS
“[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.” In re Thorpe, 777 F.2d 695, 698, 227 USPQ 964, 966 (Fed. Cir. 1985)
The recombinant E. coli microorganism of Fletcher et al. inherently comprise a pro-domain as evidenced by Thomas et al._2009. Since Fletcher et al. (inventor of the instant application) discloses the same recombinant metalloprotease enzyme with same scope of the instant application, are the inherent present in the metalloprotease of the Fletcher et al. Since the Office does not have the facilities for examining and comparing applicants' enzyme for cleaving SNARE proteins or peptides by the prior art, the burden is on the applicant to show a novel or unobvious difference between the claimed enzyme and the enzyme of the prior art. See In re Best, 562 F.2d 1252, 195 USPQ 430 (CCPA 1977) and in re Fitzgerald et al., 205 USPQ 594.
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Therefore, Fletcher et al. anticipate claims 1-2, 7, 8, 13, 14, 15, 16, 17, 18-19-20, 25-27 and 28 of the instant application as written.
Claim Rejections - 35 U.S.C. § 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 should not be negated by the way the invention was made.
The factual inquiries set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of 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 is currently called 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.
According to MPEP 2143:
“Exemplary rationales that may support a conclusion of obviousness include:
(A) Combining prior art elements according to known methods to yield
predictable results.
(B) Simple substitution of one known element for another to obtain predictable
results.
(C) Use of known techniques to improve similar devices (methods, or products)
in the same way.
(D) Applying a known technique to a known device (method, or product) ready
for improvement to yield predictable results.
(E) “Obvious to try” – choosing from a finite number of identified, predictable solutions, with a reasonable expectation of success.
(F) Known work in one field of endeavor may prompt variations of it for use in
either the same field or a different one based on design incentives or other market
forces if the variations are predictable to one of ordinary skill in the art.
(G) Some teaching, suggestions, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art
reference teachings to arrive at the claimed invention.
Note that the list of rationales provided is not intended to be an all-inclusive list. Other rationales to support a conclusion of obviousness may be relied upon by Office personnel.
Claims 1-2, 7, 8, 13, 14, 15, 16, 17, 18-19-20, 25-27 and 28 are rejected under 35 U.S.C. 103 as being unpatentable over Fetcher et al. (Fast acting snare-cleaving enzymes. US 2012/0225049A1, publication 09/06/2012, see IDS) as applied to claims 1-2, 7, 8, 13, 14, 15, 16, 17, 18-19-20, 25-27 and 28 above, and further in view of Sternlicht et al. (How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol (2001), 17: 463-516), and Weldon et al. (Designing furin-cleavable linker in recombinant immunotoxins based on Pseudomonas exotoxin A. Bioconjugate Chem (2015), 26(6): 1120-1128, internal page 1-21).
Regarding claims 1-2, 7, 8, 13, 14, 15, 16, 17, 18-19-20, 25-27 and 28, Fletcher et al. teach metalloprotease enzymes isolated from scorpion venom, which is 49.3% (upper image) amino acid identity to SEQ ID NO: 1 and 41.3% (lower image) identity to SEQ ID NO: 6 of the instant application, see sequence alignment as SnagIt image as shown below), that cleave SNARE complex proteins, their nucleic acid and amino acid sequences, and methods of use thereof in the treatment of various diseases, disorders and cosmetic conditions, wherein said metalloprotease enzymes inherently comprises N-terminal signal sequence, and pro-domain , N-terminal signal sequence in front of pro-domain (see, Sternlicht et al._2001, whole document, as evidence), wherein the SNARE proteins incudes SNAP25, VAMP2, VAMP3, and VAMP8, wherein said metalloprotease comprises three catalytic sites or centers for catalysis for cleaving SNARE proteins, wherein said metalloprotease is overexpressed in a E. coli bacterial cell by plasmid or vector for overexpression, and said metalloprotease was isolated and purified for SNARE cleaving functions. Fletcher et al. also teach composition comprising the metalloprotease enzyme in pyrogen-free water with pharmaceutically acceptable carrier, wherein the carrier is also creams (abstract, para 2, 3-5, 10-11, 16, 43, 59, 65, 81, 87, 92, 94, 141, 168, 169).
Claims 2, 8, 17, 18, and 20 are also included in this rejection because of the recitation “an amino acid sequence” (see, 112(b) rejection), but the rejection will be withdrawn if the recitation “an amino acid sequence” is changed to “the amino acid sequence”.
The recombinant E. coli microorganism of Fletcher et al. inherently comprises a pro-domain as evidenced by Sternlicht et al._2001. Since Fletcher et al. (inventor of the instant application) discloses the same recombinant metalloprotease enzyme with same scope of the instant application, are the inherent present in the metalloprotease of the Fletcher et al. Since the Office does not have the facilities for examining and comparing applicants' enzyme for cleaving SNARE proteins or peptides by the prior art, the burden is on the applicant to show a novel or unobvious difference between the claimed enzyme and the enzyme of the prior art. See In re Best, 562 F.2d 1252, 195 USPQ 430 (CCPA 1977) and In re Fitzgerald et al., 205 USPQ 594.
While claims 13-15, 19, recite products (metalloprotease) in product by process form, patentability of a product by process claim is determined by the characteristics of the product only. As there is no evidence that the degraded starch molecules product as recited in claims 13-15, 19 would be any different from the degraded starch molecules recited by the Fletcher et al. see, MPEP 2113:
2113 Product-by-Process Claims [R-08.2017]
I. PRODUCT-BY-PROCESS CLAIMS ARE NOT LIMITED TO THE MANIPULATIONS OF THE RECITED STEPS, ONLY THE STRUCTURE IMPLIED BY THE STEPS
“[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.” In re Thorpe, 777 F.2d 695, 698, 227 USPQ 964, 966 (Fed. Cir. 1985)
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Fletcher et al. do not teach recombinant protease polypeptide comprises an N-terminal prodomain and a signal peptide before the pro-domain (for claim 1, 7),
However, Sternlicht et al. teach a metalloproteinase (synonym: metalloprotease) comprises N-terminal prodomain and a signal sequence (pre-domain) which is N-terminal to catalytic domain (see, pg 3, para 4, and pg 4, para 1).
Fletcher et al. and Sternlicht et al. do not teach that a linker contains a cleavage site (for claim 15).
However, Weldon et al. teach that designing furin-cleavable linker in recombinant immunotoxins based on Pseudomonas exotoxin A, to be used as a therapeutic agent for the treatment of cancers by engineering the toxin to target malignant cells (see, Title, abstract, page 2, para 2, and see, SnagIt image).
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Therefore, it would have been obvious to one of ordinary skill in the art to arrive at the claimed invention as a whole before the effective filing date of the invention was made by combining the teachings of Fletcher et al., Sternlicht et al., and Weldon et al. about the prodomain of metalloprotease, which is universally present resulting in an inactive metalloprotease as taught by Sternlicht et al. and using Deng et al. to use furin-cleavable linker as taught by Weldon et al.in the recombinant metalloprotease of Fletcher et al., and modify Fletcher et al. to make a recombinant metalloprotease comprising prodomain, signal sequence and a furin-cleavable linker for using in the development of therapeutics against cancer, COVID, AIDS, and genetical diseases to arrive the claimed invention.
One of ordinary skilled in the art would have been motivated to use furin-cleavable linker to overexpress recombinant metalloprotease comprising prodomain, signal sequence and a furin-cleavable linker for using in the development of therapeutics against cancer, COVID, AIDS, and genetical diseases which is therapeutically, clinically pharmaceutically and financially beneficial.
One of ordinary skilled in art would have a reasonable expectation of success because Fletcher could make a recombinant metalloprotease comprising prodomain, signal sequence and a furin-cleavable linker.
Thus, the above references render the claims prima facie obvious to one of ordinary skill in the art.
Therefore, Fletcher et al. anticipate claims 1-2, 7, 8, 13, 14, 15, 16, 17, 18-19-20, 25-27 and 28 of the instant application as written.
Double Patenting Rejection
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. See 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); and 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) may be used to overcome an actual or provisional rejection based on a nonstatutory double patenting ground provided the conflicting application or patent is shown to be commonly owned with this application. See 37 CFR 1.130(b).
Effective January 1, 1994, a registered attorney or agent of record may sign a terminal disclaimer. A terminal disclaimer signed by the assignee must fully comply with 37 CFR 3.73(b).
Claims 1-2, 7, 8, 13, 14, 15, 16, 17, 18-19-20, 25-27 and 28 are rejected under the judicially created doctrine of obviousness-type double patenting as being unpatentable over at least claims 1-8 of US patent 9149666 B2, patent granted 10/06/2015).
Although the conflicting claims are not identical, they are not patentably distinct from each other because claims of the instant application are directed to a recombinant polypeptide comprising a prodomain polypeptide linked to a catalytic polypeptide, wherein the catalytic polypeptide, or a biologically active fragment thereof, has an activity of proteolytic cleavage of SNAP25, VAMP2, VAMP7, and/or VAMP8, wherein the prodomain polypeptide comprises an amino acid sequence selected from the group consisting of SEQ ID NO:1, SEQ ID NO:18, SEQ ID NO:35, SEQ ID NO:52, and a biologically active fragment of any of the foregoing, and/or the catalytic polypeptide comprises an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:19, SEQ ID NO:36, SEQ ID NO:53, and a biologically active fragment of any of the foregoing, wherein the recombinant polypeptide of claim 1, further comprising a signal peptide attached to the N-terminus of the prodomain polypeptide, wherein the signal peptide comprises an amino acid sequence selected from the group consisting of SEQ ID NO:3, SEQ ID NO:20, SEQ ID NO:37, and SEQ ID NO:54, wherein the recombinant polypeptide further comprises a linker attached to the C-terminus of the prodomain polypeptide and the N-terminus of the catalytic polypeptide, when the linker is attached to the C-terminus of the prodomain, at least one amino acid residue of the last ten amino acids of the C-terminus of the prodomain polypeptide is absent, wherein the linker comprises an amino acid sequence that is cleavable by an enzyme, wherein the enzyme is a protease, wherein the linker comprises an amino acid sequence selected from the group consisting of SEQ ID NO:69, SEQ ID NO:70, SEQ ID NO:71, SEQ ID NO:72, SEQ ID NO:73, SEQ ID NO:74, and SEQ ID NO:75, wherein the recombinant polypeptide has an amino acid sequence of any one of SEQ ID NOS:6-17, 23-34, 40-51, and 57-68, wherein the recombinant polypeptide of claim 1, further comprising a purification tag attached to the N-terminus of the prodomain polypeptide or a signal peptide, when present, wherein the purification tag is optionally connected to the N-terminus of the prodomain polypeptide or signal peptide through a linker.
The claims 1-3, 5, 12-13 and 14 of the US patent 9149666 B2 disclose an isolated polypeptide comprising an amino acid sequence selected from the group consisting of (1) SEQ ID NO:1, (2) SEQ ID NO:2, (3) SEQ ID NO:3, (4) SEQ ID NO:4, (5) a combination of SEQ ID NO:5 and SEQ ID NO:6, and (6) a combination of SEQ ID NO:7 and SEQ ID NO:8, or a biologically active fragment thereof, wherein the isolated polypeptide is a 6-His fusion polypeptide having the activity of proteolytic cleavage of SNAP25, VAMP2 and VAMP8, and a composition comprising the isolated polypeptide of claim 1 in a pharmaceutically acceptable carrier, wherein the pharmaceutically acceptable carrier comprises sterile pyrogen-free water and/or sterile pyrogen-free physiological saline solution, wherein the isolated polypeptide of claim 1 comprising a cosmetically acceptable carrier, wherein the cosmetically acceptable carrier is in the form of a spray, an emulsion, a mousse, a liquid, a cream, an oil, a lotion, an ointment, a gel or a solid.
The above indicated claim(s) of the reference patent, while not totally identical to the instant claims, are indeed a product claim of a recombinant polypeptide comprising a prodomain polypeptide linked to a catalytic polypeptide, wherein the catalytic polypeptide, or a biologically active fragment thereof, has an activity of proteolytic cleavage of SNAP25, VAMP2, VAMP7, and/or VAMP8.
Claims of the instant application listed above cannot be considered patentably distinct over claims of the reference patents when there are specifically recited embodiments that would either anticipate to claims 1-2, 7, 8, 13, 14, 15, 16, 17, 18-19-20, 25-27 and 28 of the instant application or alternatively render them obvious. Alternatively, claims 1-2, 7, 8, 13, 14, 15, 16, 17, 18-19-20, 25-27 and 28 cannot be considered patentably distinct over claims of the reference patent when there is specifically disclosed embodiment in the instant application that falls within the scope of claims of US patent 9149666 B2, i.e. there is substantially overlapping scope between the claimed invention and the teachings of the reference. One having ordinary skill in the art would have been motivated to do this because that embodiment is disclosed in the specification and in the claims as being a preferred embodiment within the claims 1-3, 5, 12-13 and 14 of the US patent 9149666 B2 as well as the specification.
Conclusion
Status of the claims:
Claims 1-2, 7-8, 13-19-20, 25-27 and 28 are rejected.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to IQBAL H CHOWDHURY whose telephone number is (571)272-8137. The examiner can normally be reached on M-F, at 9:00-5:00 PM.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Manjunath N. Rao, can be reached on 571-272-0939. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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Iqbal H. Chowdhury, Primary Patent Examiner
Art Unit 1656 (Recombinant Enzymes and Protein Crystallography)
US Patent and Trademark Office
Ph. (571)-272-8137 and Fax (571)-273-8137
/IQBAL H CHOWDHURY/
Primary Examiner, Art Unit 1656
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