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 a Non-Provisional patent application, filed on 06/28/2024.
Claims 1-36 are currently pending in the instant application.
The claims set filed on 06/28/2024 is acknowledged.
Election/Restriction
Applicant's election without traverse of Group I, Claims 1-15, drawn to an engineered acid alpha-glucosidase, or biologically active fragment thereof, comprising an amino acid sequence having at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%, or more sequence identity to a reference sequence corresponding to residues 20 to 944 of SEQ ID NO: 12, or to a reference sequence corresponding to SEQ ID NO: 12, wherein the amino acid sequence comprises at least a substitution or amino acid residue 305V, 24A/C/D/F/G/H/I/K/MV/N/P/S/T/V/Y, 28A/C/D/E/F/G/H/K/Q/T/V/W, 29A/C/D/E/F/G/H/I/K/M/N/P/R/W/Y, 39A/E/F/G/I/L/N/T, 50A/C/D/E/F/H/I/K/M/N/R/S/T/W/Y, 62D/H/I/K/M/N/P/Q/Y, 78A/C/DG/H/IKL/M/N/Q/RS/T/V/W/Y, 87A/G/H/I/K/L/MN/Q/R/S/T/V/W, 135C/D/E/F/G/H/I/K/L/N/R/Y, 266A/D/E/H/K/Q, 267H/L/T/V, 437A/H, 486C/D/F/G/H/I/K/L/M/N/Q/R/S/V/W/Y, 522A/CDG/H/IKL/M/N/PQ/RS/T/W/Y, 569A/C/D/E/G/K/M/N/P/R/W, 670A/D/G/H/K/M/Y, 692A/D/E/H/K/L/M/N/T/W, 71 1D/E/I/K/Mv/N/Q/S/T/V/Y, 736F/L, 750E/K/L/Q/R, 81 2A/D/G/S, 830D/E/F/G/H/L/M/N/S/T/W/Y, 842A/C/D/F/H/K/L/M/N/Q/R/T/W, 87 1A/C/D/F/H/I/M/N/Q/T/V/W/Y, 883A/F/Q, 894A/D/E/H/I/K/L/M/N/S/T/V/W/Y, 91 3F/I/K/MV/N/S, or 932C/D/E/G/H/K/L/M/N/P/Q/R/W/Y, or combinations thereof, wherein the amino acid positions are relative to the reference sequence corresponding to residues 20 to 944 of SEQ ID NO: 12 or 2, or to a reference sequence corresponding to SEQIDNO: 12 or 2 in the response filed on 07/06/2026 is acknowledged.
Claims 16-36 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention, there being no allowable generic or linking claim.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 1-15 are present for examination.
Priority
Acknowledgement is made of applicants claim for priority of US Provisional application 63/511,347, filed on 6/030/2023.
Information Disclosure Statement
The information disclosure statements (IDSs) submitted on 01/05/2026, and 07/06/2026 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
Drawings submitted on 06/28/2024 are accepted by the Examiner.
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 1-15 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 SEQ ID NO: 12, 2, or 14 as it is unclear what the scope of activities that is encompassed by this term includes. On page 14 of the specification, applicants define the term “biologically active” as “having similar functions of a naturally occurring molecule”. As the number of naturally occurring molecules is vast, and the scope of possible biochemical functions is even broader with no clear boundaries of what these terms include, the scope of “biologically active fragments” of SEQ ID NO: 12, 2 or 14 is vague and indefinite.
Claims 1-15 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 1 is indefinite and vague in the recitation “24A/C/D/E……./T/V/Y…” in the context of SEQ ID NO: 12 or 2, which is confusing because it is not clear whether the applicants meant “24A or 24C, or 24D …” as alternatively, or a set of mutants separated by comma (,) such as 24A/C/D………T/V/Y”, which are unknown, rendering the Metes and Bounds of the term unclear, confusing and indefinite. Claim 2 is also rejected on the same ground. Clarification is required.
Claims 1-15 are rejected under 35 U.S.C. 112(b), as being indefinite and vague for failing to particularly point out and distinctly claim the subject matter which applicant regards as the invention. A broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) may be considered indefinite, since the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c). In the present instance, claim 1 recites the broad recitation 80%, and the claim also recites 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%, or more sequence identity, which is the narrower statement of the range/limitation. The claim(s) are considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims.
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, 5, 6-7, 8-14 and 15 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.
Claim(s) 1 and 2 are directed to an engineered acid alpha-glucosidase, or biologically active fragment thereof, comprising an amino acid sequence having at least 80%-84% 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%, or more sequence identity to a reference sequence corresponding to residues 20 to 944 of SEQ ID NO: 12, or to a reference sequence corresponding to SEQ ID NO: 12, wherein the amino acid sequence comprises at least a substitution or amino acid residue 305V, 24A/C/D/F/G/H/I/K/MV/N/P/S/T/V/Y, 28A/C/D/E/F/G/H/K/Q/T/V/W, 29A/C/D/E/F/G/H/I/K/M/N/P/R/W/Y, 39A/E/F/G/I/L/N/T, 50A/C/D/E/F/H/I/K/M/N/R/S/T/W/Y, 62D/H/I/K/M/N/P/Q/Y, 78A/C/DG/H/IKL/M/N/Q/RS/T/V/W/Y, 87A/G/H/I/K/L/MN/Q/R/S/T/V/W, 135C/D/E/F/G/H/I/K/L/N/R/Y, 266A/D/E/H/K/Q, 267H/L/T/V, 437A/H, 486C/D/F/G/H/I/K/L/M/N/Q/R/S/V/W/Y, 522A/CDG/H/IKL/M/N/PQ/RS/T/W/Y, 569A/C/D/E/G/K/M/N/P/R/W, 670A/D/G/H/K/M/Y, 692A/D/E/H/K/L/M/N/T/W, 71 1D/E/I/K/Mv/N/Q/S/T/V/Y, 736F/L, 750E/K/L/Q/R, 81 2A/D/G/S, 830D/E/F/G/H/L/M/N/S/T/W/Y, 842A/C/D/F/H/K/L/M/N/Q/R/T/W, 87 1A/C/D/F/H/I/M/N/Q/T/V/W/Y, 883A/F/Q, 894A/D/E/H/I/K/L/M/N/S/T/V/W/Y, 91 3F/I/K/MV/N/S, or 932C/D/E/G/H/K/L/M/N/P/Q/R/W/Y, or combinations thereof, wherein the amino acid positions are relative to the reference sequence corresponding to residues 20 to 944 of SEQ ID NO: 12 or 2, or to a reference sequence corresponding to SEQIDNO: 12 or 2, and a mutation 305V, and a composition comprising said variant of claim 1.
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 1 and 2, are drawn to any engineered acid alpha-glucosidase, or any biologically active fragment thereof, derived from many unknown sources having any structural feature comprising an amino acid sequence having at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%, or more sequence identity to a reference sequence corresponding to residues 20 to 944 of SEQ ID NO: 12, or to a reference sequence corresponding to SEQ ID NO: 12, wherein the amino acid sequence comprises at least a substitution or amino acid residue 305V, 24A/C/D/F/G/H/I/K/MV/N/P/S/T/V/Y, 28A/C/D/E/F/G/H/K/Q/T/V/W, 29A/C/D/E/F/G/H/I/K/M/N/P/R/W/Y, 39A/E/F/G/I/L/N/T, 50A/C/D/E/F/H/I/K/M/N/R/S/T/W/Y, 62D/H/I/K/M/N/P/Q/Y, 78A/C/DG/H/IKL/M/N/Q/RS/T/V/W/Y, 87A/G/H/I/K/L/MN/Q/R/S/T/V/W, 135C/D/E/F/G/H/I/K/L/N/R/Y, 266A/D/E/H/K/Q, 267H/L/T/V, 437A/H, 486C/D/F/G/H/I/K/L/M/N/Q/R/S/V/W/Y, 522A/CDG/H/IKL/M/N/PQ/RS/T/W/Y, 569A/C/D/E/G/K/M/N/P/R/W, 670A/D/G/H/K/M/Y, 692A/D/E/H/K/L/M/N/T/W, 71 1D/E/I/K/Mv/N/Q/S/T/V/Y, 736F/L, 750E/K/L/Q/R, 81 2A/D/G/S, 830D/E/F/G/H/L/M/N/S/T/W/Y, 842A/C/D/F/H/K/L/M/N/Q/R/T/W, 87 1A/C/D/F/H/I/M/N/Q/T/V/W/Y, 883A/F/Q, 894A/D/E/H/I/K/L/M/N/S/T/V/W/Y, 91 3F/I/K/MV/N/S, or 932C/D/E/G/H/K/L/M/N/P/Q/R/W/Y, or combinations thereof, wherein the amino acid positions are relative to the reference sequence corresponding to residues 20 to 944 of SEQ ID NO: 12 or 2, or to a reference sequence corresponding to SEQIDNO: 12 or 2, and a composition comprising said variant of claim 1, i.e., 20-24% non-identity to SEQ ID NO: 2 or 12, that encompasses many mutants, variant and fragments having alpha-glucosidase activity , 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 are 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 disclosed proteins. For example, proteins having similar structure 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 completely eliminates -ketoacyl synthase activity. Similarly, the art also teaches that functionally similar molecules have different structures; Kisselev L., (2002) teach that polypeptide release factors in prokaryotes and eukaryotes have same function but different structures.
Furthermore, the genus of polypeptides or variants 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 are adequately described by the disclosure of the structures of prior art, i.e., lipase variant enzymes. 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 in principle a fuzzy 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 disclosed proteins. For example, proteins having similar structure 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 completely eliminates -ketoacyl synthase activity. Similarly, the art also teaches that functionally similar molecules have different structures; Kisselev L., (2002) teach that polypeptide release factors in prokaryotes and eukaryotes have same function but different structures.
Claims are drawn to very broadly any engineered acid alpha-glucosidase wherein said glucosidase has: a) at least 80-84% but less than 100% sequence identity comprises a substitution corresponding to 305V in SEQ ID NO: 2, or 12 i.e., 20% non-identity to SEQ ID NO: 2, that encompasses many variant lipase enzymes derived from many unknown sources and many mutants, variants, and fragments thereof, which can have wide variety of unknown structures, which can have wide variety of unknown structures, whose structures are not fully described in the specification. No information, beyond the characterization of variant lipases enzymes 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 variant lipase enzymes, 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 enzymes (variant lipase) 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.
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 also 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, as the case may be, 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 1-7, 8-10, 11-14 and 15 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 Hallows et al. (Engineered acid alpha-glucosidase. US 2021/0189365A1, publication 06/24/2021, priority 62/951,625, filed on 12/19/2019, see IDS).
The Broadest Reasonable Interpretation (BRI) of claim 1, which is drawn to An engineered acid alpha-glucosidase, or biologically active fragment thereof, comprising an amino acid sequence having at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%, or more sequence identity to a reference sequence corresponding to residues 20 to 944 of SEQ ID NO: 12, or to a reference sequence corresponding to SEQ ID NO: 12, wherein the amino acid sequence comprises at least a substitution or amino acid residue 305V, 24A/C/D/F/G/H/I/K/MV/N/P/S/T/V/Y, 28A/C/D/E/F/G/H/K/Q/T/V/W, 29A/C/D/E/F/G/H/I/K/M/N/P/R/W/Y, 39A/E/F/G/I/L/N/T, 50A/C/D/E/F/H/I/K/M/N/R/S/T/W/Y, 62D/H/I/K/M/N/P/Q/Y, 78A/C/DG/H/IKL/M/N/Q/RS/T/V/W/Y, 87A/G/H/I/K/L/MN/Q/R/S/T/V/W, 135C/D/E/F/G/H/I/K/L/N/R/Y, 266A/D/E/H/K/Q, 267H/L/T/V, 437A/H, 486C/D/F/G/H/I/K/L/M/N/Q/R/S/V/W/Y, 522A/CDG/H/IKL/M/N/PQ/RS/T/W/Y, 569A/C/D/E/G/K/M/N/P/R/W, 670A/D/G/H/K/M/Y, 692A/D/E/H/K/L/M/N/T/W, 71 1D/E/I/K/Mv/N/Q/S/T/V/Y, 736F/L, 750E/K/L/Q/R, 81 2A/D/G/S, 830D/E/F/G/H/L/M/N/S/T/W/Y, 842A/C/D/F/H/K/L/M/N/Q/R/T/W, 87 1A/C/D/F/H/I/M/N/Q/T/V/W/Y, 883A/F/Q, 894A/D/E/H/I/K/L/M/N/S/T/V/W/Y, 91 3F/I/K/MV/N/S, or 932C/D/E/G/H/K/L/M/N/P/Q/R/W/Y, or combinations thereof, wherein the amino acid positions are relative to the reference sequence corresponding to residues 20 to 944 of SEQ ID NO: 12 or 2, or to a reference sequence corresponding to SEQIDNO: 12 or 2., i.e. 20% non-identical that encompasses many alpha-glucosidase enzymes and many mutants and variants thereof.
Regarding claims 1-7, 8-10, 11-14 and 15, Hallows et al. teach an engineered acid alpha-glucosidase (GAA) polypeptide of aa1-aa944, which is 100% identical to SEQ ID NO: 2, or 12 of the instant application, and likewise 100% identical to aa20 to aa944, and 99.9% identical to SEQ ID NO: 14 (see, sequence alignments as shown below) of the instant application, and comprises signal sequence , and a pharmaceutical compositions comprising the same, and the engineered GAA polypeptides have been optimized to provide increased expression, stability at neutral pH, and activity in cell lysates, wherein the methods for utilization of the compositions comprising the engineered GAA polypeptides for therapeutic and other purposes. Hallows et al. also teach a recombinant acid alpha glucosidase and/or biologically active recombinant acid alpha glucosidase fragment comprising an amino acid sequence comprising at least 80% to 99% sequence identity to SEQ ID NO: 2, 6, 8, 12, 14, 16, 18, 20, 946, 1956, 2496, 2880, and/or 3104, which are about 100% identical to SEQ ID NO: 2 or 12 of the instant application, wherein said recombinant acid alpha glucosidase comprises at least one substitution or substitution set at one or more positions selected from 112, 123, 124, 148, 188, 193, 197, 204, 253, 264, L305V, 312, 333, 381, 402, 402/781, 489, 489/944, 500/842, 500/932, 523, 527, 612, 612/725/944, 612/922, 614, 727, 742, 748, 820, 823, 832, 842/932, 858, 862, 911, 913, 914, 916, 923, 937, and 940, wherein said recombinant acid alpha glucosidase is purified, exhibits at least one of the characteristics selected from: i) enhanced catalytic activity; ii) increased tolerance to pH 7; iii) increased tolerance to pH 4; iv) increased expression; v) increased uptake into cells; vi) increased enzymatic activity in cell lysates; vii) reduced immunogenicity; or a combination of any of i), ii), iii), iv), v), v), and/or vii), as compared to a reference sequence, and a pharmaceutical composition comprising the same with acceptable carrier or excipient (see, whole document, in particular, title, abstract, para 13, 27, 107, 127, 129, Table 2, and claims 1-67).
RESULT 2
BJN39290
ID BJN39290 standard; protein; 944 AA.
DT 05-AUG-2021 (first entry)
XX
DE Human GAA protein mutant protein, SEQ 3104.
XX
KW GAA protein; acid maltase; alpha-1,4-glucosidase; chimeric protein;
KW enzyme engineering; enzyme production; fusion protein; glucoinvertase;
KW glucosidosucrase; lysosomal a-glucosidase; lysosomal alpha-glucosidase;
KW maltase; maltase-glucoamylase; metabolic-gen.; mutein; pompes disease;
KW prophylactic to disease; protein therapy; therapeutic.
XX
OS Homo sapiens.
OS Saccharomyces cerevisiae.
OS Chimeric.
OS Synthetic.
XX
CC PN US2021189365-A1.
XX
CC PD 24-JUN-2021.
XX
CC PF 18-DEC-2020; 2020US-00126647.
XX
PR 20-DEC-2019; 2019US-0951625P.
XX
CC PA (CODE ) CODEXIS INC.
XX
CC PI Lao JP, Vroom J, Silverman AP, Homan DW, Alaoui IMH, Huisman GW;
CC PI Dellas N, Chng C, Zhu Y, Botham RC, Hallows WC;
XX
DR WPI; 2021-70131Y/062.
DR N-PSDB; BJN39289.
XX
CC PT Recombinant acid alpha glucosidase used in composition of pharmaceutical
CC PT composition for treatment of Pompe disease by parenteral injection or
CC PT infusion to human, comprises biologically active recombinant acid alpha
CC PT glucosidase fragment.
XX
CC PS Claim 1; SEQ ID NO 3104; 128pp; English.
XX
CC The present invention relates to a novel recombinant acid alpha-
CC glucosidase (GAA) having an amino acid sequence of SEQ ID NO: 2, 6, 8,
CC 12, 14, 16, 18, 20, 946, 1956, 2496, 2880 and/or 3104 (see BJN36188,
CC BJN36192, BJN36194, BJN36198, BJN36200, BJN36202, BJN36204, BJN36206,
CC BJN37132, BJN38142, BJN38682, BJN39066 and/or BJN39290). The invention
CC further claims: (1) a composition comprising the recombinant GAA protein
CC (also known as lysosomal alpha-glucosidase, alpha-1,4-glucosidase, acid
CC maltase, glucoinvertase, glucosidosucrase, lysosomal alpha-glucosidase,
CC lysosomal a-glucosidase, maltase maltase-glucoamylase); (2) a recombinant
CC polynucleotide sequence encoding the recombinant GAA protein; (3) an
CC expression vector comprising the recombinant polynucleotide; (4) a host
CC cell comprising the expression vector; (5) a method for producing the
CC recombinant GAA protein variant; (6) a pharmaceutical composition
CC comprising the recombinant GAA protein; and (7) a method for treating
CC and/or preventing the symptoms of Pompe disease in a subject. The
CC recombinant GAA protein is useful in a composition for treating Pompe
CC disease. The present sequence is human GAA protein mutant
CC (R527N/T692G/W727S/L736M/A812E), which is useful in a composition for
CC treating Pompe disease.
XX
SQ Sequence 944 AA;
Query Match 99.9%; Score 5090; Length 944;
Best Local Similarity 99.9%;
Matches 943; Conservative 1; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MEWSWVFLFFLSVTTGVHSGHILWHDFSTVPRELSGSSQVLEETHPAHQVGASRPGPRDA 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MEWSWVFLFFLSVTTGVHSGHILWHDFSTVPRELSGSSQVLEETHPAHQVGASRPGPRDA 60
Qy 61 QLHPGRPRAVPTQCDVPENSRFDCAPEKAITQEQCEARGCCYIPAKQGLQGAQMGQPWCF 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 QLHPGRPRAVPTQCDVPENSRFDCAPEKAITQEQCEARGCCYIPAKQGLQGAQMGQPWCF 120
Qy 121 FPPSYPSYKLENLSQSEMGYTATLTRTTPSFFPKDILTLRLDVMMETENRLHFTIKDPAN 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 FPPSYPSYKLENLSQSEMGYTATLTRTTPSFFPKDILTLRLDVMMETENRLHFTIKDPAN 180
Qy 181 RRYEVPLETPHVHSRAPSPLYSVEFSEEPFGVIVRRQLDGRVLLNTTVAPLFFADQFLQL 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 RRYEVPLETPHVHSRAPSPLYSVEFSEEPFGVIVRRQLDGRVLLNTTVAPLFFADQFLQL 240
Qy 241 STSLPSQYITGLAEHLSPLMLSTSWNKITLWNRDLAPTPGANLYGSHPFYLALEDGGSAH 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 STSLPSQYITGLAEHLSPLMLSTSWNKITLWNRDLAPTPGANLYGSHPFYLALEDGGSAH 300
Qy 301 GVFLVNSNAMDVVLQPSPALSWRSTGGILDVYIFLGPEPKSVVQQYLDVVGYPFMPPYWG 360
||||:|||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 GVFLLNSNAMDVVLQPSPALSWRSTGGILDVYIFLGPEPKSVVQQYLDVVGYPFMPPYWG 360
Qy 361 LGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMV 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 LGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMV 420
Qy 421 QELHQGGRRYMMIVDPGISSSGPAGSYRPYDEGLRRGVFITNETGQPLIGKVWPGSTAFP 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 QELHQGGRRYMMIVDPGISSSGPAGSYRPYDEGLRRGVFITNETGQPLIGKVWPGSTAFP 480
Qy 481 DFTNPEALAWWEDMVAEFHDQVPFDGMWIDMNEPSNFIRGSVDGCPNNELENPPYVPGVV 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 DFTNPEALAWWEDMVAEFHDQVPFDGMWIDMNEPSNFIRGSVDGCPNNELENPPYVPGVV 540
Qy 541 GGTLQAATICASSHQFLSTHYNLHNLYGTTEAIA SHRALVKARGTRPFVISRSTFAGHGR 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 GGTLQAATICASSHQFLSTHYNLHNLYGTTEAIA SHRALVKARGTRPFVISRSTFAGHGR 600
Qy 601 YAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFY 660
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 601 YAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFY 660
Qy 661 PFMRNHNSLTSLPQEPYSFSEPAQQAMRKALGLRYALLPHLYTLFHQAHVHGETVARPLF 720
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 661 PFMRNHNSLTSLPQEPYSFSEPAQQAMRKALGLRYALLPHLYTLFHQAHVHGETVARPLF 720
Qy 721 LEFPKDSSTWTVDHQMLWGEALLITPVLQPGKAEVTGYFPLGTWYDLQTVPVEALGSLPP 780
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 721 LEFPKDSSTWTVDHQMLWGEALLITPVLQPGKAEVTGYFPLGTWYDLQTVPVEALGSLPP 780
Qy 781 PPAAPREPAIHSEGQWVTLPAPLDTINVHLREGYIIPLQGPGLTTTESRKQPMALAVALT 840
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 781 PPAAPREPAIHSEGQWVTLPAPLDTINVHLREGYIIPLQGPGLTTTESRKQPMALAVALT 840
Qy 841 KSGEARGELFWDDGESLEVLERGAYTQVIFEARNNTIVNELVHVTSEGAGLQLGKVTVLG 900
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 841 KSGEARGELFWDDGESLEVLERGAYTQVIFEARNNTIVNELVHVTSEGAGLQLGKVTVLG 900
Qy 901 VATAPQQVLSNGRPVSNFTYSPDTKVLDICVALLMGEQFLVSWC 944
||||||||||||||||||||||||||||||||||||||||||||
Db 901 VATAPQQVLSNGRPVSNFTYSPDTKVLDICVALLMGEQFLVSWC 944
Because the acid alpha-glucosidase polypeptide of the claimed invention and that of acid alpha-glucosidase polypeptide of the reference is one and the same, Examiner takes the position that the limitations of claims 5, 6, 7, 8, and 11 inherently associated or comprises with the acid alpha-glucosidase polypeptide of Hallows et al. Since the Office does not have the facilities for examining and comparing applicants' microorganism for producing or not producing recited chemicals by the prior art, the burden is on the applicant to show a novel or unobvious difference between the claimed product and the product 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.
Besides, While claims 5-15 recite products 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 acid alpha-glucosidase product as recited in claims 5-15 would be any different from the acid alpha-glucosidase of Hallows 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)
Therefore, Hallows et al. anticipate claims 1-7, 8-10, 11-14 and 15 of the instant application as written.
Conclusion
Status of the claims:
Claims 1-15 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.
Information regarding the status of an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see http://pair-direct.uspto.gov. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free).
Iqbal H. Chowdhury, PhD.
Primary Patent Examiner
Art Unit 1656 (Recombinant Enzymes and Protein Crystallography)
US Patent and Trademark Office (USPTO)
Ph. (571)-272-8137 and Fax (571)-273-8137
/IQBAL H CHOWDHURY/
Primary Examiner, Art Unit 1656
Prosecution Insights