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 .
1. The Election filed May 11, 2026, in response to the Office Action of November 10, 2025, is acknowledged and has been entered. Applicants elected without traverse \ the species of:
A. sialidase having a substitution at position A42 of wild-type human Neu2(A42);
B. sialidase further comprising a substitution of valine residue at position 6 of wild-type human Neu2 (V6);
C. sialidase Neu2(A42) SEQ ID NO:198; and
D. fusion protein comprising SEQ ID NO:205 that comprises sialidase Neu2(A42) SEQ ID NO:198 and fused to trastuzumab heavy chain.
Claims 1-4, 7, 11, 15, 16, 18-20, 24, 27, 28, 30, 32-36, 45, 46, 53-57 are pending. Claims 1-4 and 18 are withdrawn as being drawn to non-elected species. Claims 7, 11, 15, 16, 19, 20, 24, 27, 28, 30, 32-36, 45, 46, 53-57 are currently under prosecution as drawn to the elected species.
Claim Rejections - 35 USC § 112
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.
2. Claims 11, 15, 16, 19, 20, 24, and 46 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claims 11, 15, 16, 19, 20, and 24 all depend from claim 7. Claim 7 recites: “A recombinant mutant human sialidase enzyme” and “wild-type human Neu2” which is also a sialidase and an enzyme.
Dependent claims 11 and 15 refer to “The enzyme of claim 7, wherein, in the sialidase…” or “The enzyme of claim 7, wherein the sialidase…”. It is unclear which enzyme and sialidase the claims are referencing from claim 7.
Claim 16 refers to “The enzyme of claim 15, wherein, in the sialidase…”
Claim 19 refers to “The enzyme of claim 7, wherein the sialidase is…”
Claim 20 recites “The enzyme of claim 19, wherein the sialidase is…”
Claim 24 recites “The enzyme of claim 7, wherein the sialidase comprises…”
For the same reasoning applied to claims 11 and 15, it is unclear which enzyme and sialidase claims 16, 19, 20, and 24 are referencing.
Claim 46 recites: “The antibody conjugate of claim 45, wherein the third polypeptide comprises the sialidase and the immunoglobulin Fc domain in an N-to C-terminal orientation”. Claim 45 encompasses both “a sialidase” and the recombinant enzyme of claim 7 that is also a sialidase. Claim 45 is unclear with regard to which sialidase is being referenced.
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.
3. Claims 7, 11, 15, 16, 19, 20, 27, 28, 30, 32-34, 36, 45, 46, 53-57 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention. This is a WRITTEN DESCRIPTION rejection.
Claim 7 is drawn to a recombinant mutant human sialidase enzyme, wherein the sialidase comprises a substitution of alanine residue at position 42 of wild-type human Neu2 (A42).
Claim 7 does not identify the sequence structure of the “recombinant mutant human sialidase enzyme” that “comprises a substitution of alanine residue that corresponds to position 42 of wild-type human Neu2” because the claimed enzyme is not required to comprise the sequence of wild-type human Neu2 or any corresponding sequence thereof, other than a substitution of one alanine amino acid that may “correspond to position 42 of wild-type human Neu2” by simply being any residue other than an alanine residue.
Claim 11 further defines the alanine at position corresponding to position 42 of wild-type human Neu2 is substituted by arginine (A42R), but does not identify the sequence structure of the claimed recombinant mutant human sialidase enzyme.
Claim 15 recites the sialidase further comprises a substitution of valine residue at a position corresponding to position 6 of wild-type human Neu2 (V6), but does not recite the sequence structure of the sialidase comprising a substitution of valine residue at a position corresponding to position 6 of wild-type human Neu.
Claim 16 further defines the valine residue at a position corresponding to position 6 of wild-type human Neu2 is substituted by tyrosine (V6Y) but does not recite the sequence structure of the sialidase comprising a substitution.
Claims 19 and 20 recite that the sialidase is human and is Neu2, but do not recite the sequence structure of the recombinant sialidase enzyme.
Dependent claims 27, 28, 30, 32-34, 36, 45, 46, 53-57 also fail to recite the sequence structure of the recombinant sialidase enzyme.
Thus, the claims encompass a vast genus of recombinant mutant human sialidase enzymes comprising any unknown sequence structure, and further comprising an Arg and Tyr residue.
With regard to the genus of recombinant mutant sialidases, the instant specification discloses:
I. Recombinant Human Sialidases
[0077] As used herein, the term “sialidase” refers to any enzyme, or a functional fragment thereof, that cleaves a terminal sialic acid residue from a substrate, for example, a glycoprotein or a glycolipid. The term sialidase includes variants having one or more amino acid substitutions, deletions, or insertions relative to a wild-type sialidase sequence, and/or fusion proteins or conjugates including a sialidase. Sialidases are also called neuraminidases, and, unless indicated otherwise, the two terms are used interchangeably herein. As used herein, the term “functional fragment” of a sialidase refers to fragment of a full-length sialidase that retains, for example, at least 10%, at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, or 100% of the enzymatic activity of the corresponding full-length, naturally occurring sialidase. Sialidase enzymatic activity may be assayed by any method known in the art, including, for example, by measuring the release of sialic acid from the fluorogenic substrate 4-methylumbelliferyl-N-acetylneuraminic acid (4MU-NeuAc). In certain embodiments, the functional fragment comprises at least 100, 150, 200, 250, 300, 310, 320, 330, 340, 350, 360, or 370 consecutive amino acids present in a full-length, naturally occurring sialidase.
[0078] Four sialidases have been found in the human genome and are referred to as Neu1, Neu2, Neu3 and Neu4.
[0079] Human Neu1 is a lysosomal neuraminidase enzyme which functions in a complex with beta-galactosidase and cathepsin A. The amino acid sequence of human Neu1 is depicted in SEQ ID NO: 7, and a nucleotide sequence encoding human Neu1 is depicted in SEQ ID NO: 23.
[0080] Human Neu2 is a cytosolic sialidase enzyme. The amino acid sequence of human Neu2 is depicted in SEQ ID NO: 1, and a nucleotide sequence encoding human Neu2 is depicted in SEQ ID NO: 24. Unless stated otherwise, as used herein, wild-type human Neu2 refers to human Neu2 having the amino acid sequence of SEQ ID NO: 1.
[0081] Human Neu3 is a plasma membrane sialidase with an activity specific for gangliosides. Human Neu3 has two isoforms: isoform 1 and isoform 2. The amino acid sequence of human Neu3, isoform 1 is depicted in SEQ ID NO: 8, and a nucleotide sequence encoding human Neu3, isoform 1 is depicted in SEQ ID NO: 25. The amino acid sequence of human Neu3, isoform 2 is depicted in SEQ ID NO: 9, and a nucleotide sequence encoding human Neu3, isoform 2 is depicted in SEQ ID NO: 34.
[0082] Human Neu4 has two isoforms: isoform 1 is a peripheral membrane protein and isoform 2 localizes to the lysosome lumen. The amino acid sequence of human Neu4, isoform 1 is depicted in SEQ ID NO: 10, and a nucleotide sequence encoding human Neu4, isoform 1 is depicted in SEQ ID NO: 26. The amino acid sequence of human Neu4, isoform 2 is depicted in SEQ ID NO: 11, and a nucleotide sequence encoding human Neu4, isoform 2 is depicted in SEQ ID NO: 35.
[0083] Four sialidases have also been found in the mouse genome and are referred to as Neu1, Neu2, Neu3 and Neu4. The amino acid sequence of mouse Neu1 is depicted in SEQ ID NO: 38, and a nucleotide sequence encoding mouse Neu1 is depicted in SEQ ID NO: 42. The amino acid sequence of mouse Neu2 is depicted in SEQ ID NO: 39 and a nucleotide sequence encoding mouse Neu2 is depicted in SEQ ID NO: 43. The amino acid sequence of mouse Neu3 is depicted in SEQ ID NO: 40, and a nucleotide sequence encoding mouse Neu3 is depicted in SEQ ID NO: 44. The amino acid sequence of mouse Neu4 is depicted in SEQ ID NO: 41, and a nucleotide sequence encoding mouse Neu4 is depicted in SEQ ID NO: 45.
[0084] Exemplary prokaryotic sialidases include sialidases from Salmonella typhimurium and Vibrio cholera. The amino acid sequence of Salmonella typhimurium sialidase (St-sialidase) is depicted in SEQ ID NO: 30, and a nucleotide sequence encoding Salmonella typhimurium sialidase is depicted in SEQ ID NO: 6. The amino acid sequence of Vibrio cholera sialidase is depicted in SEQ ID NO: 36, and a nucleotide sequence encoding Vibrio cholera sialidase is depicted in SEQ ID NO: 37.
[0085] In certain embodiments, a recombinant mutant sialidase (e.g., human sialidase) has at least about 5%, at least about 10%, at least about 15%, at least about 20%, at least about 25%, at least about 30%, at least about 35%, at least about 40%, at least about 45%, at least about 50%, at least about 55%, at least about 60%, at least about 65%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 90%, at least about 95%, about 100%, or more than 100% of the enzymatic activity of a corresponding (or template) wild-type sialidase (e.g., human sialidase).
[0086] In certain embodiments, a recombinant mutant sialidase (e.g., human sialidase) has about 5%, about 10%, about 15%, about 20%, about 25%, about 30%, about 35%, about 40%, about 45%, about 50%, about 55%, about 60%, about 65%, about 70%, about 75%, about 80%, about 85%, about 90%, about 95%, about 100%, or more than 100% of the enzymatic activity of a corresponding (or template) wild-type sialidase (e.g., human sialidase).
[0087] In certain embodiments, the recombinant mutant sialidase (e.g., human sialidase) has the same substrate specificity as the corresponding wild-type sialidase (e.g., human sialidase). In other embodiments, the recombinant mutant sialidase (e.g., human sialidase) has a different substrate specificity than the corresponding wild-type sialidase (e.g., human sialidase). For example, in certain embodiments the recombinant mutant human sialidase can cleave α2,3, α2,6, and/or α2,8 linkages. In certain embodiments the sialidase can cleave α2,3 and α2,8 linkages.
Thus, the genus of recombinant mutant sialidase enzymes, recombinant mutant human sialidase, and recombinant mutant human neu2 sialidase enzymes encompassed by the instant claims is structurally and functionally vast.
The specification discloses exemplary wild-type human Neu2 as SEQ ID NO:1 (Table 7) AND exemplary amino substitutions within that sequence (Table 7).
Other than exemplary human neu2 SEQ ID NO:1, and the mutations in Table 7 in SEQ ID NO:1, the specification fails to disclose the structural sequence required of a “recombinant mutant sialidase enzyme” that would allow one of ordinary skill in the art to immediately recognize members of the claimed genus.
To provide adequate written description and evidence of possession of the claimed recombinant mutant sialidase enzyme genus, the instant specification can structurally describe representative recombinant mutant sialidase enzymes, or describe structural features common to the members of the genus, which features constitute a substantial portion of the genus. Alternatively, the specification can show that the claimed invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics (see University of California v. Eli Lilly and Co., 119 F.3d 1559, 43 USPQ2d 1398 (Fed. Cir. 1997) and Enzo Biochem, Inc. V. Gen-Probe Inc.). A disclosure that does not adequately describe a product itself logically cannot adequately describe a method of using that product.
In this case, the only factor present in the claims is a recitation of “recombinant mutant sialidase enzyme”. The instant specification fails to describe structural features common to the members of the genus, which features constitute a substantial portion of the genus because the instant specification discloses the genus encompasses vast number of variants and discloses only a single exemplary human neu2 sequence SEQ ID NO:1 as the basis of the claimed mutations. Other than SEQ ID NO:1, no sequence structure is correlated to a recombinant mutant sialidase enzyme function in order for one to recognize members of the claimed genus. The instant specification fails to describe a representative number of recombinant mutant sialidase enzyme sequences for the genus of recombinant mutant sialidase enzymes claimed. Accordingly, in the absence of sufficient recitation of distinguishing identifying characteristics, the specification does not provide adequate written description of the claimed genus required to perform the claimed method of treating cancer.
Although Applicants may argue that it is possible to screen for recombinant mutant sialidase enzymes and that function as a sialidase enzyme, the court found in (Rochester v. Searle, 358 F.3d 916, Fed Cir., 2004) that screening assays are not sufficient to provide adequate written description for an invention because they are merely a wish or plan for obtaining the claimed chemical invention. “As we held in Lilly, “[a]n adequate written description of a DNA … ‘requires a precise definition, such as by structure, formula, chemical name, or physical properties,’ not a mere wish or plan for obtaining the claimed chemical invention.” 119 F.3d at 1566 (quoting Fiers, 984 F.2d at 1171). For reasons stated above, that requirement applies just as well to non-DNA (or RNA) chemical inventions.” Knowledge of screening methods provides no information about the structure of any future recombinant mutant sialidase enzymes yet to be discovered that may function as claimed.
Given the lack of representative examples to support the full scope of the claimed recombinant mutant sialidase enzymes and those used in the claimed method, and lack of reasonable structure-function correlation with regards to the unknown sequences in the recombinant mutant sialidase enzyme that qualify it as a sialidase enzyme, the present claims lack adequate written description. Thus, the specification does not provide an adequate written description of recombinant mutant sialidase enzymes that is required to practice the claimed invention. Since the specification fails to adequately describe the product to which the claimed method uses, it also fails to adequately describe the method.
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)(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.
4. Claim(s) 7, 11, 15, 16, 19, 20, 27, 28, 30, 53-57 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by US Patent 2020/0370013, Posey et al, claiming priority to May 2019.
As stated in the 35 USC 112(a) written description rejection above, no sequence structure is recited in the claims for the recombinant mutant sialidase enzyme, other than comprising an Arg and Tyr.
Posey teaches a recombinant mutant sialidase enzyme comprising SEQ ID NO:10 or SEQ ID NO:34, that is mutated human Neu2 sialidase enzyme, wherein SEQ ID NO:10 and 34 comprise Arg and Tyr residues (see sequences below) (Figures 1-2; Figure 14; ([7-9]; [11-18]; [21]; [24-31]; [34-40]; [42]; [45]; claims 1-28).
Posey further teaches a fusion protein comprising the mutant human Neu2 sialidase enzymes SEQ ID NOs:10 or 34 fused to an immunoglobulin hinge and Fc domain that can be derived from IgG1 (Figures 1-2; [7-9]; [11-18]; [21]; [24-31]; [34-40]; [42]; [45];[174]; claims 1-28);
nucleic acid vectors encoding the recombinant mutant sialidase enzyme, expression vectors comprising the nucleic acid, host cells comprising the expression vector ([33]; [43]; [89]; [209-239]; Figures 1-2; claims 14, 21-22, 25-26);
pharmaceutical composition comprising the recombinant mutant sialidase enzyme ([22-23]; [240]; claims 11-14 and 27); and
method of treating cancer in a subject comprising administering an effective amount of the recombinant mutant sialidase enzyme to the subject ([44]; [240-292]; claim 27).
Posey mutant Neu2 SEQ ID NO:34:
SEQ ID NO: 34
MNPCPLYDAQTGTLFLFFIAIPGQVTEQQQLQTRANVTRLCQVTSTDHGRTWSSPRDLTDAAIGPAYREWSTFAVGPGHCLQLHDRARSLVVPAYAYRKLHPIQRPIPSAFCFLSHDHGRTWARGHFVAQDTLECQVAEVETGEQRVVTLNARSHLRARVQAQSTNDGLDFQESQLVKKLVEPPPQGCQGSVISFPSPRSGPGSPAQWLLYTHPTHSWQRADLGAYLNPRPPAPEAWSEPVLLAKGSCAYSDLQSMGTGPDGSPLFGCLYEANDYEEIVFLMFTLKQAFPAEYLPQSG
Posey mutant Neu2 SEQ ID NO:10:
SEQ ID NO: 10
MALPVTALLLPLALLLHAARPGSMASLPVLQKESVFQSGAHAYRIPALLYLPGQQSLLAFAEQRASKKDEHAELIVLRRGDYDAPTHQVQWQAQEVVAQARLDGHRSMNPCPLYDAQTGTLFLFFIAIPGQVTEQQQLQTRANVTRLCQVTSTDHGRTWSSPRDLTDAAIGPAYREWSTFAVGPGHCLQLHDRARSLVVPAYAYRKLHPIQRPIPSAFCFLSHDHGRTWARGHFVAQDTLECQVAEVETGEQRVVTLNARSHLRARVQAQSTNDGLDFQESQLVKKLVEPPPQGCQGSVISFPSPRSGPGSPAQWLLYTHPTHSWQRADLGAYLNPRPPAPEAWSEPVLLAKGSCAYSDLQSMGTGPDGSPLFGCLYEANDYEEIVFLMFTLKQAFPAEYLPQSGTTTPAPRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVITLYCKRGRKKLLYIFKQPFMRPVQTTQEEDGCSCRFPEEEEGGCELRVKFSRSADAPAYKQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAYSEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHMQALPPR
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.
5. Claims 7, 11, 15, 16, 19, 20, 24, 27, 28, 30, 32, 33, 36, 45, 46, 53-57 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6, 10-13, 15-18, 21, 25, 27, 29, 31, 33, 34, 43, 44, 45, 54-58 of copending Application No. 18/260,364 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because the copending application claims a recombinant mutant sialidase enzyme SEQ ID NO:234 that is 100% identical to instant SEQ ID NO:198 and comprises A42R and V6Y mutations relative to wild-type human neu2; nucleic acids encoding the enzyme, expression vectors comprising the nucleic acid, host cells comprising the expression vectors; pharmaceutical compositions comprising the enzyme; methods of treating cancer in a subject comprising administering a composition comprising the enzyme; fusion proteins comprising the enzyme and an anti-tumor antibody and immunoglobulin Fc domain that is derived from IgG1; wherein the fusion protein comprises SEQ ID NO:219 that is 99.8% identical to instant SEQ ID NO:205 and comprises V6Y and A42R mutations; an antibody conjugate comprising the fusion protein, wherein the conjugate comprises a first polypeptide comprising an immunoglobulin light chain, second polypeptide comprising and immunoglobulin heavy chain, and third polypeptide comprising an immunoglobulin Fc domain and sialidase; wherein the third polypeptide comprises the sialidase and the Fc domain in an N- to C- terminal orientation.
Thus, the claims of the copending application render obvious the instant claims.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Instant SEQ ID NO:198 aligned with copending 18/260,364 SEQ ID NO:234:
US-18-260-364-234
Filing date in PALM: 2023-07-05
Sequence 234, US/18260364
Publication No. US20240067729A1
GENERAL INFORMATION
APPLICANT: PALLEON PHARMACEUTICALS INC.
TITLE OF INVENTION: ANTI-PD-L1 ANTIBODIES AND FUSION PROTEINS THEREOF
FILE REFERENCE: PAL-024WO
CURRENT APPLICATION NUMBER: US/18/260,364
CURRENT FILING DATE: 2023-07-05
PRIOR APPLICATION NUMBER: PCT/US2022/011504
PRIOR FILING DATE: 2022-01-06
PRIOR APPLICATION NUMBER: 63/134,412
PRIOR FILING DATE: 2021-01-06
NUMBER OF SEQ ID NOS: 259
SEQ ID NO 234
LENGTH: 380
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Description of Artificial Sequence: Synthetic
polypeptide
ALIGNMENT:
Query Match 100.0%; Score 2034; Length 380;
Best Local Similarity 100.0%;
Matches 380; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 DASLPYLQKESVFQSGAHAYRIPALLYLPGQQSLLAFAEQRRSKKDEHAELIVLRRGDYD 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 DASLPYLQKESVFQSGAHAYRIPALLYLPGQQSLLAFAEQRRSKKDEHAELIVLRRGDYD 60
Qy 61 AGTHQVQWQAQEVVAQARLDGHRSMNPCPLYDEQTGTLFLFFIAIPGQVTEQQQLQTRAN 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 AGTHQVQWQAQEVVAQARLDGHRSMNPCPLYDEQTGTLFLFFIAIPGQVTEQQQLQTRAN 120
Qy 121 VTRLCYVTSTDHGRTWSSPRDLTDAAIGPAYREWSTFAVGPGHCLQLHDRARSLVVPAYA 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 VTRLCYVTSTDHGRTWSSPRDLTDAAIGPAYREWSTFAVGPGHCLQLHDRARSLVVPAYA 180
Qy 181 YRKLHPKQRPIPSAFCFLSHDHGRTWARGHFVAQDTLECQVAEVETGEQRVVTLNARSHL 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 YRKLHPKQRPIPSAFCFLSHDHGRTWARGHFVAQDTLECQVAEVETGEQRVVTLNARSHL 240
Qy 241 RFRVQAQSTNDGLDFQESQLVKKLVEPPPTGCQGSVISFPSPRSGPGSPAQWLLYTHPTH 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 RFRVQAQSTNDGLDFQESQLVKKLVEPPPTGCQGSVISFPSPRSGPGSPAQWLLYTHPTH 300
Qy 301 SWQRADLGAYLNPRPPAPEAWSEPVLLAKGSAAYSDLQSMGTGPDGSPLFGCLYEANDYE 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 SWQRADLGAYLNPRPPAPEAWSEPVLLAKGSAAYSDLQSMGTGPDGSPLFGCLYEANDYE 360
Qy 361 EIVFLMFTLKQAFPAEYLPQ 380
||||||||||||||||||||
Db 361 EIVFLMFTLKQAFPAEYLPQ 380
Instant SEQ ID NO:205 aligned with copending 18/260,364 SEQ ID NO:219
DUPLICATES:
US-18-260-364-219
Filing date in PALM: 2023-07-05
Sequence 219, US/18260364
Publication No. US20240067729A1
GENERAL INFORMATION
APPLICANT: PALLEON PHARMACEUTICALS INC.
TITLE OF INVENTION: ANTI-PD-L1 ANTIBODIES AND FUSION PROTEINS THEREOF
FILE REFERENCE: PAL-024WO
CURRENT APPLICATION NUMBER: US/18/260,364
CURRENT FILING DATE: 2023-07-05
PRIOR APPLICATION NUMBER: PCT/US2022/011504
PRIOR FILING DATE: 2022-01-06
PRIOR APPLICATION NUMBER: 63/134,412
PRIOR FILING DATE: 2021-01-06
NUMBER OF SEQ ID NOS: 259
SEQ ID NO 219
LENGTH: 612
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Description of Artificial Sequence: Synthetic
polypeptide
ALIGNMENT:
Query Match 99.8%; Score 3286; Length 612;
Best Local Similarity 99.8%;
Matches 611; Conservative 0; Mismatches 1; Indels 0; Gaps 0;
Qy 1 DASLPYLQKESVFQSGAHAYRIPALLYLPGQQSLLAFAEQRRSKKDEHAELIVLRRGDYD 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 DASLPYLQKESVFQSGAHAYRIPALLYLPGQQSLLAFAEQRRSKKDEHAELIVLRRGDYD 60
Qy 61 AGTHQVQWQAQEVVAQARLDGHRSMNPCPLYDEQTGTLFLFFIAIPGQVTEQQQLQTRAN 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 AGTHQVQWQAQEVVAQARLDGHRSMNPCPLYDEQTGTLFLFFIAIPGQVTEQQQLQTRAN 120
Qy 121 VTRLCYVTSTDHGRTWSSPRDLTDAAIGPAYREWSTFAVGPGHCLQLHDRARSLVVPAYA 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 VTRLCYVTSTDHGRTWSSPRDLTDAAIGPAYREWSTFAVGPGHCLQLHDRARSLVVPAYA 180
Qy 181 YRKLHPKQRPIPSAFCFLSHDHGRTWARGHFVAQDTLECQVAEVETGEQRVVTLNARSHL 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 YRKLHPKQRPIPSAFCFLSHDHGRTWARGHFVAQDTLECQVAEVETGEQRVVTLNARSHL 240
Qy 241 RFRVQAQSTNDGLDFQESQLVKKLVEPPPTGCQGSVISFPSPRSGPGSPAQWLLYTHPTH 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 RFRVQAQSTNDGLDFQESQLVKKLVEPPPTGCQGSVISFPSPRSGPGSPAQWLLYTHPTH 300
Qy 301 SWQRADLGAYLNPRPPAPEAWSEPVLLAKGSAAYSDLQSMGTGPDGSPLFGCLYEANDYE 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 SWQRADLGAYLNPRPPAPEAWSEPVLLAKGSAAYSDLQSMGTGPDGSPLFGCLYEANDYE 360
Qy 361 EIVFLMFTLKQAFPAEYLPQEPKSSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISR 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 EIVFLMFTLKQAFPAEYLPQEPKSSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISR 420
Qy 421 TPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLN 480
||||||||||||||||||||||||||||||||||||||||| ||||||||||||||||||
Db 421 TPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYASTYRVVSVLTVLHQDWLN 480
Qy 481 GKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLYCLVKGFYPS 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 GKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLYCLVKGFYPS 540
Qy 541 DIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNH 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 DIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNH 600
Qy 601 YTQKSLSLSPGK 612
||||||||||||
Db 601 YTQKSLSLSPGK 612
6. Claims 7, 11, 15, 16, 19, 20, 24, 27, 28, 30, 32, 33, 36, 45, 46, 53-57 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3-6, 9, 13, 15, 17, 19-21, 23, 33-35, 44-48 of copending Application No. 18/260,378 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because the copending application claims a recombinant mutant sialidase enzyme SEQ ID NO:63 that is 100% identical to instant SEQ ID NO:198 and comprises A42R and V6Y mutations relative to wild-type human neu2; nucleic acids encoding the enzyme, expression vectors comprising the nucleic acid, host cells comprising the expression vectors; pharmaceutical compositions comprising the enzyme; methods of treating cancer in a subject comprising administering a composition comprising the enzyme; fusion proteins comprising the enzyme and an anti-tumor antibody and immunoglobulin Fc domain that is derived from IgG1; wherein the fusion protein comprises SEQ ID NO:125 that is 99.8% identical to instant SEQ ID NO:205 and comprises mutations V6Y and A42R; an antibody conjugate comprising the fusion protein, wherein the conjugate comprises a first polypeptide comprising an immunoglobulin light chain, second polypeptide comprising and immunoglobulin heavy chain, and third polypeptide comprising an immunoglobulin Fc domain and sialidase; wherein the third polypeptide comprises the sialidase and the Fc domain in an N- to C- terminal orientation.
Thus, the claims of the copending application render obvious the instant claims.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Instant SEQ ID NO:198 aligned with copending 18/260,378 SEQ ID NO:63:
US-18-260-378-63
Filing date in PALM: 2023-07-05
Sequence 63, US/18260378
Publication No. US20240059773A1
GENERAL INFORMATION
APPLICANT: PALLEON PHARMACEUTICALS INC.
TITLE OF INVENTION: SIALIDASE-PD-1-ANTIBODY FUSION PROTEINS AND METHODS OF USE
TITLE OF INVENTION: THEREOF
FILE REFERENCE: PAL-025WO
CURRENT APPLICATION NUMBER: US/18/260,378
CURRENT FILING DATE: 2023-07-05
PRIOR APPLICATION NUMBER: PCT/US2022/011487
PRIOR FILING DATE: 2022-01-06
PRIOR APPLICATION NUMBER: 63/134,415
PRIOR FILING DATE: 2021-01-06
NUMBER OF SEQ ID NOS: 150
SEQ ID NO 63
LENGTH: 380
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Description of Artificial Sequence: Synthetic
polypeptide
Query Match 100.0%; Score 2034; Length 380;
Best Local Similarity 100.0%;
Matches 380; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 DASLPYLQKESVFQSGAHAYRIPALLYLPGQQSLLAFAEQRRSKKDEHAELIVLRRGDYD 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 DASLPYLQKESVFQSGAHAYRIPALLYLPGQQSLLAFAEQRRSKKDEHAELIVLRRGDYD 60
Qy 61 AGTHQVQWQAQEVVAQARLDGHRSMNPCPLYDEQTGTLFLFFIAIPGQVTEQQQLQTRAN 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 AGTHQVQWQAQEVVAQARLDGHRSMNPCPLYDEQTGTLFLFFIAIPGQVTEQQQLQTRAN 120
Qy 121 VTRLCYVTSTDHGRTWSSPRDLTDAAIGPAYREWSTFAVGPGHCLQLHDRARSLVVPAYA 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 VTRLCYVTSTDHGRTWSSPRDLTDAAIGPAYREWSTFAVGPGHCLQLHDRARSLVVPAYA 180
Qy 181 YRKLHPKQRPIPSAFCFLSHDHGRTWARGHFVAQDTLECQVAEVETGEQRVVTLNARSHL 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 YRKLHPKQRPIPSAFCFLSHDHGRTWARGHFVAQDTLECQVAEVETGEQRVVTLNARSHL 240
Qy 241 RFRVQAQSTNDGLDFQESQLVKKLVEPPPTGCQGSVISFPSPRSGPGSPAQWLLYTHPTH 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 RFRVQAQSTNDGLDFQESQLVKKLVEPPPTGCQGSVISFPSPRSGPGSPAQWLLYTHPTH 300
Qy 301 SWQRADLGAYLNPRPPAPEAWSEPVLLAKGSAAYSDLQSMGTGPDGSPLFGCLYEANDYE 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 SWQRADLGAYLNPRPPAPEAWSEPVLLAKGSAAYSDLQSMGTGPDGSPLFGCLYEANDYE 360
Qy 361 EIVFLMFTLKQAFPAEYLPQ 380
||||||||||||||||||||
Db 361 EIVFLMFTLKQAFPAEYLPQ 380
7. Claims 7, 11, 15, 16, 19, 20, 24, 27, 28, 30, 32-36, 45, 46, 53-57 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3, 5, 9, 11, 15, 17, 19, 21-26, 35-37, 48-52, 60, 65, 66, and 68 of copending Application No. 18/260,383 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because the copending application claims a recombinant mutant sialidase enzyme SEQ ID NO:198 that is 100% identical to instant SEQ ID NO:198 and comprises A42R and V6Y mutations relative to wild-type human neu2; nucleic acids encoding the enzyme, expression vectors comprising the nucleic acid, host cells comprising the expression vectors; pharmaceutical compositions comprising the enzyme; methods of treating cancer in a subject comprising administering a composition comprising the enzyme; fusion proteins comprising the enzyme and an anti-tumor antibody and immunoglobulin Fc domain that is derived from IgG1; wherein the anti-tumor antibody is trastuzumab; wherein the fusion protein comprises SEQ ID NO:205 that is 100% identical to instant SEQ ID NO:205; an antibody conjugate comprising the fusion protein, wherein the conjugate comprises a first polypeptide comprising an immunoglobulin light chain, second polypeptide comprising and immunoglobulin heavy chain, and third polypeptide comprising an immunoglobulin Fc domain and sialidase; wherein the third polypeptide comprises the sialidase and the Fc domain in an N- to C- terminal orientation.
Thus, the claims of the copending application render obvious the instant claims.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
8. Conclusion: No claim is allowed.
9. Any inquiry concerning this communication or earlier communications from the examiner should be directed to LAURA B GODDARD whose telephone number is (571)272-8788. The examiner can normally be reached Mon-Fri, 7am-3:30pm.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Samira Jean-Louis can be reached at 571-270-3503. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/Laura B Goddard/Primary Examiner, Art Unit 1642
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