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 .
Objections/Rejections Withdrawn
Rejections and/or objections not reiterated from previous Office Actions are hereby withdrawn. The following rejections and/or objections are either reiterated or newly applied, and constitute the complete set presently being applied to the instant application.
Response to Arguments
Applicant’s arguments with respect to claim(s) 1-17 under 35 U.S.C. 103 have been considered but are moot because the new ground of rejection does not rely on any reference applied in the prior rejection of record for any teaching or matter specifically challenged in the argument.
Moreover, the Applicant’s request that the double patenting rejections be held in abeyance until patentable subject matter is identified is noted but the rejections have been modified/maintained herein.
Election/Restrictions
Applicant's election with traverse of Group 1, claims 1-17, drawn to an isolated peptide in the reply filed on 10/6/2025 is acknowledged. The traversal is on the ground(s) that it would not be unduly burdensome to perform a search on all of the claims together in the present application. This is not found persuasive because the inventions recited in Groups I-III in the Election/Restriction Requirement have separate statuses in the art in view of their different classifications. The inventions have separate statuses in the art due to their divergent subject matter. The inventions require different search queries. These require search of several different inventive concepts. Also, each invention is likely to raise different issues under 35 USC 101 and 112, first paragraph.
Thus, the requirement is still deemed proper and is therefore made FINAL.
Applicant’s election of the species SEQ ID NO: 5 in the reply filed on 10/6/2025 is acknowledged. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)).
Upon further search and examination, the species election was broadened to include a first protein moiety comprising residues 113-231 of SEQ ID NO: 2 in addition to the elected species of SEQ ID NO: 5.
Claim Status
Claims 1-10, 12-14, and 18-20 are pending. Claims 18-20 are withdrawn. Claims 1, 7-10, and 12 are currently amended. Claims 11, and 15-17 are cancelled.
Priority
The instant application is a continuation-in-part of PCT/EP2021/059434, filed 4/12/2021. The priority date of 4/12/2021 is acknowledged.
Information Disclosure Statement
The IDS submitted on 05/04/2026 is under consideration.
Claim Interpretation
Claim 1 recites “An isolated protein comprising (i) a first protein moiety… comprising an amino acid sequence having at least 70% identity to residues 113-231 of SEQ ID NO: 2” (emphasis added). This claim is being interpreted as a peptide comprising residues 113-231 of SEQ ID NO: 2, wherein a peptide or protein encompassing or containing the entirety of residues 113-231 of SEQ ID NO: 2 meets the limitation of the claim. Conversely, smaller fragments encompassed by SEQ ID NO: 1 (i.e., dipeptides) are being interpreted as not meeting the limitations of the claim. This same interpretation is being applied to all other instances where “an amino acid” is recited in claims 1-3.
Additionally, “an isolated protein”, as recited above in claim 1, is being interpreted as a recombinant protein, comprising a first moiety and a second moiety (fusion protein).
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.
Claim 14 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 14 depends from claim 11, which is cancelled, thus rendering the scope of claim 14 indefinite. For purposes of examination, claim 14 is being interpreted as if depending from claim 1 rather than claim 11.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claim(s) 1-10 and 12-13 are rejected under 35 U.S.C. 103 as being unpatentable over Chen et al. (Chen, G., Andrade-Talavera, Y., Tambaro, S. et al. Augmentation of Bri2 molecular chaperone activity against amyloid-β reduces neurotoxicity in mouse hippocampus in vitro. Commun Biol 3, 32 (2020)., cited on IDS filed 10/12/2022), as evidenced by Tambaro et al. (Blood-brain and blood-cerebrospinal fluid passage of BRICHOS domains from two molecular chaperones in mice. J Biol Chem. 2019 Feb 22;294(8):2606-2615.); in view of Chen et al. (“Chen2”, Amyloid beta: structure, biology and structure-based therapeutic development. Acta Pharmacol Sin 38, 1205–1235 (2017).), as evidenced Promega (Amino Acid Structure, accessed 11/25/2025) and MedChemExpress (Gantenerumab, accessed from https://www.medchemexpress.com/gantenerumab.html?srsltid=AfmBOopqEJRKKiT76raqgzo_66QQoevHEhHpno8qoJDV7y9RGGvoTI0E on 6/10/2026).
Chen teaches that the BRICHOS domain of recombinant human Bri2 can be used to efficiently inhibit amyloid formation, particularly Aβ42 fibril formation in vitro and in alleviating the related neurotoxicity to hippocampal slice preparations and in Drosophila models (Pg 2, left column, bottom paragraph).
Chen describes generating recombinant human Bri2 BRICHOS fusion proteins comprising the His6-NT* solubility tag chemically linked to Bri2 residues 113-231 (Pg 9, left column, “Rh Bri2 BRICHOS R221E and Bri2 BRICHOS-AU1 preparation”). As evidenced by the instant specification, residues 113-231 of Bri2 are identical to the instant SEQ ID NO: 2, which also encompasses the instant SEQ ID NO: 5 (List of appended sequences, Pg 7-9). Further, as evidenced by Tambaro, Bri2 BRICHOS domains can cross the blood-brain barrier in mice (Abstract).
Chen does not teach a fusion protein comprising SEQ ID NO: 2 linked to a second protein or polypeptide moiety selected from the group consisting of protein drugs, antibodies, enzymes, and neurotrophic factors and contains at least 50 amino acid residues.
Chen2 teaches therapeutic developments and recent advances of different strategies for treating Alzheimer’s disease, including the search for novel, potentially effective agents that act on amyloid beta (Aβ; Abstract). The therapeutics taught by Chen2 include protein drugs, antibodies, and enzymes among others (Pg 1220-1221, right column, “Immunotherapeutic approach”; Table 5; Pg 1222, left column, “Aβ-degrading proteases (AβDPs)”; Table 7; Table 9, e.g., liraglutide).
Based on these teachings, it would be prima facie obvious to substitute the solubility protein tag in the peptide taught by Chen for one of the peptide therapeutics taught by Chen2. One skilled in the art would be motivated to do so in order to combine two peptide therapeutics useful for treating Aβ fibril formations and associated neurotoxicity into a single peptide therapeutic. One would have a reasonable expectation of success as Chen already established that the Bri2 BRICHOS domain could be fused to other protein domains.
Additionally, per MPEP 2144.06(I), combining equivalents known for the same purpose is one legal precedent recognized by the courts as directed to common practices that normally require only ordinary skill in the art and are considered routine expedients: "It is prima facie obvious to combine two compositions each of which is taught by the prior art to be useful for the same purpose, in order to form a third composition to be used for the very same purpose.... [T]he idea of combining them flows logically from their having been individually taught in the prior art." In re Kerkhoven, 626 F.2d 846, 850, 205 USPQ 1069, 1072 (CCPA 1980). By extension of this, it would be obvious to combine one Aβ therapeutic with another one, thus creating a single peptide with multiple domains designed to achieve the same goal.
Regarding claims 2-4, as stated above, Chen teaches residues 113-231 of Bri2, which are 100% identical to the instant SEQ ID NO: 2, which also encompasses the instant SEQ ID NO: 5 (List of appended sequences, Pg 7-9).
Regarding claims 5 and 6, Chen further teaches that the monomeric form of Bri2 BRICHOS is most desirable as it is the most potent in preventing Aβ42-induced disruption of neuronal network activity and accumulation of oligomers may contribute to Alzheimer’s disease (Pg 2, right column, first and second paragraphs before “Results”). Thus, it is desirable to introduce mutations that can stabilize Bri2 BRICHOS in the monomeric state, such as substituted Arg for Glu at position 221 (Pg 2-3, “R221E mutant forms stable monomers and unstable oligomers”; Pg 9, left column, “Rh Bri2 BRICHOS R221E and Bri2 BRICHOS-AU1 preparation”).
Regarding claims 7 and 8, Chen describes generating recombinant human Bri2 BRICHOS fusion proteins comprising the His6-NT* solubility tag (protein tag) chemically linked to Bri2 residues 113-231 (Pg 9, left column, “Rh Bri2 BRICHOS R221E and Bri2 BRICHOS-AU1 preparation”). As evidenced by the instant Sequence Listing, the instant SEQ ID NO: 2 and SEQ ID NO: 5 are both more than 90 but less than 200 amino acids.
Regarding claims 9 and 10, Chen2 teaches, for example, the antibody Gantenerumab. As evidenced by MedChemExpress, Gantenerumab has a molecular weight of 146.28kDa (Pg 3); this means that Gantenerumab consists of approximately ~1330 amino acids (146.28kDa*(1000Da/1kDa) = 146,280Da/110Da/amino acid = 1329.82), as Promega evidences that the average molecular weight of an amino acid is 110Da.
Regarding claim 12, as stated above, Chen2 teaches antibodies to treat Aβ plaques (Pg 1220-1221, right column, “Immunotherapeutic approach”; Table 5).
Regarding claim 13, Chen2 teaches insulin-like growth factor to clear Aβ (Pg 1216, right column, final line).
Claim(s) 1-10 and 12-14 are rejected under 35 U.S.C. 103 as being unpatentable over Chen et al. (Chen, G., Andrade-Talavera, Y., Tambaro, S. et al. Augmentation of Bri2 molecular chaperone activity against amyloid-β reduces neurotoxicity in mouse hippocampus in vitro. Commun Biol 3, 32 (2020)., cited on IDS filed 10/12/2022), as evidenced by Tambaro et al. (Blood-brain and blood-cerebrospinal fluid passage of BRICHOS domains from two molecular chaperones in mice. J Biol Chem. 2019 Feb 22;294(8):2606-2615.); and Chen et al. (“Chen2”, Amyloid beta: structure, biology and structure-based therapeutic development. Acta Pharmacol Sin 38, 1205–1235 (2017).), as evidenced Promega (Amino Acid Structure, accessed 11/25/2025) and MedChemExpress (Gantenerumab, accessed from https://www.medchemexpress.com/gantenerumab.html?srsltid=AfmBOopqEJRKKiT76raqgzo_66QQoevHEhHpno8qoJDV7y9RGGvoTI0E on 6/10/2026), and further in view of Choi et al. (Lysosomal Enzyme Glucocerebrosidase Protects against Aβ1-42 Oligomer-Induced Neurotoxicity. PLoS One. 2015 Dec 2;10(12):e0143854.).
The teachings of Chen and Chen2 have been set forth above. Chen and Chen2 do not teach that the second protein or polypeptide moiety is an enzyme selected from those recited in claim 14.
Choi teaches glucocerebrosidase (GCase; β-glucocerebrosidase) can treat Aβ oligomers (Abstract).
Based on these teachings, it would be prima facie obvious to generate a Bri2 BRICHOS-GCase therapeutic fusion protein. One skilled in the art would be motivated to do so in order to combine two peptide therapeutics both useful for treating Aβ fibril formations into a single peptide. One would have a reasonable expectation of success as Chen and Chen2 established that the Bri2 BRICHOS domain could be fused to other proteins and/or protein domains, such as enzymes.
Additionally, per MPEP 2144.06(I), combining equivalents known for the same purpose is one legal precedent recognized by the courts as directed to common practices that normally require only ordinary skill in the art and are considered routine expedients: "It is prima facie obvious to combine two compositions each of which is taught by the prior art to be useful for the same purpose, in order to form a third composition to be used for the very same purpose.... [T]he idea of combining them flows logically from their having been individually taught in the prior art." In re Kerkhoven, 626 F.2d 846, 850, 205 USPQ 1069, 1072 (CCPA 1980). By extension of this, it would be obvious to combine one Aβ therapeutic with another one, thus creating a single peptide with multiple domains designed to achieve the same goal.
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.
Claims 1-4, 7, 8, and 18-20 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-13 of U.S. Patent No. 8,785,391 B2 (US ‘391). Although the claims at issue are not identical, they are not patentably distinct from each other because they contain overlapping subject matter.
Claim 1 of US ‘391 recites a method for therapeutically treating or delaying the progression of a condition selected from the group consisting of Alzheimer's disease, familial Danish dementia and familial British dementia in a mammal in need thereof, the method comprising administering to said mammal a therapeutically effective amount of an isolated protein, wherein the isolated protein decreases or reduces amyloid fibril formation and aggregation of amyloid β peptide, and wherein the isolated protein is selected from the group consisting of proteins comprising an amino acid sequence having at least 70% identity to residues 90-236 of Bri2 from human (SEQ ID NO: 2); and proteins comprising an amino acid sequence having at least 70% identity to any one of the Brichos domains of Bri2 from human (SEQ ID NO: 5), chimpanzee (SEQ ID NO: 6), bovine (SEQ ID NO: 7), pig (SEQ ID NO: 8), mouse (SEQ ID NO: 9) and rat (SEQ ID NO: 10); with the provisos that said protein is not comprising an amino acid sequence having at least 70% identity to residues 1-89 of Bri2 from human (SEQ ID NO: 3); and said protein is not comprising an amino acid sequence having at least 70% identity to human ABri23 (SEQ ID NO: 4). SEQ ID NO: 2 of US ‘391 exhibits 100% sequence identity to the instant SEQ ID NO: 2, and SEQ ID NO: 5 of US ‘391 and the instant SEQ ID NO: 5 are identical. Further, the instant specification states that an object of the invention is to provide a new treatment option for the treatment of Alzheimer’s (Pg 4, lines 24-25).
Dependent claims further include the percent identity (claims 2-4), the size of the isolated protein (claims 5-7), treatment of Alzheimer’s disease (claim 8), treating a human (claim 9), and the identity of the isolated protein (claims 10-13).
Claims 1-10 and 12-14 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-5, 20-22, and 23 of copending Application No. 17/784,591 (‘591 reference application; claim set filed 2/24/2026; allowed 4/17/2026). Although the claims at issue are not identical, they are not patentably distinct from each other because they contain overlapping subject matter.
Claim 1 of copending Application No. ‘591 recites an isolated protein comprising a moiety of 90-200 amino acid residues having at least 70% identity to SEQ ID NO: 7, wherein the amino acid residue corresponding to position 221 in SEQ ID NO: 1 is selected from the group consisting of Glu and Asp. SEQ ID NO: 7 of copending Application No. ‘591 and the instant SEQ ID NO: 5 are identical. Claim 7 similarly recites an isolated protein comprising a moiety of 90-200 amino acid residues having at least 70% identity to SEQ ID NO: 7, wherein the amino acid residue corresponding to position 221 in SEQ ID NO: 7 is not Arg, Lys, or His, or a nucleic acid encoding the isolated protein for use as a medicament.
Dependent claims include modification of position 221 (claims 2, 5, 8-11, 13, and 22), the percent identity (claims 3 and 20-21), the size of the overall isolated protein (claims 4 and 12), and a pharmaceutical composition thereof (claim 23). This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 1-10, 12, and 18-20 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 5-8, 13, 14, 16, 20-26, 29, 30, and 45-47 of copending Application No. 19/120,509 (‘509 reference application; claim set filed 4/11/2025). Although the claims at issue are not identical, they are not patentably distinct from each other because they contain overlapping subject matter.
Claim 1 of copending Application No. ‘509 recites an isolated protein comprising:
(1) a first protein moiety selected from a group of proteins comprising an amino acid sequence having at least 70% identity to residues 113-231 of Bni2 from human (SEQ ID NO: 2); and proteins comprising an amino acid sequence having at least 70% identity to any one of the BRICHOS domains of Bri2 from human (SEQ ID NO: 5), chimpanzee (SEQ ID NO: 6), bovine (SEQ ID NO: 7), pig (SEQ ID NO: 8), mouse (SEQ ID NO: 9) and rat (SEQ ID NO: 10); and
(ii) a second protein or polypeptide moiety, preferably containing at least 50 amino acid residues, wherein the second protein or polypeptide moiety is a monoclonal antibody; wherein said isolated protein is not comprising an amino acid sequence having at least 70% identity to residues 1-89 of Bri2 from human (SEQ ID NO: 3); and wherein said isolated protein is not comprising an amino acid sequence having at least 70% identity to human ABni23 (SEQ ID NO: 4). SEQ ID NO: 2 and 5 of copending Application No. ‘509 are identical to the instant SEQ ID NO: 2 and 5, respectively.
Dependent claims include modification specific species of antibodies (claims 5-8), the isolated protein is a recombinant fusion protein (claims 13, 14), the percent identity (claim 16, 20-22), modification of position 221 (claims 23 and 24), properties of the first and second protein moieties (claims 25, 26, 29, and 30), and methods of treatment (claims 45-47). This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 1-10, 12-14, and 18-20 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-31 of copending Application No. 19/527,846 (‘846 reference application; claim set filed 4/10/2026). Although the claims at issue are not identical, they are not patentably distinct from each other because they contain overlapping subject matter.
Claim 1 of copending Application No. ‘846 recites an isolated protein comprising an amino acid sequence having at least 70% identity to residues 112-231 of Bri2 from human (SEQ ID NO: 2); and proteins comprising an amino acid sequence having at least 70% identity to any one of the BRICHOS domains of Bri2 from human (SEQ ID NO: 5), chimpanzee (SEQ ID NO: 6), bovine (SEQ ID NO: 7), pig (SEQ ID NO: 8), mouse (SEQ ID NO: 9) and rat (SEQ ID NO: 10) for use in a method of treating Parkinson's Disease or other α-synucleinopathies in a mammal, including man, in need thereof. SEQ ID NO: 2 and 5-10 of copending Application No. ‘846 are identical to the instant SEQ ID NO: 2 and 5-10 recited in the instant application; thus, the instantly claimed peptides anticipate the peptides recited in the claims of copending Application No. ‘846.
Dependent claims include additional species of the peptides (claims 2-14), a fusion protein and species thereof (claims 15-28), and methods of treatment (claims 29-31). This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
No claim is allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Sara E Konopelski Snavely whose telephone number is (571)272-1841. The examiner can normally be reached Monday - Friday 9-6pm EST.
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/SARA E KONOPELSKI SNAVELY/Examiner, Art Unit 1658
/Melissa L Fisher/Supervisory Patent Examiner, Art Unit 1658
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