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
RESPONSE TO AMENDMENT
Status of Application/Amendments/claims
2. Applicant’s amendment filed May 5, 2026 is acknowledged. Claims 2-8,16-26, and 28-29 are canceled. Claims 1, 9-10, 13, 15, and 27 are amended. Claims 30-41 are newly added. Claims 1, 9-15, 27 and new claims 30-41 are pending in this application. Election was made without traverse in the reply filed on August 11, 2025.
3. Claims 1, 9-15, 27 and 30-41 are under examination with respect to SEQ ID NOs: 1, 42 and 43 in this office action.
4. Applicant’s arguments filed on May 5, 2026 have been fully considered but they are not deemed to be persuasive for the reasons set forth below.
Priority
5. The priority of the claimed chimeric receptor comprising from the N-terminal to the C-terminal direction: an extracellular domain comprising an amyloid-binding peptide or functional fragment thereof and an antibody CH2 domain or fragment thereof, a transmembrane domain that is derived from a CD8 alpha chain, and a cytoplasmic domain comprising a signal domain selected from a cytoplasmic domain I, a cytoplasmic domain II or combinations thereof recited in instant claim 1 is January 15, 2021.
The priority of the claimed chimeric receptor comprising an antibody CH2 domain comprising an amino acid sequence having at least 85% identity to recited SEQ ID NO: 33 recited in claims 11 and 38, or a cytoplasmic domain comprising an amino acid sequence having at least 85% identity to recited SEQ ID NO: 41, 42 or 45 recited in claim 13 or the receptor having at least 85% identity to the sequence of SEQ ID NO: 43, 52 or 53 recited in claims 15 and 40 is January 15, 2021.
Response to Arguments
On p. 5-7 of the response, Applicant argues that: i) amended claims no longer recite SEQ ID NOs: 21-26; ii) provisional Application No.62/962763 filed January 17, 2020 provides adequate written description support for the peptide-based chimeric receptor recited in instant claims and cites table 2 and para. [0014]-[0016] and [0161] in support of the arguments.
In response, the examiner asserts that provisional application No.62/962763 does not disclose claimed chimeric receptor recited in instant claims because:
i. Regarding the limitation “an amyloid-binding peptide or any functional fragment thereof”, provisional Application No. 62/962763 only disclosed “sequences for p5+14 and p5, p5R/G, p8, p9, p19, p20, p31, p37, p39, p42, p43, p44, p48, p50 and p58” on p. 9, Table A of 62/962763, which corresponds to instant SEQ ID NOs: 1-18 in Table A of the instant specification. But the limitation “an extracellular domain comprising an amyloid-binding peptide or any functional fragment thereof” encompasses any amyloid-binding peptide or any functional fragment thereof with any sequence.
ii. Regarding the limitation “an antibody CH2 domain or fragment thereof”, provisional application No. 62/962763 only disclosed “the CH2 domain of pFUSE-mIgG2A-Fc2 and its sequence” (p. 13 of 62/962763). But the limitation “an antibody CH2 domain or fragment thereof” encompasses any CH2 sequence from any antibody.
iii. Regarding the limitation “a transmembrane domain that is derived from a CD8 alpha chain”, provisional application No. 62/962763 only disclosed “aa 138-206 of human CD8” (see p. 13 of 62/962763). But The limitation “a transmembrane domain that is derived from a CD8 alpha chain” encompasses any sequence derived from a CD8 alpha chain, which encompasses any sequence.
iv. The limitation “a cytoplasmic domain comprising a signal domain selected from a cytoplasmic domain I, a cytoplasmic domain II or combinations thereof”, provisional application No. 62/962763 only disclosed “the PI3K cytoplasmic region I and the FcERg cytoplasmic region II” in p5+14CARFcR or “a cytoplasmic domain 1: aa 500-534 of mouse CD19 and a cytoplasmic domain II: aa 19-86 of mouse FcERG precursor” in 11-1F4CARtandem (see p. 7 and p. 13 of 62/962763). But the limitation “a cytoplasmic domain comprising a signal domain selected from a cytoplasmic domain I, a cytoplasmic domain II or combinations thereof” encompasses any sequence from any protein with a cytoplasmic domain I and/or cytoplasmic domain II.
v. The provisional application No.62/962763 filed Jan 17, 2020 only disclosed i) two CAR: 11-1F4CARtandem or p5+14CARFcR (p. 7 and p. 13); ii) design parameters of CARP paper (p. 13) and iii) sequences for p5+14 and p5, p5R/G, p8, p9, p19, p20, p31, p37, p39, p42, p43, p44, p48, p50 and p58 (p. 9, Table A of 62/962763 corresponding to instant SEQ ID NOs: 1-18 in Table A of the instant specification), and sequences for the spacer/transmembrane, the PI3K cytoplasmic region I, the FcERg cytoplasmic region II and the CH2 domain of pFUSE-mIgG2A-Fc2.
The p5+14CARFcR comprises the sequence of the final CAR-P construct-345aa on p.13 of 62/962763, which corresponds to instant SEQ ID NO:43 of the instant specification.
The CARP design comprises from the N-terminus to the C-terminus: a Signal peptide: aa 1-21 of human CD8-an Extracellular antibody sequence: a VL chain: aa 23-130 of anti-CD19 CAR-a GS linker-a VH chain: aa 148-267 of anti-CD19 CAR-stalk/transmembrane: aa 138-206 of human CD8-cytosolic sequence: aa500-534 mouse CD19 fused to aa 19-86 of mouse Fc ERG precursor-Fluorophore:mGFP (p.13).
The 11-1F4CARtandem comprises aa 1-27 of mouse CD8 a-chain, aa 1-111 of VL of anti-Abeta 11-1F4 scFv, a scFv linker-aa 1-111 of VH of anti-Abeta 11-1F4 scFv-a spacer-TM domain: aa 148-218 of mouse CD8 a-chain, a cytoplasmic domain 1: aa 500-534 of mouse CD19 and a cytoplasmic domain II: aa 19-86 of mouse FcERG precursor (see p. 7, table 1 of 62/962763, corresponding to instant SEQ ID NO:50).
Thus, the provisional application No.62/962763 does not disclose claimed chimeric receptor recited in instant claim 1. Accordingly, the priority of the claimed chimeric receptor recited in instant claim 1 is January 15, 2021.
Claim Rejections/Objections Withdrawn
6. The rejection of claims 9, 13, 15, 27 and 29 on the basis that it contains an improper Markush grouping of alternatives is withdrawn in response to Applicant’s amendment to the claims and arguments on p. 7-9 of the response.
The rejection of claim 10 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite is withdrawn in response to Applicant’s amendment to the claim.
The rejection of claims 2, 4, 7-8, 25 and 28-29 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 rejection of claims 1-2, 7 and 12-14 under 35 U.S.C. 102(a)(1) & (a)(2) as being anticipated by Rosenthal (US2019/0233496) is withdrawn in response to Applicant’s amendment to the claims and cancelation of claims 2 and 7.
The rejection of claim 4 under 35 U.S.C. 103 as being unpatentable over Rosenthal (US2019/0233496) in view of Lentzsch (US20190038745) is moot because the claim is canceled.
The rejection of claims 8-11, 15, 25 and 27-29 under 35 U.S.C. 103 as being unpatentable over Rosenthal (US2019/0233496) in view of Wall et al. (US20160243230) and Elson et al. (US2017/0298129) is withdrawn in response to Applicant’s amendment to the claims, cancelation of claims 8 and 29, and Applicant’s arguments on p. 17-20 of the response.
The provisional rejection of claims 1, 8-15, 25 and 27-29 on the ground of nonstatutory double patenting as being unpatentable over claims 1-57 of copending Application No. 19/107007 is withdrawn in response to Applicant’s amendment to the claims, cancelation of claims 8, 25 and 28 and Applicant’s arguments on p. 20-21 of the response. moot because the claims are canceled.
Claim Rejections/Objections Maintained
In view of the amendment filed on May 5, 2026, the following rejections are maintained.
Claim Rejections - 35 USC § 112
7. The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1, 9-15, 27 and 30-41 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. The rejection is maintained for the reasons of record and the reasons set forth below.
Claims 1, 9-15, 27 and 30-41 as amended are drawn to a chimeric receptor comprising from N-terminal to C-terminal direction:
an extracellular domain comprising an amyloid binding peptide or functional fragment thereof and an antibody CH2 domain or fragment thereof;
a transmembrane domain that is derived from a CD8 alpha chain; and
a cytoplasmic domain comprising a singling domain selected from a cytoplasmic domain I, a cytoplasmic domain II or combinations thereof.
The claims encompass a genus of chimeric receptor having the structure recited in claim 1, a genus of extracellular domain comprising a genus of amyloid-binding peptide or functional fragment thereof and an antibody CH2 domain or fragment thereof, a genus of transmembrane domain derived from a CD8 alpha chain, a genus of cytoplasmic domain, a genus of signaling domain, a genus of cytoplasmic domain I, a cytoplasmic domain II or combinations thereof
Claims 11 and 33 encompass a genus of antibody CH2 domain comprising an amino acid sequence having at least 85% sequence identity to the amino acid sequence set forth in SEQ ID NO:33. Claim 13 encompasses a genus of cytoplasmic domain comprising an amino acid sequence having at least 85% sequence identity to the amino acid sequence set forth in SEQ ID NO:42 or 45. Claims 15 and 40 encompass a genus of receptor having at least 85% sequence identity to the amino acid sequence set forth in any one of SEQ ID NOs:43, 52 or 53. Claims 30, 31 and 41 encompass a genus of N-terminal secretory leader sequence including a genus of fragment of a CD8 alpha chain.
Applicant has not disclosed sufficient species for the broad genus of chimeric receptor, the broad genus of extracellular domain, the broad genus of amyloid binding peptide, the broad genus of transmembrane domain, the broad genus of cytoplasmic domain, the broad genus of antibody or antigen binding fragment thereof, the broad genus of amyloid-reactive peptide, the broad genus of cytoplasmic domain comprising a signaling domain of a receptor when activated activating a macrophage and a genus of a globular domain including an immunoglobulin domain.
Response to Arguments
On p. 11-13 of the response, Applicant argues that the specification provides support for: i) the extracellular domain comprising an amyloid-binding peptide or functional fragment thereof including a peptide having a sequence set forth in SEQ ID NOs: 1-18 (see para. [0012]); ii) the CH2 domain or fragment thereof having at least 80%-99% identity to SEQ ID NO:33 (see para.[0013]); iii) the extracellular domain comprising an amyloid-binding peptide or functional fragment thereof together with a CH2 domain including p5 or p5+14, a first spacer and an N-terminal secretory leader sequence (see para.[0080]-[0099], table 2, Fig1 (ii)); iv) peptides p5 and p5+14 set forth in SEQ ID NOs: 1-18 in combination with an IgG2 CH2 domain , a CD8 alpha-derived transmembrane domain and cytoplasmic signaling domain derived from FcR or from FcR and CD19 (see para. [0012]; [0089]-[0099]; table A, [0109]-[0110]; [0141]-[0145]; [0146]-[0155]; [0156]-[0166]); v) the second spacer and transmembrane domain comprising the sequence set forth in SEQ ID NO:40 (para. [0161]); vi) the cytoplasmic domain comprising a cytoplasmic domain I, cytoplasmic domain II or functional fragment thereof or comprising an amino acid sequence having at least 80%-99% identity to any of SEQ ID NOs: 30-31, 41-42 or 45 (see para. [0014]), cytoplasmic domain derived from FcR and CD19 including cytoplasmic domain II of SEQ ID NO:41 and cytoplasmic domain I of SEQ ID NO:42 (see para. [0146]-[0155]; [0161]-[0163]); vii) the full length peptide-based receptor of SEQ ID NO: 43, 52 or 53 and identity variants thereof (see para. [0016]; [0156]-[0166]).
Applicant's arguments have been fully considered but they are not found
persuasive. Contrary to Applicant's arguments, the examiner asserts that based on
MPEP §2163, MPEP §§2163.01-2163.03, the specification fails to provide sufficient
description or information or evidence to demonstrate that Applicant is in possession of
the claimed genus of chimeric receptor having the structures and features recited in amended claim 1 because:
i. There is no well-established structural and functional relationship or correlation
between the claimed genus of chimeric receptor having the structures and features recited in claim 1 or 35 and 124I-m11-1F4 monoclonal antibody (Example 1, Figures 2 and 4A-4D) or p5+14 in binding to human AL amyloid in tissue and PET/CT imaging in patients with AL amyloidosis (Example 1, Figures 5A-B).
The specification only showed reduction in hepatic amyloid load based on 123I-SAP scintigraphy after infusion of monoclonal antibody or biodistribution of AL amyloid (light chain-associated amyloid) based on 124I-m11-1F4 monoclonal antibody (Example 1, Figures 2 and 4A-4D) or p5+14 binding to human AL amyloid in tissue and PET/CT imaging in patients with AL amyloidosis (Example 1, Figures 5A-B).
While the specification describes a hypothetic schematic drawing of the claimed chimeric receptor in figure 1 and prophetic examples of full-length chimeric receptor constructs as shown in Table C (p 45-46, Table C) and the structures of prophetic 11-1F4CARtandem in Table 1, p5+14CARFceR in Table 2 and CAR-P constructs in Table 3, the specification provides no support to demonstrate that Applicant is in possession of the prophetic examples of 11-1F4CARtandem, p5+14CARFcR shown in Tables 1-3 or even the claimed genus of peptide-based chimeric antigen receptor (CAR) because the CAR exerts effects through both target binding and intracellular signaling in view of Kim et al. (JCI, Insight, 2014; 9:e175015).
The specification fails to provide support to demonstrate that the prophetic examples of 11-1F4CARtandem, p5+14CARFcR shown in Tables 1-3 or the claimed genus of chimeric receptor can target to amyloid beta as p5+14 binding to human AL amyloid in tissue and PET/CT imaging in patients with AL amyloidosis, or to activate macrophages in vitro or in vivo to clear AL amyloidosis.
ii. There is no well-established structural and functional relationship or correlation between the claimed genus of chimeric receptor or variants recited in claims 1, 15, 35 and 40 and a functional peptide-based CAR-P/CAR that binds to human AL amyloid in tissue and PET/CT imaging in patients with AL amyloidosis as p5+14 binding to human AL amyloid in tissue and PET/CT imaging in patients with AL amyloidosis or in reducing hepatic amyloid load or biodistribution of AL amyloid as m11-1F4 monoclonal antibody.
There is no structural and functional relationship or correlation between the prophetic examples of 11-1F4CARtandem, p5+14CARFcR shown in Tables 1-3 and the 124I-m11-1F4 monoclonal antibody or p5+14 in reducing hepatic amyloid load or biodistribution of AL amyloid (light chain-associated amyloid) based on 124I-m11-1F4 monoclonal antibody (Example 1, Figures 2 and 4A-4D) or p5+14 in binding to human AL amyloid in tissue and PET/CT imaging in patients with AL amyloidosis (Example 1, Figures 5A-B).
There is also no structural and functional relationship or correlation between the claimed genus of peptide-based chimeric receptor and variants thereof recited in claims 1, 15, 35 and 40 and the 124I-m11-1F4 monoclonal antibody or p5+14 in reducing hepatic amyloid load or biodistribution of AL amyloid (light chain-associated amyloid) based on 124I-m11-1F4 monoclonal antibody (Example 1, Figures 2 and 4A-4D) or p5+14 in binding to human AL amyloid in tissue and PET/CT imaging in patients with AL amyloidosis (Example 1, Figures 5A-B).
iii. The specification fails to provide sufficient description or information as to what other common structures and sequences are required by the claimed genus of chimeric receptor and variants thereof recited in claims 1, 15, 35 and 40 and a functional peptide-based CAR-P/CAR that binds to human AL amyloid in tissue and PET/CT imaging in patients with AL amyloidosis as p5+14 binding to human AL amyloid in tissue and PET/CT imaging in patients with AL amyloidosis or in reducing hepatic amyloid load or biodistribution of AL amyloid as m11-1F4 monoclonal antibody.
The specification fails to provide sufficient description or information as to what other common structures and sequences are required by the claimed genus of extracellular domain comprising an amyloid-binding peptide or functional fragment thereof and an antibody CH2 domain or fragment thereof or variant thereof and a functional peptide-based CAR-P/CAR that binds to human AL amyloid in tissue and PET/CT imaging in patients with AL amyloidosis as p5+14 binding to human AL amyloid in tissue and PET/CT imaging in patients with AL amyloidosis or in reducing hepatic amyloid load or biodistribution of AL amyloid as m11-1F4 monoclonal antibody.
The specification fails to provide sufficient description or information as to what other common structures and sequences are required by the claimed genus of transmembrane domain derived from a CD8 alpha-chain or variants thereof recited in claim 38 and a functional peptide-based CAR-P/CAR that binds to human AL amyloid in tissue and PET/CT imaging in patients with AL amyloidosis as p5+14 binding to human AL amyloid in tissue and PET/CT imaging in patients with AL amyloidosis or in reducing hepatic amyloid load or biodistribution of AL amyloid as m11-1F4 monoclonal antibody.
The specification fails to provide sufficient description or information as to what other common structures and sequences are required by the claimed genus of cytoplasmic domain comprising a signaling domain selected from a cytoplasmic domain I and/or a cytoplasmic domain II or variants thereof in claim 13 and a functional peptide-based CAR-P/CAR that binds to human AL amyloid in tissue and PET/CT imaging in patients with AL amyloidosis as p5+14 binding to human AL amyloid in tissue and PET/CT imaging in patients with AL amyloidosis or in reducing hepatic amyloid load or biodistribution of AL amyloid as m11-1F4 monoclonal antibody.
Since the common characteristics/features of the claimed genus of chimeric receptor or variants thereof, other chimeric receptors of the prophetic examples of p5+14CARFcR or full length chimeric receptor constructs shown in Table 3 or Table C or are unknown, a skilled artisan cannot envision the functional correlations of the prophetic examples of full length chimeric receptor constructs shown in Table 3 or Table C or the claimed genus of chimeric receptor with the claimed invention in view of Burgess et al. (J of Cell Bio. 1990, 111:2129-2138, cited previously), Bowie et al. (see col 2, p. 1306, Bowie et al. Science, 1990, 247:1306-1310, cited previously), Pawson et al. (see p. 445 the second column, first paragraph, Pawson et al. 2003, Science 300:445-452, cited previously), Alaoui-lsmaili et al. (see p. 502, right col., 2th paragraph; Alaoui-lsmaili et al., Cytokine Growth Factor Rev. 2009; 20:501-507, cited previously), Guo et al. (see p. 9207, left col., 2th paragraph, Guo et al., PNAS 2004; 101:9205-9210, cited previously) and Rudikoff et al. (see p. 1979; Proc.Natl. Acad. Sci. USA 1982 Vol. 79: page 1979, cited previously).
Accordingly, in the absence of sufficient recitation of distinguishing identifying characteristics, the specification does not provide adequate written description of the genus of chimeric receptor or variants thereof, the genus of extracellular domain, the genus of amyloid binding peptide, the genus of transmembrane domain, the genus of cytoplasmic domain comprising a signaling domain selected from a genus of cytoplasmic domain I and/or II.
Based on MPEP § 2161.01 and §2163, “to satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. See, e.g., Moba, B.V. v. Diamond Automation, Inc., 325 F.3d 1306, 1319, 66 USPQ2d 1429, 1438 (Fed. Cir. 2003); Vas-Cath, Inc. v. Mahurkar, 935 F.2d at 1563, 19 USPQ2d at 1116”.
Vas-Cath Inc. v. Mahurkar, 19USPQ2d 1111, clearly states “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the ‘written description’ inquiry, whatever is now claimed.” (See page 1117.) The specification does not “clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed.” (See Vas-Cath at page 1116).
As discussed above, the skilled artisan cannot envision the detailed chemical structure of the encompassed genus of chimeric receptor, the genus of extracellular domain comprising a genus of amyloid binding peptide and a genus of an antibody CH2 domain, the genus of transmembrane domain, the genus of cytoplasmic domain comprising a signaling domain selected from a cytoplasmic domain I and/or II; and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating it. The compound itself is required. See Fiers v. Revel, 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. One cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481 at 1483.
Therefore, the claimed chimeric receptor has not met the written description provision of 35 U.S.C. §112, first paragraph. Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. §112 is severable from its enablement provision (see page 1115). Applicant is directed to the Guidelines for the Examination of Patent Applications Under the 35 U.S.C. 112, ¶ 1 "Written Description" Requirement. See MPEP § 2161.01 and 2163.
Accordingly, the rejection of claims 1, 9-15, 27 and 30-41 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 is maintained.
Conclusion
8. NO CLAIM IS ALLOWED.
9. The prior art made of record and not relied upon is considered pertinent to applicant's disclosure.
Morrissey et al. (eLife, 2018; 7:e36688; DOI: doi.org/10.7554/eLife.36688.001) teaches chimeric antigen receptors for phagocytosis (CAR-Ps) comprising an extracellular single chain antibody variable fragment (scFv) recognizing CD19 (aCD19), and the CD8 transmembrane domain present in the aCD19 CAR-T and a cytoplasmic domain from Megf10 and FcRg and a tandem PI3K recruitment domain (see abstract; p.2-7).
Wall et al. (PNAS, 2018; 115: E10839-10848. www.pnas.org/cgi/doi/pnas.1805515115) teach a peptope p66 comprising p5+14 fused to a linear epitope that is recognized by the 11-1F4mAb (see abstract; p. E10840-E10843, figure 1 and E10846, Materials and Methods-peptides/antibodies).
Wall et al. (US20160243230) teaches amyloid-reactive peptides including p5 or p5+14 and fusion peptides thereof, which comprises instant SEQ ID NO:1 and the method of treating amyloid deposition diseases using the amyloid-reactive peptides including p5 or p5+14 and fusion peptides thereof (see the sequence alignment; abstract; [0068]-[0069]; [0077]; [0102]; [0115]-[0139], tables 1-3, [0152];).
Elson et al. (US2017/0298129) teaches a fusion protein comprising an interest of protein joined directly or indirectly via a spacer to the antibody CH2 domain or fragment thereof that comprises an amino acid sequence at least 85% identical to the amino acid sequence of SEQ ID NO:33 as recited in claims 10-11 (see SEQ ID NO:59; para. [0012]-[0015]; [0131]; claims 1-4, 8 and 21).
Rosenthal (US2019/0233496) teaches a chimeric receptor having the structures described in Figures 1-4,8A,9A, 13A, 15A (
PNG
media_image1.png
156
744
media_image1.png
Greyscale
), wherein the chimeric receptor comprises: (1) an extracellular ligand-binding domain, wherein the ligand is an agent associated with a neurological disease, disorder, or injury; (2) a transmembrane domain; and (3) a signaling domain, wherein binding of the ligand to the chimeric receptor expressed in an immune cell activates the signaling domain, and the activated signaling domain induces and/or enhances (i) cell survival of the immune cell, (ii) proliferation of the immune cell, (iii) migration of the immune cell, (iv) functionality of the immune cell, or any combination thereof including macrophages (see figure 1A; [0008]-[0009];[0026]; [0085]-[0102]; [0100]; [0105]-[0107]; [0111]-[0112]; [0164]-[0166]; [0238]; Examples 26-29, claims 1-4, 6, 8-9, 11, 13, 15, 17-24, 27, 29-33, 35, 37-42, 44, 46-48, 50-55, 62-70, 74, 87), and wherein the extracellular ligand binding domain of the chimeric receptor includes an antibody, a single-domain antibody, humanized antibody or scFv, anti-Abeta scFv ([0087]-[0088]; [0220]) and the ligand includes amyloid beta ([0009]; [0111]; [0164]-[0166]; [0238], Examples 26-29); and wherein the chimeric receptor includes further comprising a flexible linker between the transmembrane domain and the signaling domain (see [0085]-[0112]), and wherein the cytoplasmic domain comprising a signal domain of receptor when activated activates a macrophage (see [0238], Example 26-29).
US20190083616 teaches an amyloid-reactive peptide comprising SEQ ID NO:1 which is 100% identical to instant SEQ ID NO:1 (see the sequence alignment below).
SEQ ID NO:1
Sequence 1, US/16036900
Publication No. US20190083616A1
GENERAL INFORMATION
APPLICANT: UNIVERSITY OF TENNESSEE RESEARCH FOUNDATION
TITLE OF INVENTION: TARGETING IMMUNOTHERAPY FOR AMYLOIDOSIS
FILE REFERENCE: 05820.004US3
CURRENT APPLICATION NUMBER: US/16/036,900
CURRENT FILING DATE: 2018-07-16
PRIOR APPLICATION NUMBER: 15/052,772
PRIOR FILING DATE: 2016-02-24
PRIOR APPLICATION NUMBER: PCT/US2015/046523
PRIOR FILING DATE: 2015-08-24
PRIOR APPLICATION NUMBER: 62/041,888
PRIOR FILING DATE: 2014-08-26
NUMBER OF SEQ ID NOS: 56
SEQ ID NO 1
LENGTH: 26
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Description of Artificial Sequence: Synthetic
peptide
FEATURE:
OTHER INFORMATION: Peptide p5
Query Match 100.0%; Score 121; Length 26;
Best Local Similarity 100.0%;
Matches 26; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 KAQKAQAKQAKQAQKAQKAQAKQAKQ 26
||||||||||||||||||||||||||
Db 1 KAQKAQAKQAKQAQKAQKAQAKQAKQ 26
US9683017 teaches an amyloid-reactive peptide comprising SEQ ID NO:16 which is 100% identical to instant SEQ ID NO:1 (see the sequence alignment below).
SEQ ID NO:1
US-14-801-717A-16
(NOTE: this sequence has 20 duplicates in the database searched)
Sequence 16, US/14801717A
Patent No. 9683017
GENERAL INFORMATION
APPLICANT: Wall, Jonathan S.
APPLICANT: Kennel, Stephen J.
APPLICANT: Sparer, Timothy E.
TITLE OF INVENTION: Inhibitory Peptides of Viral Infection
FILE REFERENCE: UTK-0236NP
CURRENT APPLICATION NUMBER: US/14/801,717A
CURRENT FILING DATE: 2015-07-16
PRIOR APPLICATION NUMBER: 62/025,912
PRIOR FILING DATE: 2012-11-01
NUMBER OF SEQ ID NOS: 25
SEQ ID NO 16
LENGTH: 26
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Heparin Binding Peptide Synthetic Construct
FEATURE:
NAME/KEY: PEPTIDE
LOCATION: (1)..(26)
Query Match 100.0%; Score 121; Length 26;
Best Local Similarity 100.0%;
Matches 26; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 KAQKAQAKQAKQAQKAQKAQAKQAKQ 26
||||||||||||||||||||||||||
Db 1 KAQKAQAKQAKQAQKAQKAQAKQAKQ 26
US10046050 teaches an amyloid-reactive peptide comprising SEQ ID NO:1 which is 100% identical to instant SEQ ID NO:1 (see the sequence alignment below).
SEQ ID NO:1
Sequence 1, US/15052772
Patent No. 10046050
GENERAL INFORMATION
APPLICANT: UNIVERSITY OF TENNESSEE RESEARCH FOUNDATION
TITLE OF INVENTION: TARGETING IMMUNOTHERAPY FOR AMYLOIDOSIS
FILE REFERENCE: 05820.P004U1
CURRENT APPLICATION NUMBER: US/15/052,772
CURRENT FILING DATE: 2016-02-24
PRIOR APPLICATION NUMBER: PCT/US2015/046523
PRIOR FILING DATE: 2015-08-24
PRIOR APPLICATION NUMBER: 62/041,888
PRIOR FILING DATE: 2014-08-26
NUMBER OF SEQ ID NOS: 56
SEQ ID NO 1
LENGTH: 26
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Description of Artificial Sequence: Synthetic
peptide
FEATURE:
OTHER INFORMATION: Peptide p5
Query Match 100.0%; Score 121; Length 26;
Best Local Similarity 100.0%;
Matches 26; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 KAQKAQAKQAKQAQKAQKAQAKQAKQ 26
||||||||||||||||||||||||||
Db 1 KAQKAQAKQAKQAQKAQKAQAKQAKQ 26
US10213506 teaches an amyloid-reactive peptide comprising SEQ ID NO:1 which is 100% identical to instant SEQ ID NO:1 (see the sequence alignment below).
SEQ ID NO:1
Sequence 1, US/15504512
Patent No. 10213506
GENERAL INFORMATION
APPLICANT: UNIVERSITY OF TENNESSEE RESEARCH FOUNDATION
TITLE OF INVENTION: TARGETING IMMUNOTHERAPY FOR AMYLOIDOSIS
FILE REFERENCE: 05820.004US2
CURRENT APPLICATION NUMBER: US/15/504,512
CURRENT FILING DATE: 2017-02-16
PRIOR APPLICATION NUMBER: PCT/US2015/046523
PRIOR FILING DATE: 2015-08-24
PRIOR APPLICATION NUMBER: 62/041,888
PRIOR FILING DATE: 2014-08-26
NUMBER OF SEQ ID NOS: 25
SEQ ID NO 1
LENGTH: 26
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Peptide p5
Query Match 100.0%; Score 121; Length 26;
Best Local Similarity 100.0%;
Matches 26; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 KAQKAQAKQAKQAQKAQKAQAKQAKQ 26
||||||||||||||||||||||||||
Db 1 KAQKAQAKQAKQAQKAQKAQAKQAKQ 26
US12139529 teaches an amyloid-reactive peptide comprising SEQ ID NO:1 which is 100% identical to instant SEQ ID NO:1 (see the sequence alignment below).
SEQ ID NO:1
Sequence 1, US/18298953
Patent No. 12139529
GENERAL INFORMATION
APPLICANT: UNIVERSITY OF TENNESSEE RESEARCH FOUNDATION (en)
TITLE OF INVENTION: ANTIBODY-PEPTIDE FUSION PROTEINS FOR TREATING AMYLOID DISORDERS (en)
FILE REFERENCE: 16599-20006.01
CURRENT APPLICATION NUMBER: US/18/298,953
CURRENT FILING DATE: 2023-04-11
NUMBER OF SEQ ID NOS: 92
SEQ ID NO 1
LENGTH: 26
TYPE: PRT
FEATURE:
NAME/KEY: REGION
LOCATION: 1..26
QUALIFIERS: note = Synthetic Construct
FEATURE:
NAME/KEY: source
LOCATION: 1..26
QUALIFIERS: mol_type = protein
organism = synthetic construct
Query Match 100.0%; Score 121; Length 26;
Best Local Similarity 100.0%;
Matches 26; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 KAQKAQAKQAKQAQKAQKAQAKQAKQ 26
||||||||||||||||||||||||||
Db 1 KAQKAQAKQAKQAQKAQKAQAKQAKQ 26
US12157765 teaches an amyloid-reactive peptide comprising SEQ ID NO:1 which is 100% identical to instant SEQ ID NO:1 (see the sequence alignment below).
SEQ ID NO:1
Sequence 1, US/18660156
Patent No. 12157765
GENERAL INFORMATION
APPLICANT: Attralus, Inc. (en)
TITLE OF INVENTION: MODIFIED IMMUNOGLOBULINS FOR TARGETING AMYLOID DEPOSITS (en)
FILE REFERENCE: 16599-20001.10
CURRENT APPLICATION NUMBER: US/18/660,156
CURRENT FILING DATE: 2024-05-09
NUMBER OF SEQ ID NOS: 83
SEQ ID NO 1
LENGTH: 26
TYPE: PRT
FEATURE:
NAME/KEY: REGION
LOCATION: 1..26
QUALIFIERS: note = Synthetic Construct
FEATURE:
NAME/KEY: source
LOCATION: 1..26
QUALIFIERS: mol_type = protein
organism = synthetic construct
Query Match 100.0%; Score 121; Length 26;
Best Local Similarity 100.0%;
Matches 26; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 KAQKAQAKQAKQAQKAQKAQAKQAKQ 26
||||||||||||||||||||||||||
Db 1 KAQKAQAKQAKQAQKAQKAQAKQAKQ 26
US12264195 teaches an amyloid-reactive peptide comprising SEQ ID NO:1 which is 100% identical to instant SEQ ID NO:1 (see the sequence alignment below).
SEQ ID NO:1
Sequence 1, US/18660162
Patent No. 12264195
GENERAL INFORMATION
APPLICANT: Attralus, Inc. (en)
TITLE OF INVENTION: MODIFIED IMMUNOGLOBULINS FOR TARGETING AMYLOID DEPOSITS (en)
FILE REFERENCE: 16599-20001.11
CURRENT APPLICATION NUMBER: US/18/660,162
CURRENT FILING DATE: 2024-05-09
NUMBER OF SEQ ID NOS: 83
SEQ ID NO 1
LENGTH: 26
TYPE: PRT
FEATURE:
NAME/KEY: REGION
LOCATION: 1..26
QUALIFIERS: note = Synthetic Construct
FEATURE:
NAME/KEY: source
LOCATION: 1..26
QUALIFIERS: mol_type = protein
organism = synthetic construct
Query Match 100.0%; Score 121; Length 26;
Best Local Similarity 100.0%;
Matches 26; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 KAQKAQAKQAKQAQKAQKAQAKQAKQ 26
||||||||||||||||||||||||||
Db 1 KAQKAQAKQAKQAQKAQKAQAKQAKQ 26
US8808666 teaches an amyloid-reactive peptide comprising SEQ ID NO:13 which is 100% identical to instant SEQ ID NO:1 (see the sequence alignment below).
SEQ ID NO:1
US-13-627-138-13
(NOTE: this sequence has 3 duplicates in the database searched)
Sequence 13, US/13627138
Patent No. 8808666
GENERAL INFORMATION
APPLICANT: WALL, Jonathan
APPLICANT: KENNEL, Stephen
TITLE OF INVENTION: PEPTIDES THAT SPECIFICALLY TARGET AMYLOID DEPOSITS
FILE REFERENCE: UTK-0230
CURRENT APPLICATION NUMBER: US/13/627,138
CURRENT FILING DATE: 2012-09-26
PRIOR APPLICATION NUMBER: US 61/318,083
PRIOR FILING DATE: 2010-03-26
PRIOR APPLICATION NUMBER: PCT/US2011/029430
PRIOR FILING DATE: 2011-03-22
NUMBER OF SEQ ID NOS: 32
SEQ ID NO 13
LENGTH: 31
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Synthetic
Query Match 100.0%; Score 121; Length 31;
Best Local Similarity 100.0%;
Matches 26; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 KAQKAQAKQAKQAQKAQKAQAKQAKQ 26
||||||||||||||||||||||||||
Db 6 KAQKAQAKQAKQAQKAQKAQAKQAKQ 31
10. THIS ACTION IS MADE FINAL. 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.
11. Any inquiry concerning this communication or earlier communications from the examiner should be directed to CHANG-YU WANG whose telephone number is (571)272-4521. The examiner can normally be reached Monday-Thursday, 7:00am-5:00pm EST.
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, Jeffrey Stucker can be reached at 571-272-0911. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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Chang-Yu Wang
July 14, 2026
/CHANG-YU WANG/Primary Examiner, Art Unit 1675
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