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
Status of Application/Election/Restrictions
Applicant’s election without traverse of Group I (claims 18, 23-31, 37-43, 45, 48-59 and 71-73), SEQ ID NO:5 for species of first peptide, SEQ ID NO:18 for species of second peptide, RR for species of linker 1 and GG for species of linker 2 in the reply filed on July 9, 2026 is acknowledged.
Claims 1-17, 19-22, 32-36, 44, 46-47, 66-67 and 70 are canceled. Claims 28, 31, 51, 59, 63-64 and 68 are amended. Claims 18, 23-31, 37-43, 45, 48-65, 68-69 and 71-76 are pending in this application. Claims 60-65, 68-69 and 74-76 are withdrawn without traverse (filed 07/09/2026) from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected inventions, there being no allowable generic or linking claim. Claims 25-26 and 31 are also withdrawn from further consideration because of non-elected sequences. Election was made without traverse in the reply filed on July 9, 2026.
Claims 18, 23-24, 27-30, 37-43, 45, 48-59 and 71-73 are under examination with respect to SEQ ID NO:5 for the first peptide, SEQ ID NO:18 for the second peptide, RR for the linker 1 and GG for the linker 2 in this office action.
Specification
The disclosure is objected to because of the following informalities: The use of the term “AddaVaxTM” “MF59®” (p. 3, [0011]), which is a trade name or a mark used in commerce, has been noted in this application. The term should be accompanied by the generic terminology; furthermore the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks. Appropriate correction is required.
Claim Rejections
Claims 52 and 54 are objected to because of the following informalities: Based on p. 3, [0011] of the instant specification, the spelling of “OS-21, TOL1055, OS-18, OS-17, OS-7” recited in claims 52 and 54 is incorrect. In addition, they are not common or unique abbreviations in the art. Applicants are required to spell out “QS-21, TQL1055, QS-18, QS-17, QS-7” at the first usage. Appropriate correction is required.
Improper Markush Grouping
Claims 23-24 and 27-31 are rejected on the basis that it contains an improper Markush grouping of alternatives. See In re Harnisch, 631 F.2d 716, 721-22 (CCPA 1980) and Ex parte Hozumi, 3 USPQ2d 1059, 1060 (Bd. Pat. App. & Int. 1984). A Markush grouping is proper if the alternatives defined by the Markush group (i.e., alternatives from which a selection is to be made in the context of a combination or process, or alternative chemical compounds as a whole) share a “single structural similarity” and a common use. A Markush grouping meets these requirements in two situations. First, a Markush grouping is proper if the alternatives are all members of the same recognized physical or chemical class or the same art-recognized class, and are disclosed in the specification or known in the art to be functionally equivalent and have a common use. Second, where a Markush grouping describes alternative chemical compounds, whether by words or chemical formulas, and the alternatives do not belong to a recognized class as set forth above, the members of the Markush grouping may be considered to share a “single structural similarity” and common use where the alternatives share both a substantial structural feature and a common use that flows from the substantial structural feature. See MPEP § 706.03(y).
The Markush grouping of different SEQ ID NOs: 2-37 in claims 23-24; SEQ ID NOs: 5-9, 13-16, 20-22, 26-27 and 31 and SEQ ID NOs: 2-96 in claims 27-31 is improper because the alternatives defined by the Markush grouping do not share both a single structural similarity and a common use for the following reasons:
The recited alternative species do not share a single structural similarity, as each species of peptides of SEQ ID NOs: has a different chemical structure because it comprises different amino acid sequences. Each peptide has a different activity or immunogenicity or forms different epitopes. Thus, the different peptides with different SEQ ID NOs: do not share a single structural similarity or biological activity.
To overcome this rejection, Applicant may set forth each alternative (or grouping of patentably indistinct alternatives) within an improper Markush grouping in a series of independent or dependent claims and/or present convincing arguments that the group members recited in the alternative within a single claim in fact share a single structural similarity as well as a common use.
Claim Rejections - 35 USC § 112
7. 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.
Claims 18, 23-24, 27-30, 37-43, 45, 48-59 and 71-73 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 pre-AIA the applicant regards as the invention.
Claims 18, 23-24, 27-30, 37-43, 45, 48-59 and 71-73 are indefinite because:
i. Claim 18 recites the limitation “linker 1 and linker 2 may be the same or different”. It is unclear what Applicant intended to include within the scope of the claim. For examination purposes, the limitation is interpreted as “linker 1 and linker 2 are the same or different”.
ii. Claims 27 and 31 recite the limitation “the group consisting of any one ….or SEQ ID NO:31”, which are Markush claims. A ‘‘Markush’’ claim recites a list of alternatively useable species; and is commonly formatted is: ‘‘selected from the group consisting of A, B, and C’’. However, the instant claims recite the format as “the group consisting of….. or…”, which renders the claim indefinite.
iii. Claims 52 and 54 contain the trademark/trade name “AddaVaxTM” “MF59®”. Where a trademark or trade name is used in a claim as a limitation to identify or describe a particular material or product, the claim does not comply with the requirements of 35 U.S.C. 112, second paragraph. See Ex parte Simpson, 218 USPQ 1020 (Bd. App. 1982). The claim scope is uncertain since the trademark or trade name cannot be used properly to identify any particular material or product. A trademark or trade name is used to identify a source of goods, and not the goods themselves. Thus, a trademark or trade name does not identify or describe the goods associated with the trademark or trade name. In the present case, the trademark/trade name is used to identify/describe a specific adjuvant and, accordingly, the identification/description is indefinite
iv. Regarding claims 52 and 54, the phrase "such as" renders the claim indefinite because it is unclear whether the limitations following the phrase are part of the claimed invention. See MPEP § 2173.05(d).
v. The rest of claims are indefinite as depending from an indefinite claim.
8. In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
Claim Rejections - 35 USC § 102
9. The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 18, 23-24, 27-30, 37, 41-43, 45 and 48 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Haque et al. (US20150361148, published on Dec 17, 2015, priority Jun 13, 2014).
Claims 18, 23-24, 27-30, 37, 41-43, 45 and 48 are drawn to a peptide comprising the structure:
[first peptide]-[linker 1]-[second peptide]-[linker 2]-[Cys],
wherein, the first peptide and the second peptide are the same or different and comprise 3-10 amino acids from residues 1-10 of SEQ ID NO:01 or from residues 12-25 of SEQ ID NO:01, and each of linker 1, linker 2 and [Cys] are optional, and linker 1 and linker 2 may be the same or different.
Haque et al. (US20150361148) teaches a polypeptide having the structure of [X-Y]n, wherein X is absent or is a linker and Y is a human amyloid peptide and n is an integer between 2 and 8 inclusive, and wherein the polypeptide includes a polypeptide comprising SEQ ID NO:14, which comprises -DAEFRHD(Abeta 1-7; instant SEQ ID NO:5)..-RR-EFRHDSG (Abeta 3-9; instant SEQ ID NO:18) (see the sequence alignment below; para. [0053]-[0056]; [0059]). The polypeptide disclosed by Haque meets the limitation recited in instant claims 18, 23-24, 27-30, 37, 41-43, 45 and 48 because independent claim 18 recites the limitation “each of linker 1, linker 2 and [Cys] are optional” and the claimed first and/or second peptide do not exclude Abeta 1-42. The linker of RR disclosed in Haque’s polypeptide is a cleavable linker as in claim 41 based on para. [0047] of the instant specification (based on the published application). Haque teaches an immunotherapy comprising the polypeptide or the polypeptide with a linker or a carrier including as in claims 42-43 and 45 (see para. [0058]-[0059]), or further comprising at least one pharmaceutically acceptable diluent as in claim 48 (see para. [0112]), or liposomes (see para. [0117];[0119]; para. [0117]-[0120]). Thus, claims 18, 23-24, 27-30, 37, 41-43, 45 and 48 are anticipated by Haque et al. (US20150361148).
SEQ ID NO:5-linker1-SEQ ID NO:18-linker2-Cys
US-14-738-016-41
Sequence 41, US/14738016
Publication No. US20150361148A1
GENERAL INFORMATION
APPLICANT: WHITEHEAD INSTITUTE FOR BIOMEDICAL RESEARCH
TITLE OF INVENTION: AMYLOID BETA EXPRESSION CONSTRUCTS
FILE REFERENCE: 26495-0016001
CURRENT APPLICATION NUMBER: US/14/738,016
CURRENT FILING DATE: 2015-06-12
PRIOR APPLICATION NUMBER: 62/012,107
PRIOR FILING DATE: 2014-06-13
NUMBER OF SEQ ID NOS: 105
SEQ ID NO 41
LENGTH: 190
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Description of Artificial Sequence: Synthetic
polypeptide
Query Match 59.9%; Score 66.5; Length 190;
Best Local Similarity 31.4%;
Matches 16; Conservative 0; Mismatches 0; Indels 35; Gaps 2;
Qy 1 DAEFRHD---------------------------------RR--EFRHDSG 16
||||||| || |||||||
Db 25 DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVRRDAEFRHDSG 75
Claim Rejections - 35 USC § 102
10. Claims 18, 23-24, 27-30, 37-43, 45, 48-59 and 71-73 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Imbimbo et al. (US20100028353, published on Feb 4, 2010, priority Jul 15, 2008) as evidenced by WO2005/058940.
Imbimbo et al. (US20100028353) teaches a polypeptide having the structure of [Ab1-7]n, wherein Ab1-7 is the sequence of DAEFRHD (instant SEQ ID NO:5) and n is 2-15, 3-12 or 3, 6, 9 or 12, and wherein the polypeptide includes a polypeptide comprising SEQ ID NO:7, which comprises -DAEFRHD (Abeta 1-7; instant SEQ ID NO:5)-GGP-DAEFRHD-GGP- (which comprises 5 amino acids -EFRHD- from instant SEQ ID NO:18: -EFRHDSG-) (see the sequence alignment below; para. [0037]-[. Tab;e 1; [0059]). The polypeptide disclosed by Imbimbo meets the limitation recited in instant claims 18, 23-24, 27-30, 37-43, 45, 48-59 and 71-73 because independent claim 18 recites the limitation “each of linker 1, linker 2 and [Cys] are optional”, the linker 1 or/and linker 2 are not limited to any specific sequence. The linker of GGP disclosed in Haque’s polypeptide is a cleavable linker as in claim 41 based on para. [0047] of the instant specification (based on para. of the published application). Imbimbo teaches that the polypeptide linker further comprises a C-terminal cysteine (C) as in claim 39 (see para. [0036]), the peptide further comprises a blocked amine at the N-terminus as in claim 40 (see para. [004]). Imbimbo teaches an immunotherapy comprising the polypeptide or the polypeptide with a linker or a carrier including bacterial thioredoxin (Trx) and carriers disclosed in WO2005/058940, which includes serum albumin, Ig molecules, thyroglobulin, ovalbumin, tetanus toxoid (TT), diphtheria toxoid (DT), CRM of diphtheria, CRM197, OMPC and H. influenza protein D, rEPA, KLH and flagellin as in claims 42-43 and 45 (see para. [0008]-[0013]; [0023]; [0041] and see para. [0073]-[0083]; [0111]-[0129] of WO2005/058940), or further comprising at least one pharmaceutically acceptable diluent as in claim 48 (see para. [0053]-[0054]) or a multiple antigen presenting system (MAP) comprising helper T-cell epitopes, immune stimulating lipophilic moieties as in claims 49-50 (see para. [0008]-[0013]; [0055]-[0061]; [0062]). Imbimbo teaches a pharmaceutical composition comprising the polypeptide and at least one adjuvant including aluminum hydroxide, aluminum phosphate, aluminum sulfate, MPL, saponins such as QS-21, oil-based adjuvants, virosomes, dsRNA, oil in water emulsions, CpG and combinations thereof as in claims 53-59 (see para. [0055]-[0061]) and an immunization kit comprising the immunotherapy composition in a first container and further comprising an adjuvant in a second container as in claims 71-73 (see para. [0055]-[0061]; [0060]). Thus, claims 18, 23-24, 27-30, 37-43, 45, 48-59 and 71-73 are anticipated by Imbimbo et al. (US20100028353).
SEQ ID NO:5-linker1:RR-SEQ ID NO:18-linker2:GG-Cys
US-12-503-490-7
Sequence 7, US/12503490
Publication No. US20100028353A1
GENERAL INFORMATION
APPLICANT: IMBIMBO, BRUNO PIETRO
APPLICANT: OTTONELLO, SIMONE
APPLICANT: VILLETTI, GINO
APPLICANT: MORETTO, NADIA
TITLE OF INVENTION: ANTI-AMYLOID IMMUNOGENIC COMPOSITIONS, METHODS AND USES
FILE REFERENCE: 344029US0
CURRENT APPLICATION NUMBER: US/12/503,490
CURRENT FILING DATE: 2009-10-06
PRIOR APPLICATION NUMBER: EP 08012716.0
PRIOR FILING DATE: 2008-07-15
NUMBER OF SEQ ID NOS: 24
SEQ ID NO 7
LENGTH: 32
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Description of Artificial Sequence: Synthetic polypeptide
Query Match 57.6%; Score 63.9; Length 32;
Best Local Similarity 51.7%;
Matches 15; Conservative 0; Mismatches 3; Indels 11; Gaps 2;
Qy 1 DAEFRHD---RREFRHDSG--------GG 18
||||||| ||||| | ||
Db 3 DAEFRHDGGPDAEFRHDGGPDAEFRHDGG 31
Claim Rejections - 35 USC § 102
11. Claims 18, 23-24, 27-30, 37-43, 45 and 48-59 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Arumugham et al. (US2007/0134762, published Jun 14, 2007, priority Dec 17, 2003).
Arumugham et al. (US2007/0134762) teaches a peptide immunogen comprising Ab1-5, 1-6, 1-7, 1-10, 3-7, 1-4 or 1-5 or 16-25, 16-22, 16-23, 17-23, 17-24, 18-24 or 18-25 (see para.[0030]-[0031]; [0090]-[0095]; p. 6-8), or multimers of monomeric immunogenic peptides, formula 2x, x is 1-5(see para. [0099]-[0103]; [0104]-[0108]), or with a linker or/and a carrier, such as Ab1-5-L, Ab 1-6-L, Ab 1-7-L, Ab 1-9-L; Ab1-5-C, Ab 1-6-C, Ab 1-7-C, Ab 1-9-C; Ab1-5-L-C, Ab 1-6-L-C, Ab 1-7-L-C, Ab 1-9-L-C, wherein L is a linker and C is a cysteine (see para. [0030]-[0031];[0115]-[0138]); and wherein the polypeptide includes a polypeptide comprising SEQ ID NO:27-39 or 20, which comprises -DAEFRHD(Abeta 1-7; instant SEQ ID NO:5)-DA-EFRHDA (which comprises 5 amino acids -EFRHD- from instant SEQ ID NO:18 (Abeta 3-9): -EFRHDSG-) (see the sequence alignment below; para. [[0104]-[0108]). Arumugham teaches that the linker includes polylysine, Gly, Gly-Gly, Ser, Ser-Ser (see para.[0129]; [0133]); and the carrier includes serum albumin, Ig molecules, thyroglobulin, ovalbumin, tetanus toxoid (TT), diphtheria toxoid (DT), CRM of diphtheria, CRM197, OMPC and H. influenza protein D, rEPA, KLH and flagellin as in claims 42-43 and 45 (see para.[0011]-[0023] [0074]-[0095]). The polypeptide disclosed by Arumugham meets the limitation recited in instant claims 18, 23-24, 27-30, 37-43, 45 and 48-59 because independent claim 18 recites the limitation “each of linker 1, linker 2 and [Cys] are optional” and the linker is not limited to a specific linker. The linker disclosed in Arumugham’s polypeptide is a cleavable linker as in claim 41 based on para. [0047] of the instant specification (based on the published application). Arumugham teaches that the peptide linker further comprises a C-terminal cysteine (C) as in claim 39 (see para. [0030]), the peptide further comprises a blocked amine at the N-terminus as in claim 40 (see para. [0034]; [0116]-[0119]). Arumugham teaches an immunotherapy comprising the polypeptide or the polypeptide with a linker or a carrier including serum albumin, Ig molecules, thyroglobulin, ovalbumin, tetanus toxoid (TT), diphtheria toxoid (DT), CRM of diphtheria, CRM197, OMPC and H. influenza protein D, rEPA, KLH and flagellin as in claims 42-43 and 45 (see para.[0011]-[0023] [0074]-[0095], [0137]; claims 371-372, 378-379, 385, 389-390; 393-394; 398-399) or further comprising at least one pharmaceutically acceptable diluent as in claim 48 (see para. [0054]; [0149]) or a multiple antigen presenting system (MAP) comprising helper T-cell epitopes, immune stimulating lipophilic moieties, self-assembling nanoparticles as antigen-presenting platforms and gold nanoparticles as in claims 49-50 (see para. [0029]; [0108]; [0201]-[0206], Example 8). Arumugham teaches a pharmaceutical composition comprising the polypeptide and at least one adjuvant including aluminum hydroxide, aluminum phosphate, aluminum sulfate, MPL, QS-21, CFA, IFA, oil in water emulsions, CpG, polyglutamic acid, polylysine, and combinations thereof as in claims 53-59 (see para. [0158]-[0160]; claims 396-401). Thus, claims 18, 23-24, 27-30, 37-43, 45 and 48-59 are anticipated by Arumugham et al. (US2007/0134762).
SEQ ID NO:5-linker1-SEQ ID NO:18-linker2-Cys
Sequence 27, US/10583503
Publication No. US20070161088A1
GENERAL INFORMATION
APPLICANT: Arumugham, Rasappa
APPLICANT: Prasad, A. Krishna
TITLE OF INVENTION: Methods of Producing Immunogenic A? Peptide Carrier Conjugates
FILE REFERENCE: 15270C-000110US
CURRENT APPLICATION NUMBER: US/10/583,503
CURRENT FILING DATE: 2006-06-16
PRIOR APPLICATION NUMBER: WO PCT/US2004/044093
PRIOR FILING DATE: 2004-12-17
PRIOR APPLICATION NUMBER: US 60/530,481
PRIOR FILING DATE: 2003-12-17
NUMBER OF SEQ ID NOS: 54
SEQ ID NO 27
LENGTH: 34
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
NAME/KEY: misc_feature
LOCATION: (24)..(24)
OTHER INFORMATION: Xaa can be any naturally occurring amino acid
Query Match 61.3%; Score 68; Length 34;
Best Local Similarity 80.0%;
Matches 12; Conservative 1; Mismatches 2; Indels 0; Gaps 0;
Qy 1 DAEFRHDRREFRHDS 15
||||||| |||||:
Db 8 DAEFRHDDAEFRHDA 22
Claim Rejections - 35 USC § 103
12. 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 of this title, 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 set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of 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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 71-73 are rejected under 35 U.S.C. 103 as being unpatentable over Arumugham et al. (US2007/0134762) or Imbimbo et al. (US20100028353) in view of Tiollier (US2007/0218086, published Sep 20, 2007, priority Apr 26, 2004).
Arumugham or Imbimbo is set forth above but fails to teach an immunization kit comprising the immunotherapy composition in a first container and further comprising an adjuvant in a second container as in claims 71-73.
Tiollier (US2007/0218086) teaches an immunization kit or vaccine kit comprising a suitable container containing a vaccine composition (i.e. the immunotherapy composition in a first container) and further comprising an adjuvant composition comprising gdT cell activator of formula I, II or III in a second container to enhance and increase immunogenicity as in claims 71-73 (see para. [0016]-[0020]).
A person of ordinary skill in the art would have recognized that selecting and applying the known immunization kit comprising the immunotherapy composition in a first container and further comprising an adjuvant in a second container and the known technique disclosed by Tiollier to the Arumugham’s immunotherapy composition or the Imbimbo’s immunotherapy composition would have yielded the predictable result of generating an immunization kit comprising the immunotherapy composition in a first container and further comprising an adjuvant in a second container and resulted in an improved product for immunization.
Using and including the known immunization kit comprising the immunotherapy composition in a first container and further comprising an adjuvant in a second container in the Arumugham’s immunotherapy composition or the Imbimbo’s immunotherapy composition would provide a better and convenient immunization kit for immunization and treatment of AD, and expand application of the Arumugham’s immunotherapy composition or the Imbimbo’s immunotherapy composition, and would increase patient’s satisfaction with treatment regimens of AD using the Arumugham’s immunotherapy composition or the Imbimbo’s immunotherapy composition because an immunization/vaccine kit comprising the immunotherapy composition in a first container and further comprising an adjuvant in a second container is well-known in the art and a routine practice in the field.
Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to select and apply the known the known immunization kit comprising the immunotherapy composition in a first container and further comprising an adjuvant in a second container and the known technique disclosed by Tiollier to the Arumugham’s immunotherapy composition or the Imbimbo’s immunotherapy composition, and yield the predictable result of an immunization kit comprising the immunotherapy composition in a first container and further comprising an adjuvant in a second container for better and convenient immunization and treatment of AD.
Conclusion
13. NO CLAIM IS ALLOWED.
Sequence Alignment
SEQ ID NO:1(Abeta 1-42) 1 DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA 42
Aa 1-10 of SEQ ID NO:1(Abeta 1-10) 1 DAEFRHDSGY-------------------------------- 10
Aa 12-25 of SEQ ID NO:1(Abeta 12-25) 1 -----------VHHQKLVFFAEDVG----------------- 14
SEQ ID NO:2(Abeta 1-10) 1 DAEFRHDSGY-------------------------------- 10
SEQ ID NO:5(Abeta 1-7) 1 DAEFRHD----------------------------------- 7
SEQ ID NO:12(Abeta 2-8) 1 -AEFRHDS---------------------------------- 7
SEQ ID NO:18(Abeta 3-9) 1 –-EFRHDSG--------------------------------- 7
SEQ ID NO:38(Abeta 2-9+C) 1 -AEFRHDSGC-------------------------------- 9
SEQ ID NO:39(Abeta 1-7+C) 1 DAEFRHDC---------------------------------- 8
SEQ ID NO:40(Abeta 15-22+C) 1 --------------QKLVFFAEC------------------- 9
14. The prior art made of record and not relied upon is considered pertinent to applicant's disclosure.
US6750324 teaches a human beta-amyloid fusion peptide comprising SEQ ID NO:68, which has the sequence-DAEFRHD-DAEFRHD-, and meets the peptide recited in instant claim 18 because “each of linker 1, linker 2 and [Cys] are optional” and the linker is not limited to a specific sequence (see the sequence alignment below).
SEQ ID NO:5-linker1-SEQ ID NO:18-linker2-Cys
AEJ59485
ID AEJ59485 standard; protein; 57 AA.
XX
AC AEJ59485;
XX
DT 05-OCT-2006 (first entry)
XX
DE Human Beta-amyloid fusion peptide SEQ ID No 68.
XX
KW beta-amyloid; A-beta; therapeutic; diagnosis; Alzheimers disease;
KW neuroprotective; nootropic.
XX
OS Homo sapiens.
OS Synthetic.
XX
CC PN US6750324-B1.
XX
CC PD 15-JUN-2004.
XX
CC PF 28-NOV-2000; 2000US-00724552.
XX
PR 02-DEC-1997; 97US-0067740P.
PR 07-APR-1998; 98US-0080970P.
PR 30-NOV-1998; 98US-00201430.
PR 28-MAY-1999; 99US-00322289.
PR 26-MAY-2000; 2000US-00580018.
XX
CC PA (NEUR-) NEURALAB LTD.
XX
CC PI Schenk DB, Bard F, Yednock T;
XX
DR WPI; 1999-385320/32.
XX
CC PT New composition for treating Alzheimer's disease.
XX
CC PS Disclosure; SEQ ID NO 68; 69pp; English.
XX
CC The present invention relates to a therapeutical composition comprising
CC an agent capable of inducing an immunogenic response against beta-amyloid
CC (A-beta) in a patient, and an adjuvant is new. The patentees also claim:
CC a method for preventing or treating a disease characterized by amyloid
CC deposit in a patient, comprising administering an agent to induce an
CC immune response against a peptide component of an amyloid deposit in the
CC patient; a method of preventing or treating Alzheimer's disease
CC comprising administering a dose of A-beta peptide to a patient; the use
CC of an A-beta peptide, or an antibody A-beta, to produce a therapeutic for
CC prevention or treatment of Alzheimer's disease; a composition comprising
CC A-beta or a fragment linked to a conjugate molecule that promotes
CC delivery of A-beta to the bloodstream of a patient and/or promotes an
CC immune response against A-beta; a composition comprising an agent capable
CC of inducing an immunogenic response against A-beta in a patient with the
CC proviso that the composition is free of Complete Freund's adjuvant; a
CC composition comprising a viral vector encoding A-beta or its fragment
CC effective to induce an immune response against A-beta; methods for
CC assessing efficacy of an Alzheimer's treatment; methods for monitoring
CC Alzheimer's disease or susceptibility to it; the use of A-beta peptide in
CC monitoring treatment of Alzheimer's disease in a patient; and a
CC diagnostic kit for monitoring treatment of Alzheimer's disease,
CC comprising an agent that binds to antibodies specific for A-beta peptide.
CC The composition is used to treat a human with Alzheimer's disease,
CC especially where the patient is asymptomatic, under 50, and has inherited
CC risk factors indicating susceptibility to Alzheimer's disease or has no
CC known risk factors for Alzheimer's disease. The present sequence is one
CC of a series of peptide agents of the invention (AEJ59468 to AEJ59488 nad
CC AEJ59494) which are capable of inducing an immunogenic response against
CC beta-amyloid (A-beta)
XX
SQ Sequence 57 AA;
Query Match 60.4%; Score 67; Length 57;
Best Local Similarity 85.7%;
Matches 12; Conservative 0; Mismatches 2; Indels 0; Gaps 0;
Qy 1 DAEFRHDRREFRHD 14
||||||| |||||
Db 1 DAEFRHDDAEFRHD 14
WO2006121656 teaches an Amyloid beta multivalent antigen #7 comprising the sequence-DAEFRHD-DAEFRHD-, which meets the peptide recited in instant claim 18 because “each of linker 1, linker 2 and [Cys] are optional” and the linker is not limited to a specific sequence (see the sequence alignment below).
SEQ ID NO:5-linker1-SEQ ID NO:18-linker2-Cys
AEM46682
ID AEM46682 standard; protein; 32 AA.
XX
AC AEM46682;
XX
DT 22-FEB-2007 (first entry)
XX
DE Amyloid beta multivalent antigen #7.
XX
KW nootropic; neuroprotective; vaccine; pharmaceutical; immune stimulation;
KW amyloid; antiaggregant; Alzheimers disease; Down syndrome;
KW senile dementia; cognitive disorder; amyloid beta; antigen.
XX
OS Synthetic.
XX
FH Key Location/Qualifiers
FT Modified-site 1
FT /label= OTHER
FT /note= "OTHER= Bromoacetylation-
FT NHCH2CH2O(CH2CH2O)6CH2CH2NHCOCH2OCH2CO- (PEG) and 6-
FT aminohexanoic acid (Aha) linkers"
FT Modified-site 8..9
FT /label= OTHER
FT /note= "OTHER= NHCH2CH2O(CH2CH2O)6CH2CH2NHCOCH2OCH2CO-
FT (PEG) linker"
FT Modified-site 16..17
FT /label= OTHER
FT /note= "OTHER= NHCH2CH2O(CH2CH2O)6CH2CH2NHCOCH2OCH2CO-
FT (PEG) linker"
FT Modified-site 24..25
FT /label= OTHER
FT /note= "OTHER= NHCH2CH2O(CH2CH2O)6CH2CH2NHCOCH2OCH2CO-
FT (PEG) linker"
FT Modified-site 32
FT /label= OTHER
FT /note= "OTHER= C-terminal amide"
XX
CC PN WO2006121656-A2.
XX
CC PD 16-NOV-2006.
XX
CC PF 01-MAY-2006; 2006WO-US016481.
XX
PR 05-MAY-2005; 2005US-0677886P.
XX
CC PA (MERI ) MERCK & CO INC.
XX
CC PI Garsky VM, Joyce JG, Keller PM, Kinney G, Liang X, Shiver JW;
XX
DR WPI; 2007-123100/12.
XX
CC PT Pharmaceutical composition for treating disease associated with amyloid
CC PT deposits in the brain (e.g. Alzheimer's disease), comprises an
CC PT immunogenic fragment of Abeta lacking a T-cell epitope, and capable of
CC PT inducing an antibody response.
XX
CC PS Example 1; Fig 5; 55pp; English.
XX
CC The invention describes a pharmaceutical composition comprising an
CC immunogenic fragment of amyloid (A) beta, lacking a T-cell epitope,
CC capable of inducing an immune response in the form of antibodies to the A
CC beta fragment. Also described is a method for preventing or treating a
CC disease associated with amyloid deposits of A beta in the brain of a
CC patient, which comprises administering a dose of an immunogenic fragment
CC of A beta, lacking a T-cell epitope, capable of inducing an immune
CC response in the form of antibodies to the A beta fragment. The
CC composition and method are useful for preventing or treating a disease
CC associated with amyloid deposits of Aβ in the brain, e.g.
CC Alzheimer's disease, Down's syndrome, cognitive impairment, or other
CC forms of senile dementia. This is the amino acid sequence of a
CC multivalent amyloid beta immunogenic peptide
XX
SQ Sequence 32 AA;
Query Match 64.0%; Score 71; Length 32;
Best Local Similarity 86.7%;
Matches 13; Conservative 0; Mismatches 2; Indels 0; Gaps 0;
Qy 2 AEFRHDRREFRHDSG 16
|||||| |||||||
Db 9 AEFRHDSGEFRHDSG 23
US20070161088 teaches a human beta-amyloid fusion peptide carrier conjugate comprising SEQ ID NO:27, which has the sequence-DAEFRHD-DAEFRHD-, and meets the peptide recited in instant claim 18 because “each of linker 1, linker 2 and [Cys] are optional” and the linker is not limited to a specific sequence (see the sequence alignment below)..
SEQ ID NO:5-linker1-SEQ ID NO:18-linker2-Cys
Sequence 27, US/10583503
Publication No. US20070161088A1
GENERAL INFORMATION
APPLICANT: Arumugham, Rasappa
APPLICANT: Prasad, A. Krishna
TITLE OF INVENTION: Methods of Producing Immunogenic A? Peptide Carrier Conjugates
FILE REFERENCE: 15270C-000110US
CURRENT APPLICATION NUMBER: US/10/583,503
CURRENT FILING DATE: 2006-06-16
PRIOR APPLICATION NUMBER: WO PCT/US2004/044093
PRIOR FILING DATE: 2004-12-17
PRIOR APPLICATION NUMBER: US 60/530,481
PRIOR FILING DATE: 2003-12-17
NUMBER OF SEQ ID NOS: 54
SEQ ID NO 27
LENGTH: 34
TYPE: PRT
ORGANISM: Homo sapiens
FEATURE:
NAME/KEY: misc_feature
LOCATION: (24)..(24)
OTHER INFORMATION: Xaa can be any naturally occurring amino acid
Query Match 61.3%; Score 68; Length 34;
Best Local Similarity 80.0%;
Matches 12; Conservative 1; Mismatches 2; Indels 0; Gaps 0;
Qy 1 DAEFRHDRREFRHDS 15
||||||| |||||:
Db 8 DAEFRHDDAEFRHDA 22
US7919088 teaches a Human amyloid beta 42-hemagglutinin epitope fusion peptide comprising SEQ ID NO:48, which has the sequence-DAEFRHD-DAEFRHD-, and meets the peptide recited in instant claim 18 because “each of linker 1, linker 2 and [Cys] are optional” and the linker is not limited to a specific sequence (see the sequence alignment below).
SEQ ID NO:5-linker1:RR-SEQ ID NO:18-linker2:GG-Cys
ID AZH06762 standard; peptide; 27 AA.
XX
AC AZH06762;
XX
DT 26-MAY-2011 (first entry)
XX
DE Human amyloid beta 42-hemagglutinin epitope fusion peptide, SEQ ID 48.
XX
KW A4 protein 42; APP protein; Beta amyloid 42; HA protein; Hemagglutinin;
KW alzheimers disease; antibody therapy; antigen;
KW autonomic nervous system disease; dysphagia; epitope; fusion protein;
KW immune stimulation; lewy body dementia; multiple system atrophy;
KW neurodegenerative disease; neuroprotective; olivopontocerebellar atrophy;
KW parkinsons disease; prophylactic to disease; shy drager syndrome;
KW therapeutic.
XX
OS Homo sapiens.
OS unidentified influenza virus.
OS Synthetic.
XX
FH Key Location/Qualifiers
FT Region 1..7
FT /note= "Amyloid beta 42-1"
FT Region 8..14
FT /note= "Amyloid beta 42-2"
FT Region 15..27
FT /note= "Hemagglutinin epitope region"
XX
CC PN US7919088-B2.
XX
CC PD 05-APR-2011.
XX
CC PF 20-AUG-2007; 2007US-00842054.
XX
PR 23-FEB-2007; 2007US-00710248.
PR 06-APR-2007; 2007US-00697646.
XX
CC PA (ELAN ) ELAN PHARM INC.
CC PA (REGC ) UNIV CALIFORNIA.
XX
CC PI Schenk DB, Games KD, Buttini MJ, Chilcote TJ, Rockenstein E;
CC PI Masliah E;
XX
DR WPI; 2011-D55310/26.
XX
CC PT Treating a disease characterized by Lewy bodies or alpha-synuclein
CC PT aggregation in the brain comprises administering an antibody comprising
CC PT complementarity determining regions of monoclonal antibody 8A5 to a
CC PT patient.
XX
CC PS Disclosure; SEQ ID NO 48; 74pp; English.
XX
CC The present invention relates to a method for reducing the risk of,
CC lessening the severity of, delaying the outset of or treating
CC synucleinopathic and amyloidogenic disease characterized by Lewy bodies
CC or alpha-synuclein aggregation in the brain. The method comprises,
CC administering an effective regime of an antibody that comprises
CC complementarity determining regions (CDRs) of monoclonal antibody 8A5
CC deposited at ATCC PTA-6909 to a patient having or at risk of the disease,
CC where the antibody specifically binds to intact human alpha-synuclein.
CC The method is useful for preventing and treating neurodegenarative
CC diseases such as parkinson's disease (PD), dementia with Lewy bodies
CC (DLB), diffuse Lewy body disease (DLBD), Lewy body variant of Alzheimer's
CC disease (LBVAD), multiple systems atrophy (MSA) (e.g.,
CC olivopontocerebellar atrophy, striatonigral degeneration and Shy-Drager
CC syndrome), neurodegeneration with brain iron accumulation type-1 (NBIA-
CC 1), pure autonomic failure, Lewy body dysphagia, incidental LBD,
CC inherited LBD (e.g., mutations of the alpha-SN gene, PARK3 and PARK4).
CC The present sequence is a fusion peptide formed by linking an immunogenic
CC peptide with a carrier peptide, where the fusion peptide is an agent that
CC induces an immune response, is used in treating amyloidogenic disease in
CC the invention.
XX
SQ Sequence 27 AA;
Query Match 60.4%; Score 67; Length 27;
Best Local Similarity 85.7%;
Matches 12; Conservative 0; Mismatches 2; Indels 0; Gaps 0;
Qy 1 DAEFRHDRREFRHD 14
||||||| |||||
Db 1 DAEFRHDDAEFRHD 14
US2008014194 teaches an Influenza virus hemagglutinin-beta amyloid 42 fusion peptide comprising SEQ ID NO:48, which has the sequence-DAEFRHD-DAEFRHD-, and meets the peptide recited in instant claim 18 because “each of linker 1, linker 2 and [Cys] are optional” and the linker is not limited to a specific sequence (see the sequence alignment below).
SEQ ID NO:5-linker1-SEQ ID NO:18-linker2-Cys
ID AOG39535 standard; peptide; 27 AA.
XX
AC AOG39535;
XX
DT 20-MAR-2008 (first entry)
XX
DE Influenza virus hemagglutinin-beta amyloid 42 fusion peptide, SEQ ID: 48.
XX
KW Prophylactic to disease; therapeutic; antibody therapy;
KW immune stimulation; drug screening; lewy bodies; Parkinsons disease;
KW Antiparkinsonian; Neurodegenerative disease; Neuroprotective; Dementia;
KW Nootropic; Alzheimers disease; Multiple system atrophy;
KW cerebroprotective; Degeneration; Beta amyloid 42; Abeta42; hemagglutinin;
KW fusion protein.
XX
OS Orthomyxoviridae.
OS Homo sapiens.
OS Chimeric.
XX
FH Key Location/Qualifiers
FT Peptide 1..14
FT /note= "Human beta-amyloid 42 (Abeta42) peptide fragment"
FT Peptide 15..27
FT /note= "Influenza virus hemagglutinin peptide fragment"
XX
CC PN US2008014194-A1.
XX
CC PD 17-JAN-2008.
XX
CC PF 06-APR-2007; 2007US-00697646.
XX
PR 31-OCT-2003; 2003US-00699517.
PR 09-AUG-2004; 2004US-00915214.
PR 19-JUL-2005; 2005US-00185907.
PR 09-AUG-2005; 2005WO-US028166.
PR 08-FEB-2007; 2007US-00660015.
PR 23-FEB-2007; 2007US-00710248.
XX
CC PA (ELAN-) ELAN PHARM INC.
CC PA (REGC ) UNIV CALIFORNIA.
XX
CC PI Schenk DB, Games KD, Buttini MJ, Chilcote TJ, Rockenstein E;
CC PI Masliah E;
XX
DR WPI; 2008-B38585/09.
XX
CC PT Preventing or treating Lewy body or alpha-synuclein aggregation in the
CC PT brain by administering to a patient having or at risk of the disease an
CC PT antibody that specifically binds to an epitope of human alpha-synuclein.
XX
CC PS Disclosure; SEQ ID NO 48; 74pp; English.
XX
CC The present invention relates to a novel method of preventing or treating
CC a synucleinopathic and amyloidogenic diseases (including Lewy body or
CC alpha-synuclein aggregation) in the brain of a patient. The method of the
CC invention comprises administering an antibody that specifically binds to
CC an epitope of human alpha-synuclein to a patient having or at risk of the
CC disease. The method is useful for preventing or treating a disease
CC characterized by Lewy bodies or alpha-synuclein aggregation in the brain,
CC several neurodegenerative diseases such as Parkinson's disease, dementia
CC with Lewy bodies, Lewy body variant of Alzheimer's disease, multiple
CC systems atrophy and neurodegeneration with brain iron accumulation type-
CC 1. The antibody of the invention is also useful for inducing an
CC immunogenic response against a component of a Lewy body in a patient. The
CC present sequence represents a fusion protein in a linear configuration
CC comprising two human beta-amyloid 42 (Abeta42) peptide fragments
CC (residues 1-7) and an Influenza virus hemagglutinin peptide fragment
CC (residues 307-319).
XX
SQ Sequence 27 AA;
Query Match 60.4%; Score 67; Length 27;
Best Local Similarity 85.7%;
Matches 12; Conservative 0; Mismatches 2; Indels 0; Gaps 0;
Qy 1 DAEFRHDRREFRHD 14
||||||| |||||
Db 1 DAEFRHDDAEFRHD 14
US2009208487 teaches a human beta-amyloid fusion peptide comprising SEQ ID NO:48, which has the sequence-DAEFRHD-DAEFRHD-, and meets the peptide recited in instant claim 18 because “each of linker 1, linker 2 and [Cys] are optional” and the linker is not limited to a specific sequence (see the sequence alignment below).
SEQ ID NO:5-linker1-SEQ ID NO:18-linker2-Cys
ID AXQ21187 standard; peptide; 27 AA.
XX
AC AXQ21187;
XX
DT 15-OCT-2009 (first entry)
XX
DE Human Beta-amyloid fusion protein amino acid SEQ ID NO:48.
XX
KW APP; Beta amyloid; antibody therapy; antiparkinsonian; fusion protein;
KW lewy body dementia; nootropic; parkinsons disease;
KW prophylactic to disease; protein therapy; therapeutic.
XX
OS Homo sapiens.
OS Chimeric.
OS Synthetic.
OS Unidentified.
XX
FH Key Location/Qualifiers
FT Region 1..7
FT /note= "Human beta-amyloid protein fragment"
FT Region 8..14
FT /note= "Human beta-amyloid protein fragment"
XX
CC PN US2009208487-A1.
XX
CC PD 20-AUG-2009.
XX
CC PF 23-FEB-2007; 2007US-00710248.
XX
PR 31-OCT-2003; 2003US-00699517.
PR 09-AUG-2004; 2004US-00915214.
PR 19-JUL-2005; 2005US-00185907.
PR 09-AUG-2005; 2005WO-US028166.
PR 08-FEB-2007; 2007US-00660015.
XX
CC PA (ELAN-) ELAN PHARM INC.
XX
CC PI Buttini MJ, Chilcote TJ, Games KD, Masliah E, Rockenstein E;
CC PI Schenk DB;
XX
DR WPI; 2009-M83585/57.
XX
CC PT Effecting prophylaxis or treating disease characterized by Lewy bodies or
CC PT alpha-synuclein aggregation in the brain comprises administering regime
CC PT of antibody that binds to epitope of human alpha-synuclein.
XX
CC PS Disclosure; SEQ ID NO 48; 70pp; English.
XX
CC The present invention relates to a method of effecting prophylaxis or
CC treating a disease characterized by Lewy bodies or alpha-synuclein
CC aggregation in the brain. The method comprises administering to a patient
CC having or at risk of the disease an effective regime of an antibody that
CC specifically binds to an epitope within residues 70-140 of human alpha-
CC synuclein, residues comprising fully defined 140 amino acids (SEQ ID NO:1
CC AXQ21140) given in the specification. The method is useful for effecting
CC prophylaxis or treating a disease characterized by Lewy bodies or alpha-
CC synuclein aggregation in the brain, where the disease is Parkinson's
CC disease. The present sequence represents a human Beta-amyloid fusion
CC protein amino acid sequence used to induce immunogenic response for the
CC therapeutic purpose of the invention.
XX
SQ Sequence 27 AA;
Query Match 60.4%; Score 67; Length 27;
Best Local Similarity 85.7%;
Matches 12; Conservative 0; Mismatches 2; Indels 0; Gaps 0;
Qy 1 DAEFRHDRREFRHD 14
||||||| |||||
Db 1 DAEFRHDDAEFRHD 14
WO200072880 teaches a Tetanus toxoid epitope AN90543 comprising the sequence-DAEFRHD-DAEFRHD-, and meets the peptide recited in instant claim 18 because “each of linker 1, linker 2 and [Cys] are optional” and the linker is not limited to a specific sequence (see the sequence alignment below).
SEQ ID NO:5-linker1-SEQ ID NO:18-linker2-Cys
AAB46180
(NOTE: this sequence has 15 duplicates in the database searched)
ID AAB46180 standard; peptide; 34 AA.
XX
AC AAB46180;
XX
DT 04-APR-2001 (first entry)
XX
DE Tetanus toxoid epitope AN90543.
XX
KW Amyloid deposit; APP; Abeta; brain; human; clearing response; nootropic;
KW Fc receptor mediated phagocytosis; immunogenic response; neuroprotective;
KW amyloid precursor protein; Alzheimer's disease.
XX
OS Clostridium tetani.
XX
CC PN WO200072880-A2.
XX
CC PD 07-DEC-2000.
XX
CC PF 26-MAY-2000; 2000WO-US014810.
XX
PR 28-MAY-1999; 99US-00322289.
XX
CC PA (NEUR-) NEURALAB LTD.
XX
CC PI Schenk DB, Bard F, Vasquez NJ, Yednock T;
XX
DR WPI; 2001-032104/04.
XX
CC PT Preventing or treating a disease associated with amyloid deposits,
CC PT especially Alzheimer's disease, comprises administering amyloid specific
CC PT antibody.
XX
CC PS Disclosure; Page 31; 143pp; English.
XX
CC This invention describes a novel method of preventing or treating a
CC disease associated with amyloid deposits of amyloid precursor protein
CC (APP) Abeta fragments in the brain of a patient, which comprises
CC administering to the patient: (a) an antibody that binds to Abeta, the
CC antibody binds to an amyloid deposit and induces a clearing response (Fc
CC receptor mediated phagocytosis) against it (b) a polypeptide containing
CC an N-terminal segment of at least residues 1-5 of Abeta; or (c) an agent
CC that induces an immunogenic response against residues 1-3 to 7-11 of
CC Abeta. The products of the invention have nootropic and neuroprotective
CC activity. The method is also useful for monitoring a course of treatment
CC being administered to a patient e.g. active and passive immunization. The
CC methods are useful for prophylactic and therapeutic treatment of
CC Alzheimer's disease
XX
SQ Sequence 34 AA;
Query Match 61.3%; Score 68; Length 34;
Best Local Similarity 80.0%;
Matches 12; Conservative 1; Mismatches 2; Indels 0; Gaps 0;
Qy 1 DAEFRHDRREFRHDS 15
||||||| |||||:
Db 8 DAEFRHDDAEFRHDA 22
JP2013112668 teaches a Glycine max A1aB1bMK1 protein comprising SEQ ID NO:17, which has the sequence-DAEFRHDSGYEVHHQKK-DAEFRHDSGYEVHHQKK-, and meets the peptide recited in instant claim 18 because “each of linker 1, linker 2 and [Cys] are optional” and the linker is not limited to a specific sequence (see the sequence alignment below).
SEQ ID NO:5-linker1-SEQ ID NO:18-linker2-Cys
BAP11285
ID BAP11285 standard; protein; 528 AA.
XX
AC BAP11285;
XX
DT 18-JUL-2013 (first entry)
XX
DE Glycine max A1aB1bMK1 protein, SEQ ID 17.
XX
KW A1aB1bMK1 protein; alzheimers disease; amnesia; antibody production;
KW genetically engineered; neuroprotective; nootropic;
KW prophylactic to disease; therapeutic; vaccine, synthetic.
XX
OS Glycine max.
OS Synthetic.
XX
CC PN JP2013112668-A.
XX
CC PD 10-JUN-2013.
XX
CC PF 30-NOV-2011; 2011JP-00262159.
XX
PR 30-NOV-2011; 2011JP-00262159.
XX
CC PA (HOKK ) HOKKO CHEM IND CO LTD.
CC PA (UYHI-) UNIV HIROSHIMA.
XX
CC PI Terakawa T, Hasegawa H, Shimada Y, Kawarabayashi T, Shoji M;
CC PI Takahashi A;
XX
DR WPI; 2013-K26569/39.
DR N-PSDB; BAP11284.
XX
CC PT Vaccine composition useful for preventing and/or treating Alzheimer's
CC PT disease, comprises fusion protein comprising specific amino acid
CC PT sequences of amyloid beta peptide and amino acid sequence of seed storage
CC PT protein.
XX
CC PS Example 4; SEQ ID NO 17; 62pp; Japanese.
XX
CC The present invention relates to a vaccine composition comprising a
CC fusion protein. The fusion protein is derived from the (N)-terminal
CC portion of an amyloid (beta) peptide having single or multiple repeats,
CC which are inserted into an amino acid sequence of a seed storage protein.
CC The seed deposit protein is an A1aB1b subunit of an 11S globulin of
CC soybean, a seed protein of a kidney bean, or a prolamin of Oryza sativa.
CC The composition produces amyloid specific antibody and reduces amyloid
CC plaque associated with soluble and insoluble amyloid (beta) 1-42 when
CC administered to an animal. The composition is useful for preventing and
CC treating Alzheimer's disease and recovering cognitive memory loss without
CC side effects. The present sequence refers to a a Glycine max A1aB1bMK1
CC protein, which is used for preparing the vaccine composition comprising
CC the fusion protein of the invention.
XX
SQ Sequence 528 AA;
Query Match 60.5%; Score 67.1; Length 528;
Best Local Similarity 34.0%;
Matches 16; Conservative 0; Mismatches 2; Indels 29; Gaps 2;
Qy 1 DAEFRHDR----------REFRHDSG-------------------GG 18
||||||| ||||||| ||
Db 205 DAEFRHDSGYEVHHQKKDAEFRHDSGYEVHHQAQKGKHQQEEENEGG 251
WO2006121656 teaches a beta-amyloid multivalent antigen#7 comprising the sequence -AEFRHDSG-EFRHDSG-, which meets the peptide recited in instant claim 18 because “each of linker 1, linker 2 and [Cys] are optional” and the linker is not limited to a specific sequence (see the sequence alignment below).
SEQ ID NO:5-linker1-SEQ ID NO:18-linker2-Cys
AEM46682
ID AEM46682 standard; protein; 32 AA.
XX
AC AEM46682;
XX
DT 22-FEB-2007 (first entry)
XX
DE Amyloid beta multivalent antigen #7.
XX
KW nootropic; neuroprotective; vaccine; pharmaceutical; immune stimulation;
KW amyloid; antiaggregant; Alzheimers disease; Down syndrome;
KW senile dementia; cognitive disorder; amyloid beta; antigen.
XX
OS Synthetic.
XX
FH Key Location/Qualifiers
FT Modified-site 1
FT /label= OTHER
FT /note= "OTHER= Bromoacetylation-
FT NHCH2CH2O(CH2CH2O)6CH2CH2NHCOCH2OCH2CO- (PEG) and 6-
FT aminohexanoic acid (Aha) linkers"
FT Modified-site 8..9
FT /label= OTHER
FT /note= "OTHER= NHCH2CH2O(CH2CH2O)6CH2CH2NHCOCH2OCH2CO-
FT (PEG) linker"
FT Modified-site 16..17
FT /label= OTHER
FT /note= "OTHER= NHCH2CH2O(CH2CH2O)6CH2CH2NHCOCH2OCH2CO-
FT (PEG) linker"
FT Modified-site 24..25
FT /label= OTHER
FT /note= "OTHER= NHCH2CH2O(CH2CH2O)6CH2CH2NHCOCH2OCH2CO-
FT (PEG) linker"
FT Modified-site 32
FT /label= OTHER
FT /note= "OTHER= C-terminal amide"
XX
CC PN WO2006121656-A2.
XX
CC PD 16-NOV-2006.
XX
CC PF 01-MAY-2006; 2006WO-US016481.
XX
PR 05-MAY-2005; 2005US-0677886P.
XX
CC PA (MERI ) MERCK & CO INC.
XX
CC PI Garsky VM, Joyce JG, Keller PM, Kinney G, Liang X, Shiver JW;
XX
DR WPI; 2007-123100/12.
XX
CC PT Pharmaceutical composition for treating disease associated with amyloid
CC PT deposits in the brain (e.g. Alzheimer's disease), comprises an
CC PT immunogenic fragment of Abeta lacking a T-cell epitope, and capable of
CC PT inducing an antibody response.
XX
CC PS Example 1; Fig 5; 55pp; English.
XX
CC The invention describes a pharmaceutical composition comprising an
CC immunogenic fragment of amyloid (A) beta, lacking a T-cell epitope,
CC capable of inducing an immune response in the form of antibodies to the A
CC beta fragment. Also described is a method for preventing or treating a
CC disease associated with amyloid deposits of A beta in the brain of a
CC patient, which comprises administering a dose of an immunogenic fragment
CC of A beta, lacking a T-cell epitope, capable of inducing an immune
CC response in the form of antibodies to the A beta fragment. The
CC composition and method are useful for preventing or treating a disease
CC associated with amyloid deposits of Aβ in the brain, e.g.
CC Alzheimer's disease, Down's syndrome, cognitive impairment, or other
CC forms of senile dementia. This is the amino acid sequence of a
CC multivalent amyloid beta immunogenic peptide
XX
SQ Sequence 32 AA;
Query Match 64.0%; Score 71; Length 32;
Best Local Similarity 86.7%;
Matches 13; Conservative 0; Mismatches 2; Indels 0; Gaps 0;
Qy 2 AEFRHDRREFRHDSG 16
|||||| |||||||
Db 9 AEFRHDSGEFRHDSG 23
WO2017008638 teaches a Abeta 1-15-loop1G72 fusion peptide comprising SEQ ID NO:68, which has the sequence-DAEFRHDSGYEVHHQ-GGG-DAEFRHDSGYEVHHQ-GGG-, and meets the peptide recited in instant claim 18 because “each of linker 1, linker 2 and [Cys] are optional” and the linker is not limited to a specific sequence (see the sequence alignment below).
SEQ ID NO:5-linker1-SEQ ID NO:18-linker2-Cys
BDN10587
ID BDN10587 standard; protein; 183 AA.
XX
AC BDN10587;
XX
DT 09-MAR-2017 (first entry)
XX
DE Abeta1-15-loop1G72 construct protein.
XX
KW A beta 1; Beta amyloid; alzheimers disease; amyloid-beta;
KW neuroprotective; nootropic; prophylactic to disease; protein production;
KW protein therapy; recombinant protein; therapeutic; vaccine, general.
XX
OS Homo sapiens.
OS Synthetic.
XX
FH Key Location/Qualifiers
FT Region 4..18
FT /note= "This region is repeated 10 times"
XX
CC PN WO2017008638-A1.
XX
CC PD 19-JAN-2017.
XX
CC PF 29-JUN-2016; 2016WO-CN087643.
XX
PR 15-JUL-2015; 2015CN-10415556.
XX
CC PA (CHAN-) CHANGCHUN BCHT BIOTECHNOLOGY CO.
CC PA (UYJI ) UNIV JILIN.
XX
CC PI Kong W, Wu H, Jiang C, Yu X, Fu L, Li Y;
XX
DR WPI; 2017-060928/14.
XX
CC PT New recombinant P particle formed from norovirus capsid P protein of
CC PT chimeric A-beta 1-m peptide used in pharmaceutical composition for
CC PT preventing or treating Alzheimer's disease in mammal, preferably human.
XX
CC PS Example 5; Fig 3E; 81pp; Chinese.
XX
CC The present invention relates to a recombinant P particle formed from a
CC norovirus capsid P protein of a chimeric amyloid-beta protein (A beta 1),
CC where the the recombinant P particles form an ordered and repetitive
CC antigen array. The invention further discloses: (1) a polynucleotide
CC encoding the recombinant P particle; (2) a pharmaceutical composition
CC comprising the recombinant P particle, where the composition is vaccine
CC comprising an adjuvant, preferably CpG adjuvant or aluminum adjuvant; and
CC (3) a method for preparing the recombinant P particle in a simple and
CC cost-effective manner. The recombinant P particle of the invention is
CC useful in pharmaceutical composition for preventing or treating
CC Alzheimer's disease in a mammal, preferably human. The present sequence
CC represents a Abeta1-15-loop1G72 construct protein which is used in
CC constructing the recombinant P particle. Note: SEQ ID NOs: 152-278 are
CC mentioned under claim 7 and example 3 but the corresponding sequences are
CC not shown in the specification.
XX
SQ Sequence 183 AA;
Query Match 61.5%; Score 68.3; Length 183;
Best Local Similarity 45.7%;
Matches 16; Conservative 0; Mismatches 2; Indels 17; Gaps 2;
Qy 1 DAEFRHDR-----------REFRHDSG------GG 18
||||||| ||||||| ||
Db 4 DAEFRHDSGYEVHHQGGGDAEFRHDSGYEVHHQGG 38
WO2009029272 teaches a beta-amyloid fusion peptide comprising SEQ ID NO:29, which has the sequence-DAEFRHDSGYEGS-DAEFRHDSGYEGS-, and meets the peptide recited in instant claim 18 because “each of linker 1, linker 2 and [Cys] are optional” and the linker is not limited to a specific sequence (see the sequence alignment below).
SEQ ID NO:5-linker1-SEQ ID NO:18-linker2-Cys
AWI77214
ID AWI77214 standard; protein; 128 AA.
XX
AC AWI77214;
XX
DT 14-MAY-2009 (first entry)
XX
DE Plasmid vaccine protein sequence SEQ:29.
XX
KW vaccine, general; immune stimulation; immunotherapy;
KW prophylactic to disease; alzheimers disease; neuroprotective; nootropic;
KW plasmid.
XX
OS Unidentified.
OS Synthetic.
XX
FH Key Location/Qualifiers
FT Region 1..68
FT /note= "Beta-DF3 region"
FT Region 69..78
FT /note= "Spacer region"
FT Region 79..89
FT /note= "Amyloid beta protein portion"
FT Region 90..91
FT /note= "Spacer region"
FT Region 92..102
FT /note= "Amyloid beta protein portion"
FT Region 103..104
FT /note= "Spacer region"
FT Region 105..115
FT /note= "Amyloid beta protein portion"
FT Region 116..128
FT /note= "PADRE region"
XX
CC PN WO2009029272-A2.
XX
CC PD 05-MAR-2009.
XX
CC PF 27-AUG-2008; 2008WO-US010186.
XX
PR 27-AUG-2007; 2007US-0966218P.
PR 16-APR-2008; 2008US-0124274P.
XX
CC PA (AGAD/) AGADJANYAN M G.
XX
CC PI Agadjanyan MG, Ghochikyan A;
XX
DR WPI; 2009-F47458/20.
DR N-PSDB; AWI77199.
XX
CC PT New composition comprises a nucleic acid sequence comprising a B cell
CC PT epitope, a non-self T cell epitope and with a molecular adjuvant or
CC PT without molecular adjuvant, useful for treating Alzheimer's disease.
XX
CC PS Example 6; SEQ ID NO 29; 56pp; English.
XX
CC The present invention relates to a novel method for (Alzheimer's disease)
CC AD prevention and treatment via Abeta-specific antibodies. The invention
CC also includes epitope vaccines composed of several copies of self B cell
CC epitope of amyloid peptide, foreign T cell epitope derived from the
CC conventional vaccines or pathogens to which the human population is
CC frequently exposed and molecular adjuvant. The rationale to use N>1
CC copies of B cell epitope in vaccine composition is to significantly
CC enhance the anti-Ass humoral immune response and the avidity of Ass
CC specific antibodies. The rationale to use foreign T cell epitope is to
CC avoid the generation of autoreactive T cells and to overcome tolerance to
CC self-epitope. More importantly, inclusion of various Th epitopes in the
CC composition of the epitope vaccine will allow to induce quick and potent
CC ant-Ass antibody responses using pre-existing memory CD4+Th cells induced
CC in general population by previous infections and/or immunizations with
CC conventional vaccines, for example Tetanus, Diphtheria, Pertussis,
CC Influenza, HBV. The present sequence represents a plasmid vaccine protein
CC sequence used in the method of the invention.
XX
SQ Sequence 128 AA;
Query Match 60.7%; Score 67.4; Length 128;
Best Local Similarity 63.6%;
Matches 14; Conservative 0; Mismatches 2; Indels 6; Gaps 1;
Qy 1 DAEFRHDR------REFRHDSG 16
||||||| |||||||
Db 79 DAEFRHDSGYEGSDAEFRHDSG 100
CN101486768 teaches a GST-human beta-amyloid Abeta9-immunoenhancing K6 fusion peptide comprising SEQ ID NO:10, which has the sequence-DAEFRHD-SG-DAEFRHD-SG, and meets the peptide recited in instant claim 18 because of the limitation “each of linker 1, linker 2 and [Cys] are optional” and the linker is not limited to a specific sequence (see the sequence alignment below).
SEQ ID NO:5-linker1-SEQ ID NO:18-linker2-Cys
AXQ00510
ID AXQ00510 standard; protein; 376 AA.
XX
AC AXQ00510;
XX
DT 01-OCT-2009 (first entry)
XX
DE GST-human beta-amyloid Abeta9-immunoenhancing K6 fusion protein, SEQ 10.
XX
KW APP gene; Abeta9; Beta amyloid; GST; Glutathione S-transferase; K6;
KW alzheimers disease; fusion protein; immune stimulation; neuroprotective;
KW nootropic; prophylactic to disease; recombinant protein; therapeutic.
XX
OS Homo sapiens.
OS Synthetic.
OS Unidentified.
XX
FH Key Location/Qualifiers
FT Protein 1..226
FT /note= "Glutathione S-transferase (GST) protein"
FT Peptide 362..367
FT /note= "Immunoenhancing peptide K6"
XX
CC PN CN101486768-A.
XX
CC PD 22-JUL-2009.
XX
CC PF 25-FEB-2009; 2009CN-10066564.
XX
PR 25-FEB-2009; 2009CN-10066564.
XX
CC PA (UYJI-) UNIV JILIN.
XX
CC PI Cui L, Huang X, Zhang Y;
XX
DR WPI; 2009-M18073/55.
DR N-PSDB; AXQ00514.
XX
CC PT New recombinant antigenic protein comprising immune enhanced sequences
CC PT and human beta-amyloid peptide sequences, for treating and preventing
CC PT Alzheimer disease.
XX
CC PS Claim 6; SEQ ID NO 10; 32pp; Chinese.
XX
CC The present invention relates to a novel recombinant antigenic protein
CC comprising immune enhanced sequences and human beta-amyloid peptide
CC sequences, for treating and preventing Alzheimers disease. The invention
CC further provides a fused gene for encoding recombinant antigenic protein
CC for treating Alzheimer disease and pGEX-4T-1, pGEX-4T-2 or pGEX-4T-3 for
CC constructing recombinant expression vector. The present sequence
CC represents an amino acid sequence of fusion protein comprising Human beta
CC -amyloid Abeta42 peptide, Glutathione S-transferase (GST) protein and an
CC immunoenhacing peptide which is encoded by a fusion gene used for
CC treating and preventing Alzheimers disease.
XX
SQ Sequence 376 AA;
Query Match 61.1%; Score 67.8; Length 376;
Best Local Similarity 77.8%;
Matches 14; Conservative 0; Mismatches 2; Indels 2; Gaps 1;
Qy 1 DAEFRHDR--REFRHDSG 16
||||||| |||||||
Db 227 DAEFRHDSGDAEFRHDSG 244
15. 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.
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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
September 17, 2026
/CHANG-YU WANG/Primary Examiner, Art Unit 1675
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