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
Applicant’s amendment filed July 9, 2026 is acknowledged. Claims 7 and 14 are cancelled. Claims 1-6, 8-13 and 15-18 are amended. Claims 19-20 are newly added. Claims 1-6, 8-13,15-18 and new claims 19-20 are pending in this Application. Claims 8-12 and 15-20 are withdrawn without traverse (filed 01/29/2026) from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected inventions, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on January 29, 2026.
Amended claim 18 and Newly submitted claims 19-20 are directed to an invention that is independent or distinct from the invention originally claimed for the following reasons: claims 18-20 are directed to a method of treatment, which is categorized in Group III and is withdrawn without traverse (filed 01/29/2026) from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected inventions, there being no allowable generic or linking claim.
Since applicant has received an action on the merits for the originally presented invention, this invention has been constructively elected by original presentation for prosecution on the merits. Accordingly, claims 18-20 are withdrawn without traverse (filed 01/29/2026) from consideration as being directed to a non-elected invention. See 37 CFR 1.142(b) and MPEP § 821.03.
To preserve a right to petition, the reply to this action must distinctly and specifically point out supposed errors in the restriction requirement. Otherwise, the election shall be treated as a final election without traverse. Traversal must be timely. Failure to timely traverse the requirement will result in the loss of right to petition under 37 CFR 1.144. If claims are subsequently added, applicant must indicate which of the subsequently added claims are readable upon the elected invention.
Should applicant traverse on the ground that the inventions are not patentably distinct, applicant should submit evidence or identify such evidence now of record showing the inventions to be obvious variants or clearly admit on the record that this is the case. In either instance, if the examiner finds one of the inventions unpatentable over the prior art, the evidence or admission may be used in a rejection under 35 U.S.C. 103 or pre-AIA 35 U.S.C. 103(a) of the other invention.
4. Claims 1-6 and 13 are under examination in this office action.
5. Applicant’s arguments filed on July 9, 2026 have been fully considered but they are not deemed to be persuasive for the reasons set forth below.
Specification
6. The objection to the specification is withdrawn in response to Applicant’s amendment to the specification.
Claim Rejections/Objections Withdrawn
7. The objection to claims 1-7 and 13-14 is withdrawn in response to Applicant’s amendment to the claims and cancelation of claims 7 and 14.
The rejection of claims 5, 7, 14 and 18 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 claims and cancelation of claims 7 and 14.
The rejection of claim 18 under 35 U.S.C. 101 because the disclosed invention is inoperative and therefore lacks utility is withdrawn in response to Applicant’s amendment to the claim.
The rejection of claims 7,14 and 18 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 withdrawn in response to Applicant’s amendment to the claims and cancelation of claims 7 and 14.
The rejection of claims 1, 4-7, 13-14 and 18 under 35 U.S.C. 102(a)(1) as being anticipated by Hu et al. (US20190309092; also published as WO2018017863) is withdrawn in response to Applicant’s amendment to the claims and cancelation of claims 7 and 14.
Claim Rejections/Objections Maintained
In view of the amendment filed on July 9, 2026, the following rejections are maintained.
Claim Objections
8. Claims 18-20 are objected to because of the following informalities: the status of claims 18-20 is incorrect because claims 18-20 are directed to a method of treatment, which is withdrawn from further consideration. Appropriate correction is required. See MPEP 714 & 37 CFR 1.121.
“In the claim listing, the status of every claim must be indicated after its claim number by using one of the following identifiers in a parenthetical expression: (Original), (Currently amended), (Canceled), (Withdrawn), (Previously presented), (New), and (Not entered).”
Claim Rejections - 35 USC § 112
9. 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 1-6 and 13 stand 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 1-6 and 13 as amended are drawn to a ScFv type protein comprising a structure of VH domain-peptide ligand-VL domain, wherein the VH comprises at least amino acids N173, Y176, K181, Y217, Y222 from SEQ ID NO:3 and the VL comprises at least amino acids K31, Y33, N35 from SEQ ID NO:3. Claims 2 and 3 encompass a genus of SCFv type protein comprising a structure of VH domain-peptide ligand-VL domain, wherein the VH comprises SEQ ID NOs:10-12 for HCDRs1-3 respectively and VL comprises SEQ ID NOs:7-9 for LCDRs1-3 or wherein the VH comprises aa Q117-S237 of SEQ ID NO:3 and the VL comprises aa D1-I111 of SEQ ID NO:3.
Briefly, the claims encompass a genus of structurally and functionally undefined ScFv type proteins comprising a genus of VH domain-a genus of peptide ligand-a genus of VL domain. Applicant has not disclosed sufficient species for the broad genus of SCFv type protein comprising the claimed structure of VH domain-peptide ligand-VL domain and recited features. The specification only describes an anti-VLA-4 scFv that has a structure of a VH domain-peptide ligand-a VL domain, and comprises the amino acid sequence of instant SEQ ID NO:3 and binds to a4b1 integrin, and wherein the VH comprises the sequence of SEQ ID NO: 5 (aa Q117-S237 of SEQ ID NO:3), the peptide ligand comprises the sequence of SEQ ID NO:16 (-GGGGS-) and the VL comprises the sequence of SEQ ID NO:6 (aa D1-I111 of SEQ ID NO:3).
The specification provides no structural and functional relationship between the claimed genus of ScFv type protein and the binding specificity and affinity to a defined antigen. The specification provides no structural and functional relationship between the claimed genus of ScFv type protein and the anti-VLA-4 ScFv protein comprising the amino acid sequence SEQ ID NO:3 capable of binding to a4b1 integrin or VAL4 shown in Examples. The instant specification fails to provide sufficient descriptive information, such as definitive structural or functional features of the claimed genus of ScFv type proteins comprising the structure of VH domain-peptide ligand-VL domain with no defined sequences for the VH domain, peptide ligand and VL domain. The specification does not teach what other common structures and amino acid sequences can or cannot be changed or included in the claimed genus of ScFv type proteins comprising a genus of VH domain-a genus of peptide ligand-a genus of VL domain. Furthermore, the prior art does not provide compensatory structural or correlative teachings sufficient to enable one of skill to identify what other ScFv type proteins might be. Since the common characteristics/features of other ScFv type proteins are unknown, a skilled artisan cannot contemplate the functional correlations of the genus with the claimed invention. Accordingly, in the absence of sufficient recitation of distinguishing identifying characteristics, the specification does not provide adequate written description of the genus of ScFv type proteins.
Response to Arguments
On p. 16-17 of the response, Applicant argues that i) claim 1 is not a functional claim to any protein binding to a4b1 integrin. Instead claim 1 is a specific and structurally defined class of molecules having the structure and features recited in claim 1; ii) the specification provides support to demonstrate possession of the claimed ScFv comprising the sequence of SEQ ID NO:3 or the VH of SEQ ID NO:5 and the VL of SEQ ID NO:6 or the CDR of SEQ ID NOs: 7-12 and cites para. [0074] and MPEP2163, Amgen, Inc. v. Sanofi in support of the arguments.
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 ScFv type protein comprising a structure of VH domain-peptide ligand-VL domain, wherein the VH comprises at least amino acids N173, Y176, K181, Y217, Y222 from SEQ ID NO:3 and the VL comprises at least amino acids K31, Y33, N35 from SEQ ID NO:3 because:
i. There is no structural and functional relationship or correlation between the claimed genus of a ScFv type protein comprising a structure of VH domain-peptide ligand-VL domain, wherein the VH comprises at least amino acids N173, Y176, K181, Y217, Y222 from SEQ ID NO:3 and the VL comprises at least amino acids K31, Y33, N35 from SEQ ID NO:3 and the binding specificity and affinity to a defined antigen.
There is also no structural and functional relationship between the claimed genus of ScFv type protein and the anti-VLA-4 ScFv protein comprising the amino acid sequence SEQ ID NO:3 capable of binding to a4b1 integrin or VAL4 shown in Examples.
The specification provides no structural and functional relationship between the claimed ScFv type protein and the binding specificity and affinity to a defined antigen except the anti-VLA-4 ScFv protein comprising the amino acid sequence SEQ ID NO:3 capable of binding to a4b1 integrin or VAL4 shown in Examples.
The specification’s general reference to “ScFv type protein comprising the structure of VH-peptide ligand-VL and VH comprising at least amino acids N173, Y176, K181, Y217, Y222 from SEQ ID NO:3 and the VL comprises at least amino acids K31, Y33, N35 from SEQ ID NO:3” does not clearly suggest a particular sequence of structurally and functionally undefined ScFv for any binding activity or epitope. A skilled artisan cannot envision the functional correlations of the claimed genus with the claimed invention.
The specification fails to teach what other structures/amino acid sequences can or cannot be included/changed in the claimed ScFv type protein in order to preserve any specific activity or the activity of anti-VLA-4 ScFv protein comprising the amino acid sequence SEQ ID NO:3 capable of binding to a4b1 integrin or VAL4 shown in Examples. The specification provides no identification of any particular portion of the structure that must be conserved for the claimed genus of structurally and functionally undefined ScFv type protein comprising the structure and features with no defined sequences for the VH domain, peptide ligand and VL domain and function or activity.
There is no information regarding the relation of structure of the caimed genus of ScFv to the function of any specific binding activity or epitopes or anti-VLA-4 ScFv protein comprising SEQ ID NO:3. Furthermore, the prior art does not provide compensatory structural or correlative teachings sufficient to enable one of skill to identify what other ScFv type proteins might be. Since the common characteristics/features of other ScFv type proteins are unknown, a skilled artisan cannot contemplate the functional correlations of the genus with the claimed invention. Accordingly, in the absence of sufficient recitation of distinguishing identifying characteristics, the specification does not provide adequate written description of the genus of ScFv type proteins.
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 ScFv type proteins comprising the structure of VH domain-peptide ligand-VL domain with no defined sequences for the VH domain, peptide ligand and VL domain, 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 ScFv type protein comprising the structure of VH domain-peptide ligand-VL domain with no defined sequences for the VH domain, peptide ligand and VL domain 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 1-6 and 13 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.
New Grounds of Rejection Necessitated by the Amendment
The following rejections are new grounds of rejections necessitated by the amendment filed on July 9, 2026.
Claim Rejections - 35 USC § 102
10. 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 1, 4-6 and 13 stand rejected under 35 U.S.C. 102(a)(1) as being anticipated by Yuan et al. (Biochem J., 1996; 318:591-596, as in IDS) as evidenced by Hanf et al. (Methods, 2014; 65:68-76, cited previously).
Claims 1, 4-6 and 13 as amended are drawn to a ScFv type protein comprising a structure of VH domain-peptide ligand-VL domain, wherein the VH comprises at least amino acids N173, Y176, K181, Y217, Y222 from SEQ ID NO:3 and the VL comprises at least amino acids K31, Y33, N35 from SEQ ID NO:3.
Yuan et al. teach an anti-VLA-4 ScFv antibody sFv-195 comprising a structure of a VH-a linker (GGGGS)x-a VL-KDEL (see figure 1 below) and capable of binding to VLA-4 (i.e. a4b1 integrin), and wherein the VH and VL comprise the sequences of VH and VL from anti-a4 integrin antibody HP1/2 (see abstract; p.592, 1st col.), which meets the limitations recited in instant claims 1, 4-6 and 13 because the sequence of the VH domain from anti-a4 integrin antibody HP1/2 comprises at least amino acids N173, Y176, K181, Y217 and Y222 from SEQ ID NO:3 and the sequence of the VL domain comprises at least amino acids K31, Y33, N35 from SEQ ID NO:3 as evidenced by Hanf et al. (see p. 72, figure 1 in Hanf et al., Methods, 2014; 65:68-76). The linker in the ScFv protein disclosed by Yuan contains –(GGGGS)x-(instant SEQ ID NO:16), which meets the limitations recited in claims 4-5 (see p.592, 1st col.). Yuan teaches the anti-VLA-4 ScFv antibody sFv-195 in a culture medium (see p.592, 1st col.), which meets the limitation “a composition comprising the ScFv protein and a pharmaceutically acceptable excipient” recited in claim. The anti-VLA-4 ScFv antibody sFv-195 disclosed by Yuan can bind to a4b1 integrin as in claim 6 because VLA-4 is a4b1 integrin, and the ScFv protein disclosed by Yuan has the same structure and comprise the same sequences as the instantly claimed scFv type protein. Thus, claims 1, 4-6 and 13 are anticipated by Yuan.
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Conclusion
11. NO CLAIM IS ALLOWED.
12. The prior art made of record and not relied upon is considered pertinent to applicant's disclosure.
Hu et al. (US20190309092) teaches a modified single chain antigen-binding fragment comprising a structure of VL domain-linker (GGGGS)x-VH domain-CH1 and having the amino acid sequence of SEQ ID NO:12, wherein the VH comprises at least amino acids N173, Y176, K181, Y217 and Y222 from SEQ ID NO:3 and the VL domain comprises at least amino acids K31, Y33, N35 from SEQ ID NO:3 (see the sequence alignment below).
SEQ ID NO:3
US-16-318-615-12
Sequence 12, US/16318615
Publication No. US20190309092A1
GENERAL INFORMATION
APPLICANT: Hu, Chih-Yung
APPLICANT: Huang, Chao-Yang
APPLICANT: Chen, Yu-Jung
APPLICANT: Wu, Chia-Cheng
APPLICANT: Kuan, Chien-Tsun
APPLICANT: Lo, Chia-Hsiang
APPLICANT: Tsai, Hsien-yu
TITLE OF INVENTION: MODIFIED ANTIGEN-BINDING FAB FRAGMENTS AND ANTIGEN-BINDING
TITLE OF INVENTION: MOLECULES COMPRISING THE SAME
FILE REFERENCE: D62975/PC0095
CURRENT APPLICATION NUMBER: US/16/318,615
CURRENT FILING DATE: 2019-01-17
PRIOR APPLICATION NUMBER: US 62/364,854
PRIOR FILING DATE: 2016-07-21
NUMBER OF SEQ ID NOS: 17
SEQ ID NO 12
LENGTH: 578
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: VL1-Linker-VH1-CH1-CH2-CH3(Knob)
Query Match 94.6%; Score 1189; Length 578;
Best Local Similarity 92.0%;
Matches 229; Conservative 0; Mismatches 8; Indels 12; Gaps 1;
Qy 1 DVVMTQSPLSLPVTPGEPASISCRSSQSLAKSYSNTYLSWYLQKPGQSPQLLIYGIGNGG 60
||||||||||||||||||||||||||||||||| |||||||||||||||||||||| |
Db 1 DVVMTQSPLSLPVTPGEPASISCRSSQSLAKSYGNTYLSWYLQKPGQSPQLLIYGISNRF 60
Qy 61 SGVPARFSGSGSGTDFTLLISRVEAEDVGVYYCLQGTHQPYTFGQGTKVEI--------- 111
|||| ||||||||||||| ||||||||||||||||||||||||||||||||
Db 61 SGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCLQGTHQPYTFGQGTKVEIKRCGGGSGG 120
Qy 112 ---GGGGSQVQLVQSGAEVKKPGASVKVSCKGSGYTFTSYWMHWVRQAPGQRLEWIGEIG 168
||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 GGSGGGGSQVQLVQSGAEVKKPGASVKVSCKGSGYTFTSYWMHWVRQAPGQRLEWIGEID 180
Qy 169 PSESNTNYNQKFKGRVTLTVDISASTAYMELSSLRSEDTAVYYCARGGYAGWDYAIDYWG 228
||||||||||||||||||||||||||||||||||||||||||||||||| ||||||||||
Db 181 PSESNTNYNQKFKGRVTLTVDISASTAYMELSSLRSEDTAVYYCARGGYDGWDYAIDYWG 240
Qy 229 QGTLVTVSS 237
|||||||||
Db 241 QGTLVTVSS 249
SEQ ID NO:5-SEQ ID NO:6
US-16-318-615-12
Sequence 12, US/16318615
Publication No. US20190309092A1
GENERAL INFORMATION
APPLICANT: Hu, Chih-Yung
APPLICANT: Huang, Chao-Yang
APPLICANT: Chen, Yu-Jung
APPLICANT: Wu, Chia-Cheng
APPLICANT: Kuan, Chien-Tsun
APPLICANT: Lo, Chia-Hsiang
APPLICANT: Tsai, Hsien-yu
TITLE OF INVENTION: MODIFIED ANTIGEN-BINDING FAB FRAGMENTS AND ANTIGEN-BINDING
TITLE OF INVENTION: MOLECULES COMPRISING THE SAME
FILE REFERENCE: D62975/PC0095
CURRENT APPLICATION NUMBER: US/16/318,615
CURRENT FILING DATE: 2019-01-17
PRIOR APPLICATION NUMBER: US 62/364,854
PRIOR FILING DATE: 2016-07-21
NUMBER OF SEQ ID NOS: 17
SEQ ID NO 12
LENGTH: 578
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: VL1-Linker-VH1-CH1-CH2-CH3(Knob)
Query Match 94.8%; Score 1165.3; Length 578;
Best Local Similarity 90.0%;
Matches 224; Conservative 0; Mismatches 8; Indels 17; Gaps 1;
Qy 1 DVVMTQSPLSLPVTPGEPASISCRSSQSLAKSYSNTYLSWYLQKPGQSPQLLIYGIGNGG 60
||||||||||||||||||||||||||||||||| |||||||||||||||||||||| |
Db 1 DVVMTQSPLSLPVTPGEPASISCRSSQSLAKSYGNTYLSWYLQKPGQSPQLLIYGISNRF 60
Qy 61 SGVPARFSGSGSGTDFTLLISRVEAEDVGVYYCLQGTHQPYTFGQGTKVEI--------- 111
|||| ||||||||||||| ||||||||||||||||||||||||||||||||
Db 61 SGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCLQGTHQPYTFGQGTKVEIKRCGGGSGG 120
Qy 112 --------QVQLVQSGAEVKKPGASVKVSCKGSGYTFTSYWMHWVRQAPGQRLEWIGEIG 163
|||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 GGSGGGGSQVQLVQSGAEVKKPGASVKVSCKGSGYTFTSYWMHWVRQAPGQRLEWIGEID 180
Qy 164 PSESNTNYNQKFKGRVTLTVDISASTAYMELSSLRSEDTAVYYCARGGYAGWDYAIDYWG 223
||||||||||||||||||||||||||||||||||||||||||||||||| ||||||||||
Db 181 PSESNTNYNQKFKGRVTLTVDISASTAYMELSSLRSEDTAVYYCARGGYDGWDYAIDYWG 240
Qy 224 QGTLVTVSS 232
|||||||||
Db 241 QGTLVTVSS 249
SEQ ID NO:7-SEQ ID NO:8-SEQ ID NO:9
US-16-318-615-12
Sequence 12, US/16318615
Publication No. US20190309092A1
GENERAL INFORMATION
APPLICANT: Hu, Chih-Yung
APPLICANT: Huang, Chao-Yang
APPLICANT: Chen, Yu-Jung
APPLICANT: Wu, Chia-Cheng
APPLICANT: Kuan, Chien-Tsun
APPLICANT: Lo, Chia-Hsiang
APPLICANT: Tsai, Hsien-yu
TITLE OF INVENTION: MODIFIED ANTIGEN-BINDING FAB FRAGMENTS AND ANTIGEN-BINDING
TITLE OF INVENTION: MOLECULES COMPRISING THE SAME
FILE REFERENCE: D62975/PC0095
CURRENT APPLICATION NUMBER: US/16/318,615
CURRENT FILING DATE: 2019-01-17
PRIOR APPLICATION NUMBER: US 62/364,854
PRIOR FILING DATE: 2016-07-21
NUMBER OF SEQ ID NOS: 17
SEQ ID NO 12
LENGTH: 578
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: VL1-Linker-VH1-CH1-CH2-CH3(Knob)
Query Match 77.6%; Score 177; Length 578;
Best Local Similarity 46.3%;
Matches 38; Conservative 0; Mismatches 4; Indels 40; Gaps 2;
Qy 1 SCRSSQSLAKSYSNTYLSW-----------LIYGIGNGGSGVP----------------- 32
|||||||||||| |||||| ||||| | ||||
Db 22 SCRSSQSLAKSYGNTYLSWYLQKPGQSPQLLIYGISNRFSGVPDRFSGSGSGTDFTLKIS 81
Qy 33 ------------LQGTHQPYTF 42
||||||||||
Db 82 RVEAEDVGVYYCLQGTHQPYTF 103
SEQ ID NO:10-SEQ ID NO:11-SEQ ID NO:12
US-16-318-615-12
Sequence 12, US/16318615
Publication No. US20190309092A1
GENERAL INFORMATION
APPLICANT: Hu, Chih-Yung
APPLICANT: Huang, Chao-Yang
APPLICANT: Chen, Yu-Jung
APPLICANT: Wu, Chia-Cheng
APPLICANT: Kuan, Chien-Tsun
APPLICANT: Lo, Chia-Hsiang
APPLICANT: Tsai, Hsien-yu
TITLE OF INVENTION: MODIFIED ANTIGEN-BINDING FAB FRAGMENTS AND ANTIGEN-BINDING
TITLE OF INVENTION: MOLECULES COMPRISING THE SAME
FILE REFERENCE: D62975/PC0095
CURRENT APPLICATION NUMBER: US/16/318,615
CURRENT FILING DATE: 2019-01-17
PRIOR APPLICATION NUMBER: US 62/364,854
PRIOR FILING DATE: 2016-07-21
NUMBER OF SEQ ID NOS: 17
SEQ ID NO 12
LENGTH: 578
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: VL1-Linker-VH1-CH1-CH2-CH3(Knob)
Query Match 85.6%; Score 222.6; Length 578;
Best Local Similarity 47.7%;
Matches 42; Conservative 0; Mismatches 2; Indels 44; Gaps 2;
Qy 1 SGYTFTSYWMH--------------EIGPSESNTNYNQKFKGRV---------------- 30
||||||||||| || ||||||||||||||||
Db 153 SGYTFTSYWMHWVRQAPGQRLEWIGEIDPSESNTNYNQKFKGRVTLTVDISASTAYMELS 212
Qy 31 --------------GGYAGWDYAIDYWG 44
||| ||||||||||
Db 213 SLRSEDTAVYYCARGGYDGWDYAIDYWG 240
WO2018017863 (as in IDS) teaches a modified Fab single chain antibody protein comprising a structure of VL-linker-VH-CH1 and having the sequence of SEQ ID NO:12, which meets the limitations recited in claim 1 (see the sequence alignment below).
SEQ ID NO:3
BEY89577
ID BEY89577 standard; protein; 578 AA.
XX
AC BEY89577;
XX
DT 22-MAR-2018 (first entry)
XX
DE VL1-Linker-VH1-CH1-CH2-CH3(Knob) peptide construct, SEQ ID 12.
XX
KW antibody therapy; antimicrobial-gen.; cancer; cytostatic;
KW infectious disease; therapeutic.
XX
OS Synthetic.
OS Unidentified.
XX
CC PN WO2018017863-A1.
XX
CC PD 25-JAN-2018.
XX
CC PF 20-JUL-2017; 2017WO-US043126.
XX
PR 21-JUL-2016; 2016US-0364854P.
XX
CC PA (DCBU-) DCB-USA LLC.
CC PA (BIOT-) DEV CENT BIOTECHNOLOGY.
XX
CC PI Hu C, Huang C, Chen Y, Wu C, Kuan C, Lo C, Tsai H;
XX
DR WPI; 2018-07404W/11.
XX
CC PT New modified antigen-binding Fab fragment comprising light and heavy
CC PT chain variable domains and light and heavy chain constant domains, useful
CC PT for treating cancers and infectious diseases.
XX
CC PS Example 1; SEQ ID NO 12; 53pp; English.
XX
CC The present invention relates to a novel modified antigen-binding Fab
CC fragment, useful for treating cancers and infectious diseases. The
CC invention further relates to: (1) an antigen-binding molecule comprising
CC two or more of the antigen-binding Fab fragments defined above; (2) a
CC polynucleotide encoding the antigen-binding Fab fragment; (3) a vector
CC comprising polynucleotides encoding the antigen-binding Fab fragment; (4)
CC a host cell comprising the vector; and (5) a method for preparing the
CC antigen-binding molecule. The antigen-binding Fab fragment and the
CC antigen-binding molecule are useful for treating cancers, infectious
CC diseases, other diseases or disorders. The present sequence is a VL1-
CC Linker-VH1-CH1-CH2-CH3(Knob) peptide construct, useful for treating
CC diseases.
XX
SQ Sequence 578 AA;
Query Match 94.6%; Score 1189; Length 578;
Best Local Similarity 92.0%;
Matches 229; Conservative 0; Mismatches 8; Indels 12; Gaps 1;
Qy 1 DVVMTQSPLSLPVTPGEPASISCRSSQSLAKSYSNTYLSWYLQKPGQSPQLLIYGIGNGG 60
||||||||||||||||||||||||||||||||| |||||||||||||||||||||| |
Db 1 DVVMTQSPLSLPVTPGEPASISCRSSQSLAKSYGNTYLSWYLQKPGQSPQLLIYGISNRF 60
Qy 61 SGVPARFSGSGSGTDFTLLISRVEAEDVGVYYCLQGTHQPYTFGQGTKVEI--------- 111
|||| ||||||||||||| ||||||||||||||||||||||||||||||||
Db 61 SGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCLQGTHQPYTFGQGTKVEIKRCGGGSGG 120
Qy 112 ---GGGGSQVQLVQSGAEVKKPGASVKVSCKGSGYTFTSYWMHWVRQAPGQRLEWIGEIG 168
||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 GGSGGGGSQVQLVQSGAEVKKPGASVKVSCKGSGYTFTSYWMHWVRQAPGQRLEWIGEID 180
Qy 169 PSESNTNYNQKFKGRVTLTVDISASTAYMELSSLRSEDTAVYYCARGGYAGWDYAIDYWG 228
||||||||||||||||||||||||||||||||||||||||||||||||| ||||||||||
Db 181 PSESNTNYNQKFKGRVTLTVDISASTAYMELSSLRSEDTAVYYCARGGYDGWDYAIDYWG 240
Qy 229 QGTLVTVSS 237
|||||||||
Db 241 QGTLVTVSS 249
SEQ ID NO:7-SEQ ID NO:8-SEQ ID NO:9
BEY89577
ID BEY89577 standard; protein; 578 AA.
XX
AC BEY89577;
XX
DT 22-MAR-2018 (first entry)
XX
DE VL1-Linker-VH1-CH1-CH2-CH3(Knob) peptide construct, SEQ ID 12.
XX
KW antibody therapy; antimicrobial-gen.; cancer; cytostatic;
KW infectious disease; therapeutic.
XX
OS Synthetic.
OS Unidentified.
XX
CC PN WO2018017863-A1.
XX
CC PD 25-JAN-2018.
XX
CC PF 20-JUL-2017; 2017WO-US043126.
XX
PR 21-JUL-2016; 2016US-0364854P.
XX
CC PA (DCBU-) DCB-USA LLC.
CC PA (BIOT-) DEV CENT BIOTECHNOLOGY.
XX
CC PI Hu C, Huang C, Chen Y, Wu C, Kuan C, Lo C, Tsai H;
XX
DR WPI; 2018-07404W/11.
XX
CC PT New modified antigen-binding Fab fragment comprising light and heavy
CC PT chain variable domains and light and heavy chain constant domains, useful
CC PT for treating cancers and infectious diseases.
XX
CC PS Example 1; SEQ ID NO 12; 53pp; English.
XX
CC The present invention relates to a novel modified antigen-binding Fab
CC fragment, useful for treating cancers and infectious diseases. The
CC invention further relates to: (1) an antigen-binding molecule comprising
CC two or more of the antigen-binding Fab fragments defined above; (2) a
CC polynucleotide encoding the antigen-binding Fab fragment; (3) a vector
CC comprising polynucleotides encoding the antigen-binding Fab fragment; (4)
CC a host cell comprising the vector; and (5) a method for preparing the
CC antigen-binding molecule. The antigen-binding Fab fragment and the
CC antigen-binding molecule are useful for treating cancers, infectious
CC diseases, other diseases or disorders. The present sequence is a VL1-
CC Linker-VH1-CH1-CH2-CH3(Knob) peptide construct, useful for treating
CC diseases.
XX
SQ Sequence 578 AA;
Query Match 77.6%; Score 177; Length 578;
Best Local Similarity 46.3%;
Matches 38; Conservative 0; Mismatches 4; Indels 40; Gaps 2;
Qy 1 SCRSSQSLAKSYSNTYLSW-----------LIYGIGNGGSGVP----------------- 32
|||||||||||| |||||| ||||| | ||||
Db 22 SCRSSQSLAKSYGNTYLSWYLQKPGQSPQLLIYGISNRFSGVPDRFSGSGSGTDFTLKIS 81
Qy 33 ------------LQGTHQPYTF 42
||||||||||
Db 82 RVEAEDVGVYYCLQGTHQPYTF 103
SEQ ID NO:10-SEQ ID NO:11-SEQ ID NO:12
BEY89577
ID BEY89577 standard; protein; 578 AA.
XX
AC BEY89577;
XX
DT 22-MAR-2018 (first entry)
XX
DE VL1-Linker-VH1-CH1-CH2-CH3(Knob) peptide construct, SEQ ID 12.
XX
KW antibody therapy; antimicrobial-gen.; cancer; cytostatic;
KW infectious disease; therapeutic.
XX
OS Synthetic.
OS Unidentified.
XX
CC PN WO2018017863-A1.
XX
CC PD 25-JAN-2018.
XX
CC PF 20-JUL-2017; 2017WO-US043126.
XX
PR 21-JUL-2016; 2016US-0364854P.
XX
CC PA (DCBU-) DCB-USA LLC.
CC PA (BIOT-) DEV CENT BIOTECHNOLOGY.
XX
CC PI Hu C, Huang C, Chen Y, Wu C, Kuan C, Lo C, Tsai H;
XX
DR WPI; 2018-07404W/11.
XX
CC PT New modified antigen-binding Fab fragment comprising light and heavy
CC PT chain variable domains and light and heavy chain constant domains, useful
CC PT for treating cancers and infectious diseases.
XX
CC PS Example 1; SEQ ID NO 12; 53pp; English.
XX
CC The present invention relates to a novel modified antigen-binding Fab
CC fragment, useful for treating cancers and infectious diseases. The
CC invention further relates to: (1) an antigen-binding molecule comprising
CC two or more of the antigen-binding Fab fragments defined above; (2) a
CC polynucleotide encoding the antigen-binding Fab fragment; (3) a vector
CC comprising polynucleotides encoding the antigen-binding Fab fragment; (4)
CC a host cell comprising the vector; and (5) a method for preparing the
CC antigen-binding molecule. The antigen-binding Fab fragment and the
CC antigen-binding molecule are useful for treating cancers, infectious
CC diseases, other diseases or disorders. The present sequence is a VL1-
CC Linker-VH1-CH1-CH2-CH3(Knob) peptide construct, useful for treating
CC diseases.
XX
SQ Sequence 578 AA;
Query Match 85.6%; Score 222.6; Length 578;
Best Local Similarity 47.7%;
Matches 42; Conservative 0; Mismatches 2; Indels 44; Gaps 2;
Qy 1 SGYTFTSYWMH--------------EIGPSESNTNYNQKFKGRV---------------- 30
||||||||||| || ||||||||||||||||
Db 153 SGYTFTSYWMHWVRQAPGQRLEWIGEIDPSESNTNYNQKFKGRVTLTVDISASTAYMELS 212
Qy 31 --------------GGYAGWDYAIDYWG 44
||| ||||||||||
Db 213 SLRSEDTAVYYCARGGYDGWDYAIDYWG 240
SEQ ID NO:5-SEQ ID NO:6
BEY89577
ID BEY89577 standard; protein; 578 AA.
XX
AC BEY89577;
XX
DT 22-MAR-2018 (first entry)
XX
DE VL1-Linker-VH1-CH1-CH2-CH3(Knob) peptide construct, SEQ ID 12.
XX
KW antibody therapy; antimicrobial-gen.; cancer; cytostatic;
KW infectious disease; therapeutic.
XX
OS Synthetic.
OS Unidentified.
XX
CC PN WO2018017863-A1.
XX
CC PD 25-JAN-2018.
XX
CC PF 20-JUL-2017; 2017WO-US043126.
XX
PR 21-JUL-2016; 2016US-0364854P.
XX
CC PA (DCBU-) DCB-USA LLC.
CC PA (BIOT-) DEV CENT BIOTECHNOLOGY.
XX
CC PI Hu C, Huang C, Chen Y, Wu C, Kuan C, Lo C, Tsai H;
XX
DR WPI; 2018-07404W/11.
XX
CC PT New modified antigen-binding Fab fragment comprising light and heavy
CC PT chain variable domains and light and heavy chain constant domains, useful
CC PT for treating cancers and infectious diseases.
XX
CC PS Example 1; SEQ ID NO 12; 53pp; English.
XX
CC The present invention relates to a novel modified antigen-binding Fab
CC fragment, useful for treating cancers and infectious diseases. The
CC invention further relates to: (1) an antigen-binding molecule comprising
CC two or more of the antigen-binding Fab fragments defined above; (2) a
CC polynucleotide encoding the antigen-binding Fab fragment; (3) a vector
CC comprising polynucleotides encoding the antigen-binding Fab fragment; (4)
CC a host cell comprising the vector; and (5) a method for preparing the
CC antigen-binding molecule. The antigen-binding Fab fragment and the
CC antigen-binding molecule are useful for treating cancers, infectious
CC diseases, other diseases or disorders. The present sequence is a VL1-
CC Linker-VH1-CH1-CH2-CH3(Knob) peptide construct, useful for treating
CC diseases.
XX
SQ Sequence 578 AA;
Query Match 94.8%; Score 1165.3; Length 578;
Best Local Similarity 90.0%;
Matches 224; Conservative 0; Mismatches 8; Indels 17; Gaps 1;
Qy 1 DVVMTQSPLSLPVTPGEPASISCRSSQSLAKSYSNTYLSWYLQKPGQSPQLLIYGIGNGG 60
||||||||||||||||||||||||||||||||| |||||||||||||||||||||| |
Db 1 DVVMTQSPLSLPVTPGEPASISCRSSQSLAKSYGNTYLSWYLQKPGQSPQLLIYGISNRF 60
Qy 61 SGVPARFSGSGSGTDFTLLISRVEAEDVGVYYCLQGTHQPYTFGQGTKVEI--------- 111
|||| ||||||||||||| ||||||||||||||||||||||||||||||||
Db 61 SGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCLQGTHQPYTFGQGTKVEIKRCGGGSGG 120
Qy 112 --------QVQLVQSGAEVKKPGASVKVSCKGSGYTFTSYWMHWVRQAPGQRLEWIGEIG 163
|||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 GGSGGGGSQVQLVQSGAEVKKPGASVKVSCKGSGYTFTSYWMHWVRQAPGQRLEWIGEID 180
Qy 164 PSESNTNYNQKFKGRVTLTVDISASTAYMELSSLRSEDTAVYYCARGGYAGWDYAIDYWG 223
||||||||||||||||||||||||||||||||||||||||||||||||| ||||||||||
Db 181 PSESNTNYNQKFKGRVTLTVDISASTAYMELSSLRSEDTAVYYCARGGYDGWDYAIDYWG 240
Qy 224 QGTLVTVSS 232
|||||||||
Db 241 QGTLVTVSS 249
13. Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
14. 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.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
Chang-Yu Wang
October 6, 2026
/CHANG-YU WANG/Primary Examiner, Art Unit 1675
