IP Library Granted Patent US 8,853,360
Granted Patent B2
US 8,853,360 · App. 13/167,156 · Granted Oct 7, 2014

Engineered botulinum neurotoxin C1 with selective substrate specificity

Inventors: Meyer B. Jackson (Madison, WI); Dongsheng Wang (Madison, WI)
Assignee: Wisconsin Alumni Research Foundation
C07K14/33G01N2333/33
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Quick Facts
Patent No.
US 8,853,360
App. No.
13/167,156
Granted
Oct 7, 2014
Kind
B2
Abstract

An isolated polypeptide comprising a botulinum neurotoxin C1 light chain having a modified amino acid sequence relative to the sequence of a wild-type botulinum neurotoxin C1 light chain is disclosed. The modified botulinum neurotoxin C1 light chain is capable of selectively cleaving syntaxin protein, but has substantially reduced or no activity against SNAP-25 as compared to wild type botulinum neurotoxin C1 light chain, and is thus useful as a research tool and in medical treatment.

Claims (25)

1. An isolated polypeptide comprising a botulinum neurotoxin C1 light chain having a modified amino acid sequence relative to the amino acid sequence of a wild-type botulinum neurotoxin C1 light chain having the amino acid sequence set forth in SEQ ID NO:1, wherein the modifications comprise:

(a) the amino acid substitutions L200W, M221W, and I226W;

(b) the amino acid substitutions L200W, M221W, and I226H;

(c) the amino acid substitutions L200W, M221W, and I226K;

(d) the amino acid substitutions L200W, M221W, and I226L;

(e) the amino acid substitutions L200W, K216A, S217G, E218K, M221W, and I226W;

(f) the amino acid substitutions L200W, K216A, S217A, E218A, M221W, and I226W;

(g) the amino acid substitutions S51T, R52N, and N53P; or

(h) the amino acid substitutions F50Y, S51T, and R52N;

wherein the modified botulinum neurotoxin C1 light chain is capable of selectively cleaving syntaxin protein but has substantially reduced or no activity against SNAP-25, as compared to the wild-type botulinum neurotoxin C1 light chain.

2. The isolated polypeptide of claim 1 , wherein the modifications comprise:

(a) the amino acid substitutions L200W, M221W, and I226W;

(b) the amino acid substitutions L200W, M221W, and I226H;

(c) the amino acid substitutions L200W, M221W, and I226K;

(d) the amino acid substitutions L200W, M221W, and I226L;

(e) the amino acid substitutions S51T, R52N, and N53P; or

(f) the amino acid substitutions F50Y, S51T, and R52N.

3. The isolated polypeptide of claim 2 , wherein the modifications comprise:

(a) the amino acid substitutions L200W, M221W, and I226W;

(b) the amino acid substitutions L200W, M221W, and I226H;

(c) the amino acid substitutions L200W, M221W, and I226K;

(d) the amino acid substitutions L200W, M221W, and I226L; or

(e) the amino acid substitutions S51T, R52N, and N53P.

4. The isolated polypeptide of claim 3 , wherein the modifications comprise the amino acid substitutions S51T, R52N, and N53P.

5. A composition comprising the isolated polypeptide of claim 1 and a carrier.

Assignments (2)
CONFIRMATORY LICENSE Recorded Jul 11, 2011
From: WISCONSIN ALUMNI RESEARCH FOUNDATION
To: NATIONAL INSTITUTES OF HEALTH (NIH), U.S. DEPT. OF HEALTH AND HUMAN SERVICES (DHHS), U.S. GOVERNMENT
Reel/Frame 026568/0727 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jul 5, 2011
From: JACKSON, MEYER; WANG, DONGSHENG
To: WISCONSIN ALUMNI RESEARCH FOUNDATION
Reel/Frame 026541/0478 →
Continuity (2)
Provisional Application 61357713 · Jun 23, 2010
Related Publication 20110318385A1 · Dec 29, 2011