IP Library Granted Patent US 8,337,866
Granted Patent B2
US 8,337,866 · App. 13/227,255 · Granted Dec 25, 2012

Porin B (PorB) as a therapeutic target for prevention and treatment of infection by

Assignee: The Regents of the University of California
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Quick Facts
Patent No.
US 8,337,866
App. No.
13/227,255
Granted
Dec 25, 2012
Kind
B2
Abstract

The present invention features peptides of a PorB polypeptide, which PorB peptides are useful in production of antibodies that bind the full-length PorB polypeptide and as a therapeutic agent. In specific embodiments the invention features a composition comprising one or more PorB peptides (other than a full-length PorB polypeptide), which peptides contain at least one epitope that can elicit Chlamydia -neutralizing antibodies. The invention also features methods for induction of a protective immune response against infection by Chlamydia and Chlamydiophila.

Claims (24)

1. A composition comprising:

an isolated polypeptide up to 60 amino acids in length, wherein the isolated polypeptide contains an amino acid sequence of SEQ ID NO: 12 (QKNACSFDLCNSYDVL), or an amino acid sequence of SEQ ID NO: 12 comprising at least one conservative amino acid substitution, wherein the isolated polypeptide binds to neutralizing C. trachomatis PorB polypeptide-specific antisera; and

a pharmaceutically acceptable carrier.

2. The composition of claim 1 , wherein the isolated polypeptide contains the amino acid sequence of SEQ ID NO: 12.

3. The composition of claim 1 , wherein the isolated polypeptide contains the amino acid sequence of SEQ ID NO: 12 comprising at least one conservative amino acid substitution.

4. The composition of claim 2 , wherein the isolated polypeptide is a fusion polypeptide comprising a non-PorB amino acid sequence and the amino acid sequence of SEQ ID NO:12.

5. The composition of claim 3 , wherein the isolated polypeptide is a fusion polypeptide comprising a non-PorB amino acid sequence and the amino acid sequence of SEQ ID NO:12 comprising at least one conservative amino acid substitution.

6. The composition of claim 1 , wherein the isolated polypeptide is a polypeptide of amino acid sequence of SEQ ID NO:12.

7. The composition of claim 1 , wherein the isolated polypeptide is a polypeptide of amino acid sequence of SEQ ID NO:12 comprising at least one conservative amino acid substitution.

8. The composition of claim 1 , wherein the isolated polypeptide is a polypeptide of amino acid sequence of SEQ ID NO: 7 (FPVIPGINIEQKNACSFDLCNSYDVL).

9. The composition of claim 1 , wherein the isolated polypeptide comprises at least 30 amino acids.

10. The composition of claim 1 , wherein the isolated polypeptide comprises at least 40 amino acids.

11. The composition of claim 1 , wherein the isolated polypeptide comprises at least 50 amino acids.

12. The composition of claim 1 , wherein the composition additionally comprises at least one PorB polypeptide with an amino acid sequence different from the amino acid sequence of SEQ ID NO: 12 or SEQ ID NO: 12 comprising at least one conservative amino acid substitution.

13. The composition of claim 11 , wherein the composition additionally comprises at least one PorB polypeptide with an amino acid sequence selected from the group consisting of: SEQ ID NO:8 (ND2), SEQ ID NO:9 (ND3), and SEQ ID NO:10 (ND4).

14. The composition of claim 1 , wherein the composition additionally comprises at least one PorB polypeptide with an amino acid sequence selected from the group consisting of: SEQ ID NO:11 (B1-2), B2-3 (SEQ ID NO:13), SEQ ID NO:14 (B2-4), SEQ ID NO:15 (B3-2), SEQ ID NO:16 (B3-3), SEQ ID NO:17 (B3-4), SEQ ID NO:18 (B4-4), SEQ ID NO:19 (B5-1), and SEQ ID NO:20 (B5-2).

15. A composition comprising:

an isolated C. trachomatis PorB polypeptide up to 60 amino acids in length containing an amino acid sequence of SEQ ID NO: 12 (QKNACSFDLCNSYDVL), or an amino acid sequence of SEQ ID NO: 12 comprising at least one conservative amino acid substitution, wherein the isolated polypeptide binds to neutralizing C. trachomatis PorB polypeptide-specific antisera; and

a pharmaceutically acceptable carrier.

16. The composition of claim 15 , wherein the isolated polypeptide contains the amino acid sequence of SEQ ID NO: 12.

17. The composition of claim 15 , wherein the isolated polypeptide contains the amino acid sequence of SEQ ID NO: 12 comprising at least one conservative amino acid substitution.

18. The composition of claim 15 , wherein the isolated polypeptide is a polypeptide of amino acid sequence of SEQ ID NO: 12 (QKNACSFDLCNSYDVL).

19. The composition of claim 15 , wherein the isolated polypeptide is a polypeptide of amino acid sequence of SEQ ID NO:12 comprising at least one conservative amino acid substitution.

20. The composition of claim 15 , wherein the composition additionally comprises at least one PorB polypeptide with an amino acid sequence different from the amino acid sequence of SEQ ID NO: 12 or SEQ ID NO:12 comprising at least one conservative amino acid substitution.

Assignments (2)
CONFIRMATORY LICENSE Recorded Oct 3, 2016
From: UNIVERSITY OF CALIFORNIA BERKELEY
To: NATIONAL INSTITUTES OF HEALTH (NIH), U.S. DEPT. OF HEALTH AND HUMAN SERVICES (DHHS), U.S. GOVERNMENT
Reel/Frame 040205/0558 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Dec 20, 2011
From: STEPHENS, RICHARD S.; KAWA, DIANE
To: THE REGENTS OF THE UNIVERSITY OF CALIFORNIA
Reel/Frame 027420/0414 →
Continuity (5)
Continuation 12687063 · Jan 13, 2010
Continuation 11823869 · Jun 27, 2007
Continuation 11414278 · Apr 27, 2006
Division 10094407 · Mar 7, 2002
Related Publication 20120134999A1 · May 31, 2012