IP Library › Granted Patent US 8,128,939
Granted Patent B2
US 8,128,939 · App. 12/102,696 · Granted Mar 6, 2012

Mutants of cholesterol-dependent cytolysins and uses thereof

Assignee: The Board of Regents of the University of Oklahoma
View Patent ↗
Loading inventors, assignments & file history…
Monitor This Case
Get email alerts when status or documents change.
Order Certified Copies
Most orders are placed with the USPTO same day — all within 24 business hours.
Order via The Patent Place →
Pre-filled with this patent's details
Quick Facts
Patent No.
US 8,128,939
App. No.
12/102,696
Granted
Mar 6, 2012
Kind
B2
Abstract

Mutants of cholesterol-dependent cytolysins comprising at least one amino acid substitution in at least one of Loop 1, Loop 2, or Loop 3 of Domain 4, nucleic acids encoding such polypeptide mutants, and compositions and vaccines comprising such polypeptide mutants.

Claims (18)

1. A purified mutant pneumolysin polypeptide comprising an amino acid sequence that is at least 90% identical to SEQ ID NO:1 and comprises a substitution in at least one of amino acid positions 458, 459, and 460; and wherein said mutant pneumolysin polypeptide has reduced hemolytic activity and reduced pore-forming activity as compared to a wild type pneumolysin polypeptide.

2. The purified mutant pneumolysin polypeptide of claim 1 wherein the amino acid sequence is at least 95% identical to SEQ ID NO:1.

3. The purified mutant pneumolysin polypeptide of claim 1 wherein the amino acid sequence is at least 96% identical to SEQ ID NO:1.

4. The purified mutant pneumolysin polypeptide of claim 1 wherein the amino acid sequence is at least 97% identical to SEQ ID NO:1.

5. The purified mutant pneumolysin polypeptide of claim 1 wherein the amino acid sequence is at least 98% identical to SEQ ID NO:1.

6. The purified mutant pneumolysin polypeptide of claim 1 wherein the amino acid sequence is at least 99% identical to SEQ ID NO:1.

7. The purified mutant pneumolysin polypeptide of claim 1 comprising a substitution in amino acid position 458.

8. The purified mutant pneumolysin polypeptide of claim 1 comprising a substitution in amino acid position 459.

9. The purified mutant pneumolysin polypeptide of claim 1 comprising a substitution in amino acid position 460.

10. The purified mutant pneumolysin polypeptide of claim 1 wherein the mutant pneumolysin polypeptide is substantially non-hemolytic, non-pore forming, and non-binding to cell membranes.

11. The purified mutant pneumolysin polypeptide of claim 1 wherein the hemolytic activity is less than 30% of that of the wild type pneumolysin polypeptide.

12. The purified mutant pneumolysin polypeptide of claim 1 wherein the hemolytic activity is less than 20% of that of the wild type pneumolysin polypeptide.

13. The purified mutant pneumolysin polypeptide of claim 1 wherein the hemolytic activity is less than 10% of that of the wild type pneumolysin polypeptide.

14. The purified mutant pneumolysin polypeptide of claim 1 wherein the hemolytic activity is less than 5% of that of the wild type pneumolysin polypeptide.

15. The purified mutant pneumolysin polypeptide of claim 1 wherein the hemolytic activity is less than 1% of that of the wild type pneumolysin polypeptide.

16. A composition comprising one or more of the mutant pneumolysin polypeptides of claim 1 disposed in a pharmaceutically-acceptable carrier, vehicle, adjuvent or diluent.

17. A vaccine comprising the purified mutant pneumolysin polypeptide of claim 1 .

18. The vaccine of claim 12 further comprising capsular polysaccharide serotypes, or immunogenic proteins or protein subunits or fragments.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Aug 4, 2008
From: TWETEN, RODNEY K.
To: THE BOARD OF REGENTS OF THE UNIVERSITY OF OKLAHOMA
Reel/Frame 021336/0291 →
Continuity (2)
Provisional Application 60923281 · Apr 13, 2007
Related Publication 20090285846A1 · Nov 19, 2009