BARBARA E MURRAY, M.D.
Osteopathic Medicine at Fannin St, Houston, TX

6908994, Jun 21, 2005

May 10, 2000

09/568470

Rebecca L. Rich - Salt Lake City UT, US
Bernd Kriekemeyer - Ulm, DE
Rick T. Owens - Stewartsville NJ, US
Magnus Hook - Houston TX, US
Barbara E. Murray - Houston TX, US
Sreedhar R. Nallapareddy - Houston TX, US
George M. Weinstock - Houston TX, US

The Texas A&M University System - College, Station TX
Board of Regents of the University of Texas System - Austin TX

C07H021/04, C07H021/02, A61K039/00, A61K039/02

536 237, 536 231, 4241841, 4241901, 4242341

A collagen-binding MSCRAMM entitled Ace from enterococcal bacteria is provided which was homologous to the ligand-binding region of Cna, the collagen-binding MSCRAMM from , and which can be utilized in a similar manner as other collagen-binding MSCRAMMs to inhibit adhesion of enterococcal bacteria to extracellular matrix proteins. The N-terminal region of Ace contained a region (residues 174-319), or A domain, which appears to be equivalent to the minimal ligand-binding region of the collagen-binding protein Cna (Cna 151-318), and contains several 47-residue tandem repeat units, called B domain repeat units, between the collagen-binding site and cell wall-associated regions. The Ace protein of the invention can thus be utilized in methods of preventing and/or treating enterococcal infection, and in addition, antibodies raised against Ace, or its A domain, can be used to effectively inhibit the adhesion of enterococcal cells to a collagen substrate. The Ace protein of the present invention is thus a functional collagen-binding MSCRAMM and can be utilized to treat or prevent invention in the same manner as other isolated MSCRAMMs have been utilized, namely in methods of treating or preventing infections and diseases caused by enterococcal bacteria.

2013024, Sep 19, 2013

Feb 4, 2010

13/147612

Eszter Nagy - Vienna, AT
Beatrice Tschanun - Vienna, AT
Markus Hanner - Pressbaum, AT
Manfred Berger - Wiener Neustadt, AT
Andreas Meinke - Pressbaum, AT
Alexander Von Gabain - Vienna, AT
Barbara Murray - Houston TX, US
Kavindra Singh - Houston TX, US

Intercell AG - Vienna

C07K 14/335, C07K 16/12

4241391, 4241901, 424 932, 435 71, 435 711, 435331, 4353201, 514 212, 514 44 R, 530350, 5303873, 5303879, 536 237

The present invention relates to a protective peptide of () or a functional active variant thereof, optionally further consisting of additional amino acid residue(s); a nucleic acid coding for the same; a pharmaceutical composition comprising said peptide or said nucleic acid; an antibody or functional active fragment thereof specifically binding to the antigen; a hybridoma cell line which produces said antibody; a method for producing said antibody; a pharmaceutical composition comprising said antibody; the use of said peptide or said nucleic acid for the manufacture of a medicament for the immunization or treatment of a subject; the use of said antibody or functional fragment thereof for the manufacture of a medicament for the treatment of an infection; a method of diagnosing an infection; and the use of said peptide for the isolation and/or purification and/or identification of an interaction partner of the peptide.

7638135, Dec 29, 2009

Apr 11, 2005

11/102757

Rebecca L. Rich - Salt Lake City UT, US
Bernd Kriekemeyer - Ulm, DE
Rick T. Owens - Stewartsville NJ, US
Magnus Hook - Houston TX, US
Barbara E. Murray - Houston TX, US
Sreedhar R. Nallapareddy - Houston TX, US
George M. Weinstock - Houston TX, US

The Texas A & M University System - College Station TX
Board of Regents of the University of Texas System - Austin TX

A61K 39/02, A61K 39/38, A61K 39/00, C07H 21/02, C07H 21/04

4242341, 4241901, 4241841, 536 231, 536 237

A collagen-binding MSCRAMM entitled Ace from enterococcal bacteria is provided which was homologous to the ligand-binding region of Cna, the collagen-binding MSCRAMM from , and which can be utilized to inhibit adhesion of enterococcal bacteria to extracellular matrix proteins. The N-terminal region of Ace contained a region (residues 174-319), or A domain, contains several 47-residue tandem repeat units between the collagen-binding site and cell wall-associated regions. The Ace protein can be utilized in methods of preventing and/or treating enterococcal infection, and in addition, antibodies raised against Ace, or its A domain, can be used to effectively inhibit the adhesion of enterococcal cells to a collagen substrate.