The patent badge is an abbreviated version of the USPTO patent document. The patent badge does contain a link to the full patent document.
The patent badge is an abbreviated version of the USPTO patent document. The patent badge covers the following: Patent number, Date patent was issued, Date patent was filed, Title of the patent, Applicant, Inventor, Assignee, Attorney firm, Primary examiner, Assistant examiner, CPCs, and Abstract. The patent badge does contain a link to the full patent document (in Adobe Acrobat format, aka pdf). To download or print any patent click here.
Patent No.:
Date of Patent:
Jun. 21, 2005
Filed:
May. 10, 2000
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);
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 (US);
Board of Regents of the University of Texas System, Austin, TX (US);
Abstract
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.