University of Texas Health Science Center at Houston
The Staphylococcus Pseudintermedius Adhesin Spsd Contains A Central Fibronectin-Binding Domain
Abstract
dc:description.abstract<p><em>Staphylococcus pseudintermedius</em> is a Gram-positive bacterium significant because of its ability to cause costly and difficult to treat veterinary infections worldwide. It exhibits several similarities to <em>Staphylococcus aureus</em>, however, very little is known about its surface adhesins. Surface adhesins in <em>S. aureus</em> are significant contributors to pathogenesis. <em>S. pseudintermedius</em> encodes the surface protein SpsD, which contains characteristics of the microbial surface components recognizing adhesive matrix molecules family and confers attachment of the heterologous host <em>Lactococcus lactis</em> to fibronectin. This work has identified a centrally-located fibronectin binding domain in SpsD which binds the 30 kDa N-terminal domain of fibronectin with high affinity. The data indicate that a tandem β-zipper mechanism of binding may be taking place, and warrants further study into SpsD’s role in overall colonization of the host.</p>
Degree
thesis:*- Name thesis:degree_name
- Masters of Science (MS)
- Level thesis:degree_level
- Thesis (MS)
- Year dc:date.available
- 2013
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Bordt, Andrea S.
- Contributors dc:contributor
-
- Dr. Magnus Hook
- Dr. Steven Norris
- Dr. Theresa Koehler
Subjects
dc:subject × 7Identifiers
dc:identifier.*- Repository record dc:identifier
- https://digitalcommons.library.tmc.edu/utgsbs_dissertations/412
- OAI identifier oai:identifier
- oai:digitalcommons.library.tmc.edu:utgsbs_dissertations-1451