{"id":{"repo_id":"uthsc","oai_identifier":"oai:digitalcommons.library.tmc.edu:utgsbs_dissertations-1451"},"canonical_url":"https://search.dev.ndltd.org/etd/uthsc/oai:digitalcommons.library.tmc.edu:utgsbs_dissertations-1451","repository":{"repo_id":"uthsc","name":"University of Texas Health Science Center at Houston","base_url":"https://digitalcommons.library.tmc.edu/do/oai/"},"display":{"title":"The Staphylococcus Pseudintermedius Adhesin Spsd Contains A Central Fibronectin-Binding Domain","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>","abstract_html":"&lt;p&gt;&lt;em&gt;Staphylococcus pseudintermedius&lt;/em&gt; 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 &lt;em&gt;Staphylococcus aureus&lt;/em&gt;, however, very little is known about its surface adhesins. Surface adhesins in &lt;em&gt;S. aureus&lt;/em&gt; are significant contributors to pathogenesis. &lt;em&gt;S. pseudintermedius&lt;/em&gt; 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 &lt;em&gt;Lactococcus lactis&lt;/em&gt; 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.&lt;/p&gt;","abstract_has_math":false,"creators":["Bordt, Andrea S."],"institution":null,"degree_name":"Masters of Science (MS)","degree_level":"Thesis (MS)","degree_discipline":null,"degree_department":null,"school":null,"contributors":["Dr. Magnus Hook","Dr. Steven Norris","Dr. Theresa Koehler"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2013,"date_issued":"2013-12-01T08:00:00Z","date_published":"2013-12-01T08:00:00Z","updated_at":"2026-07-24T05:48:47Z","subjects":["Staphylococcus pseudintermedius","SpsD","Fibronectin","Animal Diseases","Biochemistry","Biology","Medicine and Health Sciences"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://digitalcommons.library.tmc.edu/utgsbs_dissertations/412","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Dr. Magnus Hook","Dr. Steven Norris","Dr. Theresa Koehler"]},{"key":"dc:creator","label":"Author","values":["Bordt, Andrea S."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2013-12-13T08:00:00Z"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis (MS)"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Masters of Science (MS)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Staphylococcus pseudintermedius","SpsD","Fibronectin","Animal Diseases","Biochemistry","Biology","Medicine and Health Sciences"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://digitalcommons.library.tmc.edu/utgsbs_dissertations/412"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["<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>"]},{"key":"dc:title","label":"Title","values":["The Staphylococcus Pseudintermedius Adhesin Spsd Contains A Central Fibronectin-Binding Domain"]}]}],"canonical_facts":{"dc:contributor":["Dr. Magnus Hook","Dr. Steven Norris","Dr. Theresa Koehler"],"dc:creator":["Bordt, Andrea S."],"dc:date.available":["2013-12-13T08:00:00Z"],"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>"],"dc:identifier":["https://digitalcommons.library.tmc.edu/utgsbs_dissertations/412"],"dc:subject":["Staphylococcus pseudintermedius","SpsD","Fibronectin","Animal Diseases","Biochemistry","Biology","Medicine and Health Sciences"],"dc:title":["The Staphylococcus Pseudintermedius Adhesin Spsd Contains A Central Fibronectin-Binding Domain"],"thesis:degree_level":["Thesis (MS)"],"thesis:degree_name":["Masters of Science (MS)"]},"updated_at":"2026-07-24T05:48:47Z"}