BEGIN:VCALENDAR VERSION:2.0 METHOD:PUBLISH PRODID:-//Missouri State University/Calendar of Events//EN CALSCALE:GREGORIAN X-WR-TIMEZONE:America/Chicago BEGIN:VTIMEZONE TZID:America/Chicago BEGIN:DAYLIGHT TZOFFSETFROM:-0600 TZOFFSETTO:-0500 DTSTART:20070311T020000 RRULE:FREQ=YEARLY;BYMONTH=3;BYDAY=2SU TZNAME:CDT END:DAYLIGHT BEGIN:STANDARD TZOFFSETFROM:-0500 TZOFFSETTO:-0600 DTSTART:20071104T020000 RRULE:FREQ=YEARLY;BYMONTH=11;BYDAY=1SU TZNAME:CST END:STANDARD END:VTIMEZONE BEGIN:VEVENT UID:5db1ec99-7428-4e90-99cc-3741b5714844.222636@calendar.missouristate.edu CREATED:20221018T133205Z LAST-MODIFIED:20221018T133205Z LOCATION:Meyer Library\, Duane G. 101 SUMMARY:Chemistry & Biochemistry Seminar: "The Pseudomonas aeruginosa biof ilm matrix protein CdrA" DESCRIPTION:The Chemistry and Biochemistry department will host Dr. Courtn ey Reichhart\, assistant professor at Washington University in St. Louis. \n\n\nA hallmark feature of chronic infections is the formation of microb ial communities called biofilms. Within biofilms\, microbes are encased i n a mesh-like\, biopolymer-rich extracellular matrix. The matrix promotes microbial cell-cell interactions\, adherence to host tissues and protect ion from antimicrobials.\n\n\nThe Pseudomonas aeruginosa biofilm matrix c an include the exopolysaccharides (EPS) Psl and Pel\, extracellular DNA ( eDNA) and proteins. CdrA was the first P. aeruginosa biofilm matrix prote in to be discovered and is required for robust biofilm formation. CdrA pr omotes aggregation via CdrA-EPS interactions. Homology modeling predicted that CdrA has several binding motifs including sites for binding to exop olysaccharides. However\, the high molecular weight and repetitive struct ure of CdrA has made determining its structure\, including its binding mo tifs\, challenging. As such\, we still have limited structural informatio n about CdrA despite that it has been known to be an important matrix pro tein for over a decade. Our early results provide evidence of CdrA struct ure and interactions\, and how these properties relate to its function as a biofilm adhesin. Since CdrA is similar to other structural biofilm mat rix proteins including that it has a repetitive primary structure\, binds to EPS\, and has both cell-associated and secreted forms\, we believe th at our findings may provide general insight into biofilm assembly\, and t he approaches that we are using to study CdrA should be translatable to s imilar adhesins. X-ALT-DESC;FMTTYPE=text/html:<html><head><title></title></head><body><p>Th e Chemistry and Biochemistry department will host Dr. Courtney Reichhart\ , assistant professor at Washington University in St. Louis.</p>\n<p>A ha llmark feature of chronic infections is the formation of microbial commun ities called biofilms. Within biofilms\, microbes are encased in a mesh-l ike\, biopolymer-rich extracellular matrix. The matrix promotes microbial cell-cell interactions\, adherence to host tissues and protection from a ntimicrobials.</p>\n<p>The Pseudomonas aeruginosa biofilm matrix can incl ude the exopolysaccharides (EPS) Psl and Pel\, extracellular DNA (eDNA) a nd proteins. CdrA was the first P. aeruginosa biofilm matrix protein to b e discovered and is required for robust biofilm formation. CdrA promotes aggregation via CdrA-EPS interactions. Homology modeling predicted that C drA has several binding motifs including sites for binding to exopolysacc harides. However\, the high molecular weight and repetitive structure of CdrA has made determining its structure\, including its binding motifs\, challenging. As such\, we still have limited structural information about CdrA despite that it has been known to be an important matrix protein fo r over a decade. Our early results provide evidence of CdrA structure and interactions\, and how these properties relate to its function as a biof ilm adhesin. Since CdrA is similar to other structural biofilm matrix pro teins including that it has a repetitive primary structure\, binds to EPS \, and has both cell-associated and secreted forms\, we believe that our findings may provide general insight into biofilm assembly\, and the appr oaches that we are using to study CdrA should be translatable to similar adhesins.</p>\n<p></p></body></html> DTSTART;TZID=America/Chicago:20221019T153500 DTEND;TZID=America/Chicago:20221019T162500 SEQUENCE:0 URL:https://chemistry.missouristate.edu/Seminars.htm CATEGORIES:Public,Alumni,Current Students,Faculty,Future Students,Staff END:VEVENT END:VCALENDAR