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SUMMARY:Structural and Functional Characterization of Novel Carbohydrate D
 eacetylase from Bacteroides
DTSTART;VALUE=DATE-TIME:20260609T173000Z
DTEND;VALUE=DATE-TIME:20260609T181500Z
DTSTAMP;VALUE=DATE-TIME:20260606T093820Z
UID:indico-contribution-10367@events.saip.org.za
DESCRIPTION:Speakers: Krystle McLaughlin (Vassar College)\nOther authors: 
 Lilith A. Schwartz1\, Jordan O. Norman1\, Sharika Hasan1\, Olive E. Adamek
 1\, Elisa Dzuong1\, Jasmine C. Lowenstein1\, Olivia G. Yost1\, Banumathi S
 ankaran2\, \n1 Department of Chemistry\, Vassar College\, 124 Raymond Ave\
 , Poughkeepsie\, NY\, 12604\n2 Advanced Light Source\, Lawrence Berkeley N
 ational Lab\, Berkeley CA\n\n\n\nBacteroides ovatus\, a commonly identifie
 d Bacteroides species in the human gut\, has been shown to have beneficial
  effects like the suppression of intestinal inflammation. However\, increa
 sed populations of B. ovatus also correlate with several autoimmune diseas
 e states\, such as Systemic Lupus Erythematosus (SLE). Many host-microbe i
 nteractions depend on bacterial cell surface carbohydrates\, including cap
 sular polysaccharides (CPS). CPS from related B. fragilis has known immuno
 modulatory effects. While their significance is understood\, CPS biosynthe
 sis has not been well studied. In this talk\, we present structural charac
 terization of a polysaccharide deacetylase from Bacteroides ovatus (BoPDA)
  thought to be involved in CPS biosynthesis. High resolution crystal struc
 tures reveal an unusual metal binding strategy for the CE4 family and an a
 typical\, non-modular domain architecture. Carbohydrate binding assays and
  deacetylase activity assays were used to investigate the function of the 
 enzyme. BoPDA is the first protein CPS biosynthetic enzyme from B. ovatus 
 to be characterized\, so this work helps further our understanding of this
  essential bacterial process.\n\nhttps://events.saip.org.za/event/274/cont
 ributions/10367/
LOCATION:
URL:https://events.saip.org.za/event/274/contributions/10367/
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