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SUMMARY:Description: TIE proteins: chemical harpoons of Gram-positive bact
 eria - Dr. Ulrich Schwarz-Linek 
DTSTART:20180213T130000Z
DTEND:20180213T140000Z
UID:TALK95779@talks.cam.ac.uk
CONTACT:12292
DESCRIPTION:Bacteria rely on surface-associated proteins for host colonisa
 tion and pathogenesis. TIE proteins are highly prevalent and diverse in Gr
 am-positive bacteria\, and are known or predicted to play roles in bacteri
 al adhesion to host tissue and biofilm formation. These cell wall-anchored
  proteins are composed of domains containing self-generating intramolecula
 r thioester\, isopeptide and ester cross-links between amino acid sidechai
 ns. TIE proteins may have evolved to mediate fast\, mechanically persisten
 t binding of bacteria. The distal adhesin domains of TIE proteins contain 
 reactive thioesters and can be likened to "chemical harpoons"\, covalently
  anchoring bacteria to their targets\, such as host cell surface proteins.
  Bacterial-encoded covalent adhesion is a new molecular principle in host:
 microbe interactions\, and an unexploited antimicrobial target. In additio
 n\, all three TIE domain types offer exciting opportunities for protein en
 gineering.
LOCATION:Department of Biochemistry\, Sanger Building Jean Thomas Lecture 
 Theatre
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