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DTSTART:20110930T113000
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URL:https://murmitoyen.com/events/vanille/udem/detail/68134
LOCATION:Université de Montréal - Pavillon Claire-McNicoll\, 2900\, chemi
 n de la Tour\, Montréal\, QC\, Canada\, H3T 1J6
SUMMARY:Lipoprotein cofactors located in the outer membrane activate bacter
 ial cell wall synthases
DESCRIPTION:Conférence du Dre Catherine Paradis-Bleau\, postdoctoral fello
 w\,Department of Microbiology and Molecular Genetics Harvard Medical Schoo
 l.Cette conférence sera prononcée en anglais Résumé To fortify their 
 cytoplasmic membrane and protect it from osmotic lysis\, bacterial cells t
 ypically surround themselves with a crosslinked polysaccharide meshwork ca
 lled peptidoglycan (PG). The major cellular PG synthases are thought to be
  the penicillinbinding proteins (PBPs)\; the targets of penicillin and rel
 ated antibiotics. Although PBPs have been well characterized in vitro\, su
 rprisingly little is known about how these enzymes build the PG in vivo. U
 sing Escherichia coli as a model organism\, we developed a genetic screen 
 to directly identify factors essential for the in vivo activity of the PBP
 s. We identified two outer membrane lipoproteins of previously unknown fun
 ction as critical PG assembly factors. These proteins have been named LpoA
  and LpoB for lipoprotein modulators of PBP function from the outer membra
 ne. We demonstrated that LpoA and LpoB form specific trans-envelope comple
 xes with their cognate PBP and are essential for PBP function in vivo. Fur
 thermore\, we confirmed that the lipoproteins directly activate their cogn
 ate PBP in vitro. These results indicate that essential PBP accessory prot
 eins play a central role in PG biogenesis\, and like the PBPs they work wi
 th\, these factors are attractive targets for antibiotic development.Conf
 érence présentée par le Département de microbiologie et immunologie de
  l'Université de Montréal. Crédit photo : site Web du Département de m
 icrobiologie et immunologie
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