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BEGIN:VEVENT
DTSTAMP:20260513T081916Z
DTSTART;VALUE=DATE-TIME:20191203T120000
DTEND;VALUE=DATE-TIME:20191203T130000
SUMMARY:SLS/WMS Micro Seminar: Disulfide bond formation underpins antimic
 robial resistance in Enterobacteria\, Dr Despoina Mavridou\, Imperial Co
 llege London
TZID:Europe/London
UID:20191203-8a1785d76dde7e71016e16f5e6e04bd6@warwick.ac.uk
CREATED:20191127T144012Z
DESCRIPTION:Abstract: Extracytoplasmic proteins assume their native struc
 ture with the help of chaperones and folding catalysts en route to their
  final location. Disulfide bond formation plays an integral part in this
  process\, contributing to protein stability and function. Despite their
  simple chemistry\, disulfide bonds are introduced into substrate protei
 ns by dedicated folding pathways in most organisms. In the periplasm of 
 Gram-negative bacteria this is performed by the DSB system\, and more sp
 ecifically by the oxidase DsbA. Although the function of the DSB protein
 s is well characterized and their role in bacterial pathogenesis has bee
 n discussed\, their contribution to antimicrobial resistance (AMR) has n
 ever been explored. We have demonstrated that disulfide bond formation i
 s necessary for the function of key antimicrobial resistance determinant
 s in the cell envelope of Enterobacteria. More specifically\, we have fo
 und that deletion of DsbA abrogates or severely affects the breakdown of
  β-lactam antibiotics by β-lactamases\, resistance to polymyxins due to 
 the activity of mobile colistin resistance (MCR) enzymes and intrinsic r
 esistance to multiple antibiotics arising from the action of Resistance-
 Nodulation-Division (RND) efflux pumps. Such diverse resistance determin
 ants are impaired because the absence of DsbA compromises stability and 
 folding of β-lactamases and MCR enzymes\, whilst also leading to altered
  periplasmic proteostasis indirectly impacting efflux pump function. Imp
 ortantly\, the DSB system is a tractable AMR target\, as chemical inhibi
 tion of disulfide bond formation sensitizes multidrug-resistant clinical
  isolates to several classes of existing antibiotics. We are currently f
 ocused on the discovery of improved DsbA inhibitors since their generati
 on could lead to the development of next-generation antibiotic adjuvants
  that would function as broad-acting resistance breakers.
LOCATION:MBU/A151\, Medical School Building
CATEGORIES:BiomedicalSciences,DivisionalSeminars,BMS_MI,Joint WMS/SLS Mic
 ro
LAST-MODIFIED:20191127T144012Z
ORGANIZER;CN=Jas Bains:
END:VEVENT
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