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SUMMARY:UNRAVELLING THE STRUCTURAL AND MECHANISTIC DIVERSITY OF BACTERIAL 
 AUTOTRANSPORTER VIRULENCE FACTORS
DTSTART;VALUE=DATE-TIME:20161125T030000Z
DTEND;VALUE=DATE-TIME:20161125T031500Z
DTSTAMP;VALUE=DATE-TIME:20260809T073145Z
UID:indico-contribution-830@events01.synchrotron.org.au
DESCRIPTION:Speakers: Jason Paxman (La Trobe University)\nAutotransporter 
 proteins are the largest group of outer membrane and secreted virulence fa
 ctors from important bacterial pathogens such as Salmonella enterica\, Shi
 gella flexneri\, Neisseria meningitidis and pathogenic E. coli strains.  T
 hey are important contributors to bacterial pathogenesis\, functioning as 
 toxins\, adhesins and facilitators of biofilm formation.  Their importance
  to human health has generated great interest.  However\, we are still str
 uggling to understand their mechanisms of action.  There are currently onl
 y 12 structures of autotransporters in the protein data bank.  \n\nOur res
 earch centres on the AIDA-I-type autotransporters which are the largest fa
 mily of autotransporters.  We were the first to determine the structure an
 d mechanism of action for one of these family members Antigen 43a from uro
 pathogenic E. coli (UPEC)1.  Our work showed how Antigen 43 causes aggrega
 tion and biofilm formation\, which are important for UPEC colonisation and
  persistence within the urinary tract.  Since this time we have been using
  the MX beamlines at the Australian Synchrotron to determine the crystal s
 tructures of two new autotransporters.  Our findings have revealed a surpr
 ising structural diversity amongst the autotransporters\, which has allowe
 d us to elucidate their distinct mechanisms of action and roles in bacteri
 al pathogenesis.  Interestingly\, the structures have also revealed how ba
 cteria use post-translational modifications to change the virulence functi
 ons of their proteins.\n\nThis research is also helping us to understand h
 ow we can target these autotransporters for therapeutic intervention.  To 
 this end we are again using X-ray crystallography to help aid us in the de
 velopment of specific inhibitors of key autotransporters.\n\nhttps://event
 s01.synchrotron.org.au/event/39/contributions/830/
LOCATION:NCSS Seminar Room
URL:https://events01.synchrotron.org.au/event/39/contributions/830/
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