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SUMMARY:Elucidating the Conformational States and Corresponding Membrane Dy
 namics of a Pore-Forming Toxin
LOCATION:Chemistry A101
TZID:America/Denver
DTSTART:20191001T000000
UID:2026-06-05-06-46-06@natsci.colostate.edu
DTSTAMP:20260605T064606
Description:Literature Seminar\nListeriolysin O (LLO) is a toxic protein se
 creted by the pathogen\, Listeria monocytogenes\, which has spurred severa
 l food-borne outbreaks in recent years. LLO mediates the entryway of Liste
 ria into host tissues by assembling transmembrane pores and therefore\, LL
 O is an important target for the development of antimicrobial defenses to 
 combat the spread of Listeria. Although studies upon homologous pore-formi
 ng toxins have aided in identifying the mechanism by which LLO forms these
  pores\, the nature of the structural change that induces the pre-pore to 
 pore transition in the oligomeric LLO assembly is not currently known. Fur
 thermore\, it is thought that the cell membrane plays an integral role in 
 pore formation\, but further investigation is needed to understand how the
  properties of membranes enable or hinder the development of pores and how
  LLO binding impacts the membrane lipid dynamics. This talk will focus on 
 a recent publication that aimed to uncover the conformational states of th
 e LLO protein and the impact of pore development on lipid diffusion within
  an artificial membrane surface using a combination of experimental and co
 mputational methods. 4:00 pm
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