BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//Memento EPFL//
BEGIN:VEVENT
SUMMARY:Towards a molecular-level understanding of bacterial type 3 secret
 ion:  Resolving cytosolic complex formation in living cells by tracking si
 ngle-molecules
DTSTART:20181213T150000
DTSTAMP:20260528T092929Z
UID:cd4beb5cba396a19f53494085e2f20e268dc813346e4fdb470157a4a
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Andreas Gahlmann Center for Cell and Membrane Physiology
  University of Virginia  \nAbout a third of bacterial proteins are either
  transported across or integrated into the cell membranes\, so that they c
 an perform functions that are vital for bacterial survival in specific env
 ironmental niches. Directional transport of selected proteins often relies
  on large membrane-embedded biomolecular assemblies. For example\, the dua
 l membrane-spanning Type 3 Secretion System (T3SS) enables Gram-negative b
 acterial pathogens to inject so-called effector proteins directly into the
  cytosol of eukaryotic host cells – a virulence mechanism that currently
  results in more than 1 million human deaths per year. While the cocktail 
 of injected effector proteins differs for each pathogen\, the structural p
 roteins of T3SSs are highly conserved\, making Type 3 secretion systems a 
 key target for anti-virulence treatments. Our research focuses on providin
 g a detailed understanding of how T3SSs are functionally regulated at the 
 molecular level and how the T3SS and similar assemblies ultimately enable 
 bacterial survival and virulence. \nIn this talk\, I will describe how si
 ngle-molecule localization and tracking microscopy in different genetic ba
 ckgrounds provides a path towards describing the molecular mechanism(s) of
  type 3 secretion in living cells. Through computational aberration correc
 tion and quantitative numerical analysis\, we determine the subcellular lo
 cations and 3D motion trajectories of single fluorescently labeled protein
 s. Our results indicate that the structural T3SS proteins also exist in fr
 eely diffusing cytosolic complexes with different molecular compositions. 
 Some\, but not all\, of these complexes only form in the presence of other
  T3SS proteins and their abundances change upon activation of secretion. R
 esolving the cytosolic diffusion states of T3SS proteins provides importan
 t insights into the dynamic regulatory network that controls type 3 secret
 ion.
LOCATION:SV 1717 https://plan.epfl.ch/?room==SV%201717
STATUS:CONFIRMED
END:VEVENT
END:VCALENDAR