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SUMMARY:Telling membranes where to go - the macroautophagy machinery in ph
 agocytosis and viral envelope acquisition - Professor  Christian Münz\, V
 iral Immunobiology\, University of Zürich\, Switzerland
DTSTART:20220302T133000Z
DTEND:20220302T143000Z
UID:TALK168983@talks.cam.ac.uk
CONTACT:Bobbie Claxton
DESCRIPTION:Macroautophagy delivers cytoplasmic constituents to lysosomes 
 for degradation. However\, the machinery that mediates autophagosome forma
 tion and their degradation\, participates also in other membrane trafficki
 ng events\, including endo- and exocytosis. Among these\, phagocytosis ass
 ociated with the autophagosome marker LC3 (LAP) contributes to antigen pre
 sentation on MHC class II molecules for helper CD4+ T cell stimulation. Du
 ring LAP\, reactive oxygen species (ROS) produced by NADPH oxidase 2 (NOX2
 ) stabilize LAPosomes in human macrophages by inhibiting LC3 deconjugation
  from their cytosolic surface. Oxidation-mediated inhibition of the LC3B-d
 econjugating ATG4B protease sustains MHC class II presentation of exogenou
 s fungal antigens. Redox regulation of ATG4B is therefore an important mec
 hanism for maintaining LC3 decoration of LAPosomes to support antigen proc
 essing for MHC class II presentation.\n\nIn contrast to this immunity prom
 oting function of the macroautophagy machinery\, viruses use parts of it f
 or cytosolic replication compartments and envelope acquisition during non-
 lytic release. Along these lines\, several components of the macroautophag
 y machinery can be found in purified particles of the human oncogenic Epst
 ein Barr virus (EBV). A viral capsid scaffolding protein that is also cont
 ained in purified EBV particles was found to bind to both LC3B\, preferent
 ially in its lipidated form\, and a viral glycoprotein of the EBV envelope
 . Accordingly\, even in the absence of an essential function of this EBV c
 apsid scaffolding protein for infectious virus production\, viral glycopro
 tein containing membranes were released. These findings suggest a role for
  LC3B binding to an EBV capsid scaffolding protein in the assembly and rel
 ease of EBV envelope-like membranes. \n\nClick here to join live - https:/
 /us06web.zoom.us/j/81417271414 
LOCATION:Online via zoom
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