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SUMMARY:The assembly of the Chikungunya virus depends on multiple protein-
 protein interactions
DTSTART:20250606T100000Z
DTEND:20250606T110000Z
DTSTAMP:20260810T050900Z
UID:indico-event-1652@indico.cells.es
DESCRIPTION:Speakers: Mauricio Comas-García (Universidad Autónoma San Lu
 ís de Potosí (Mexico))\n\nAbstractChikungunya virus is a single-stranded
  RNA virus that infects mammals and birds and is transmitted by an inverte
 brate vector. This virus belongs to the Alphavirus genus and is structural
 ly characterized by two concentric T = 4 icosahedral shells separated by a
  lipid bilayer. Initially\, it was thought that in the cytoplasm\, the cor
 e (inner shell) was icosahedral\; however\, recent data using Cryo-ET has 
 shown that in the cytoplasm\, the core is amorphous\, and it is only upon 
 interacting with the glycoproteins (E1 and E2) that are in the plasma memb
 rane that the double icosahedron is assembled during budding. Additionally
 \, it was believed that the primary driving force behind assembly and budd
 ing was the interaction between the core and the glycoprotein E2. However\
 , our experimental and coarse-grained simulation data strongly suggest tha
 t other protein-protein interactions are required for correct assembly\, e
 fficient budding\, and particle stability. In particular\, we show that a 
 steric repulsion between trimers of the heterodimers of E1/E2 is required 
 for assembly and particle stability. Furthermore\, we show that removing t
 his steric interaction affects particle morphology\, suggesting that these
  sugars act as a molecular handshake.  \n\nhttps://indico.cells.es/event/
 1652/\n\nZoom: https://zoom.us/j/95503114426?pwd=edsWez8CNkWUBeIaLb1VL2CU5
 WpSv0.1
LOCATION:Maxwell Auditorium (ALBA Synchrotron)
URL:https://indico.cells.es/event/1652/
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