Interactions between the transmembrane segments of the alphavirus E1 and E2 proteins play a role in virus budding and fusion.

ABSTRACT: The alphavirus envelope is built by heterodimers of the membrane proteins E1 and E2. The complex is formed as a p62E1 precursor in the endoplasmic reticulum. During transit to the plasma membrane (PM), it is cleaved into mature E1-E2 heterodimers, which are oligomerized into trimeric complexes, so-called spikes that bind both to each other and, at the PM, also to nucleocapsid (NC) structures under the membrane. These interactions drive the budding of new virus particles from the cell surface. The virus enters new cells by a low-pH-induced membrane fusion event where both inter- and intraheterodimer interactions are reorganized to establish a fusion-active membrane protein complex. There are no intact heterodimers left after fusion activation; instead, an E1 homotrimer remains in the cellul

SUBMITTER: Sjoberg M 

PROVIDER: S-EPMC149539 | biostudies-literature | 2003 Mar

REPOSITORIES: biostudies-literature