Characterization of prototype foamy virus gag late assembly domain motifs and their role in particle egress and infectivity.

ABSTRACT: Foamy viruses (FV) are unusual among retroviruses since they require both Gag and Env structural proteins for particle egress. Recently significant progress has been made towards the mechanistic understanding of the viral release process, in particular that of retroviruses, and the viral domains and cellular pathways involved. However little is currently known about domains of FV structural proteins and cellular proteins engaged in this process. By mutational analysis of sequence motifs in prototype FV (PFV) Gag, bearing homology to known late assembly (L) domains, a PSAP motif with L domain function that was functionally interchangeable by heterologous L domains was identified. In contrast the inactivation of a PPPI motif had no significant influence on PFV particle release, although muta

SUBMITTER: Stange A 

PROVIDER: S-EPMC1082757 | biostudies-literature | 2005 May

REPOSITORIES: biostudies-literature