Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins

摘要: The release of enveloped viruses from infected cells often requires a virally encoded activity, termed late-budding domain (L domain), by essential PTAP, PPXY, or YPDL sequence motifs. PTAP-type L domains recruit one three endosomal sorting complexes required for transport (ESCRT-I). However, subsequent events in viral budding are poorly defined, and neither nor PPXY-type require ESCRT-I. Here, we show that ESCRT-I other class E vacuolar protein (VPS) factors linked complex series protein–protein interactions. In particular, interactions between ESCRT-III bridged AIP-1/ALIX, mammalian orthologue the yeast VPS factor, Bro1. Expression certain components as fusion proteins induces late defect afflicts all L-domain types, suggesting integrity is general manner. Notably, prototype YPDL-type equine infectious anemia virus (EIAV) acts recruiting AIP-1/ALIX expression truncated form small interfering RNA-induced depletion specifically inhibits EIAV function. Overall, these findings indicate subvert subset to mediate budding, some which each whereas others apparently act adaptors physically link specific types machinery.