Enveloped viruses escape infected cells by budding through limiting membranes. In the
decade since the discovery that HIV recruits cellular ESCRT (endosomal sorting complexes …

The Gag proteins of HIV-1, like those of other retroviruses, are necessary and sufficient for
the assembly of virus-like particles. The roles played by HIV-1 Gag proteins during the life …

Like other enveloped viruses, HIV-1 uses cellular machinery to bud from infected cells. We
now show that Tsg101 protein, which functions in vacuolar protein sorting (Vps), is required …

HIV-1 and other retroviruses exit infected cells by budding from the plasma membrane, a
process requiring membrane fission. The primary late assembly (L) domain in the p6 region …

Budding of enveloped viruses has been shown to be driven by interactions between a
nucleocapsid and a proteolipid membrane. By contrast, we here describe the assembly of …

Retroviral Gag proteins encode sequences, termed late domains, which facilitate the final
stages of particle budding from the plasma membrane. We report here that interactions …

Ubiquitination appears to be involved in virus particle release from infected cells. Free
ubiquitin (Ub), as well as Ub covalently bound to a small fraction of p6 Gag, is detected in …

▪ Abstract Human immunodeficiency virus (HIV) and other retroviruses acquire their
envelopes and spread infection by budding through the limiting membranes of producer …

VP40, the putative matrix protein of both Ebola and Marburg viruses, possesses a conserved
proline-rich motif (PY motif) at its N terminus. We demonstrate that the VP40 protein can …

Enveloped viruses mature by budding at cellular membranes. It has been generally thought
that this process is driven by interactions between the viral transmembrane proteins and the …