Open AccessPeptide Inhibitors of HIV-1 Egress
Author(s) -
Abdül Waheed,
Eric O. Freed
Publication year - 2008
Publication title -
acs chemical biology
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 1.899
H-Index - 111
eISSN - 1554-8937
pISSN - 1554-8929
DOI - 10.1021/cb800296j
Subject(s) - tsg101 , escrt , endosome , microbiology and biotechnology , peptide , human immunodeficiency virus (hiv) , group specific antigen , chemistry , plasma protein binding , biology , computational biology , biophysics , biochemistry , virology , intracellular , microvesicles , gene , microrna
HIV-1 release requires a direct interaction between the p6 domain of the Gag protein and Tsg101, a component of the cellular endosomal sorting complex required for transport I (ESCRT-I). Disruption of the binding between Gag and Tsg101 is highly detrimental to particle release, making this viral-host cell interaction a potential target for the development of novel anti-HIV-1 agents. An article in this issue reports on the application of a bacterial reverse two-hybrid strategy to identify a cyclic peptide that disrupts Gag-Tsg101 binding and suppresses HIV-1 particle release.