Abstract:
BACKGROUND:The N-heptad repeat region of the HIV-1 Transmembrane Envelope protein is a trimerization domain that forms part of a "six helix bundle" crucial to Envelope-mediated membrane fusion. N-heptad repeat peptides have been used as extracellular reagents to inhibit virus fusion. RESULTS:When expressed intracellularly with wild-type HIV-1 Envelope protein, the N-heptad repeat domain efficiently hetero-oligomerized with Envelope and trapped it in the endoplasmic reticulum or early Golgi, as indicated by lack of transport to the cell surface, absent proteolytic processing, and aberrant glycosylation. CONCLUSION:Post-translational processing of HIV Envelope is very sensitive to an agent that binds to the N-heptad repeat during synthesis, suggesting that it might be possible to modify drugs that bind to this region to have transport-blocking properties.
journal_name
Retrovirologyjournal_title
Retrovirologyauthors
Ou W,Silver Jdoi
10.1186/1742-4690-2-51subject
Has Abstractpub_date
2005-08-10 00:00:00pages
51issn
1742-4690pii
1742-4690-2-51journal_volume
2pub_type
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