Abstract
In recognition of the growing influence of cell biology in retrovirus research, we recently organized a Summer conference sponsored by the American Society for Cell Biology (ASCB) on the Cell Biology of HIV-1 and other Retroviruses (July 20–23, 2006, Emory University, Atlanta, Georgia). The meeting brought together a number of leading investigators interested in the interplay between cell biology and retrovirology with an emphasis on presentation of new and unpublished data. The conference was arranged from early to late events in the virus replication cycle, with sessions on viral fusion, entry, and transmission; post-entry restrictions to retroviral infection; nuclear import and integration; gene expression/regulation of retroviral Gag and genomic RNA; and assembly/release. In this review, we will attempt to touch briefly on some of the highlights of the conference, and will emphasize themes and trends that emerged at the meeting.Meeting reportThe conference began with a keynote address from W. Sundquist on the biochemistry of HIV-1 budding. This presentation will be described in the section on Assembly and Release of Retroviruses.
Highlights
Meeting report: The conference began with a keynote address from W
Eric Freed opened the meeting by introducing work from his laboratory that identified the cholesterol-binding agent amphotericin B methyl ester (AME) as a potential compound to block HIV-1 replication [1]
Another important mediator of viral entry was highlighted by Michel Tremblay whose work has historically focused on integral membrane-spanning intracellular adhesion molecules (ICAMs) that are incorporated within the envelopes of retroviruses
Summary
Bieniasz described a study that has taken advantage of our increased knowledge of post-entry restriction factors to engineer HIV-1 variants that are able to bypass blocks imposed on HIV-1 infection by non-human primate cells. Acetylation of C-terminal lysines (Lys264, 266 and 273) and conserved (in retroviruses) regions of IN were shown to be important for DNA association, IN strand transfer activity and possibly IN protein stability in HIV-1 infected cells.
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