Human proteins that add or remove the methyladenosine modification of cellular RNA, or recognize methylated RNA significantly affect HIV-1 infection or viral protein synthesis in cells, suggesting an important role for HIV-1 RNA methylation in regulating viral replication.

Angiomotin (AMOT) is a cellular host factor that links HIV-1 to the ubiquitin E3 ligase, NEDD4L, and promotes virion assembly and envelopment.

Folding and unfolding of a 6-helix bundle controls HIV assembly and maturation.

Unbiased molecular dynamics simulations reveal the insertion mechanism of the lipidated tail of the matrix domain of HIV-1 Gag into realistic membrane models and show its effect on lipid sorting.

While HIV-1 Gag protein binds tightly to several RNAs, it binds to the viral RNA 'packaging signal' with higher specificity than to control RNAs.

PI(4,5)P2 plays a much broader role during the HIV-1 particle assembly process than assumed; it is indispensable not only for recruitment of Gag to the plasma membrane but also for the maintenance of Gag assemblies.

The formation of HIV-1 particles requires a bending of the membrane that cannot be achieved by the Gag protein alone and thus there is need for the I-BAR protein IRSp53 to aid in the formation of HIV-1 buds.

During viral assembly, ESCRTIII and VPS4 are recruited after most of the HIV-1 membrane is bent but disappear prior to scission of the virion from the cell.

HIV escapes human immune pressure through a single mutation in V2 domain of envelope protein leading to emergence of mutant-specific broadly reactive antibodies, a phenomenon recapitulated in combinatorial vaccine design.

In vitro reconstitution shows how HIV-1 Gag assemblies on membranes can package the RNA genome in the presence of a vast excess of competing cellular RNAs, and that selectivity and immature lattice assembly are deeply intertwined with one another.