Visualization of HIV-1 fusion by trapping the prehairpin intermediate.

HIV-1 capsids enter the host cell nucleus, where they are partially disrupted to release the viral genome upon completion of reverse transcription.

TRIM28 was found to be a versatile dual-function latency contributor by bridging both suppressive epigenetic modifications and RNAP II transcriptional-pausing, and can be a novel target to develop latency-reversing agents.

Interaction of HIV capsids with the cellular protein cleavage-and-polyadenylation factor 6 at the inner side of nuclear pores promotes nuclear entry of the viral replication complex in primary human macrophages.

A bnAb derived from a case of HIV superinfection has distinct qualities from other HIV-specific bnAbs, including framework residues that contribute to neutralization breadth and a unique viral escape profile.

HIV vaccine-induced binding and neutralizing antibody epitope specificities were mapped at high resolution directly from polyclonal sera, overcoming shortcomings in traditional serum mapping approaches and enabling highly detailed vaccine design.

A robust method to quantitatively visualize HIV-1 replication complexes in infected cells shows that these complexes remain associated with the viral capsid beyond nuclear import in primary macrophages.

CLR01 is a small molecule that could be an effective topical microbicide to eliminate HIV (and other enveloped viruses), and to antagonize host-encoded amyloid fibrils that promote HIV infection.

New HIV-1 protease inhibitor designs result in more potent inhibitors with high genetic barriers to resistance and the ability to lead virus evolution down less fit pathways when resistance occurs.

By inhibiting the activation of NF-κB, HIV-1 Vpu exerts much broader immunosuppressive effects than previously anticipated and may be an important determinant of chronic inflammation in HIV-1 infected individuals.