Structural and biophysical studies help to follow the disassembly of the HIV-1 capsid in vitro, and reveal the role of a small molecule called IP6 in regulating capsid stability.

An early start to long-term antiretroviral therapy limits the size of the HIV-1 reservoir more effectively than treatment that starts later.

High-resolution structures of HIV-1 RT in complex with two newly developed non-nucleoside inhibitors explain how they retain antiviral activities against drug-resistant RT mutants with considerably reduced susceptibility to rilpivirine.

Whole genome deep sequencing of many longitudinally sampled HIV-1 populations reveals that reversions towards ancestral HIV-1 genome sequences occur throughout the course of infection.

Disassembly of the HIV-1 capsid is a catastrophic process, whereby initiation and propagation can be controlled independently by molecules that bind to different features of the capsid lattice.

Combined tissue clearing, 3D-immunofluorescence, and electron tomography spatially revealed the dynamics of early HIV-1 spread within lymphoid tissues of humanized mice at the resolution of single cells and individual virions.

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.

Lymph node gp120 specific B cells extract locally injected HIV-1 gp120 from SIGN-R1 positive macrophages that line the subcapsular sinus overlying the lymph node interfollicular channels.

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.

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.