Biochemical and cell-based analyses reveal how a non-enveloped virus exploits the chaperone activity of an ER transmembrane protein to penetrate the ER membrane required for successful virus infection.

Quasi-enveloped hepatitis A virions undergo clathrin-mediated endocytosis, followed by ALIX-dependent trafficking to lysosomes where the quasi-envelope is degraded, triggering uncoating of the RNA genome in association with lysosomal membrane rupture.

The high-resolution structure of a filamentous flexible plant virus shows that there is structural homology between its coat protein and the nucleoproteins of an unrelated group of enveloped RNA animal viruses.

A novel membrane, formed by a monolayer of lipids in a U-shaped conformation, envelops a virus that can withstand extremes of temperature and acidity.

The mechanism triggering HBV membrane fusion involves ERp57, a cellular protein disulfide isomerase, and ultimately leads to the exposition of a fusion peptide that was identified in the pre-S1 determinant.

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

Viruses, including SARS-CoV-2, retain infectivity longer at low temperatures and extreme relative humidities because these conditions slow down the chemical reactions that inactivate those viruses.

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.

A disease-associated polymorphism in a related protein that regulates neurotransmitter release reveals that antiviral protein IFITM3 forms oligomers to rigidify membranes and inhibit virus fusion with cells.

The mechanism of membrane-fusion catalysis in influenza viral infection of target cells is robust against the presence of a large fraction of non-productive viral fusion proteins.