Allosteric mechanism of membrane fusion activation in a herpesvirus.

ABSTRACT: Herpesviridae infect nearly all humans for life, causing diseases that range from painful to life-threatening¹. These viruses penetrate cells by employing a complex apparatus composed of separate receptor-binding, signal-transmitting, and membrane-fusing components². But how these components coordinate their functions is unknown. Here, we determined the 4.19-angstrom cryoEM reconstruction of the central signal-transmitting component from herpes simplex virus 2, the gH/gL complex, in its elusive pre-activation state. Analysis of the continuum of conformational ensembles observed in cryoEM data revealed a series of structural rearrangements in gH/gL that allosterically transmit the fusion-triggering signal from the receptor-binding glycoprotein gD to the membrane

SUBMITTER: Gonzalez-Del Pino GL 

PROVIDER: S-EPMC11430019 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature