Herpesvirus membrane fusion - a team effort.

07:00 EST 11th January 2020 | BioPortfolio

Summary of "Herpesvirus membrane fusion - a team effort."

One of the essential steps in every viral 'life' cycle is entry into the host cell. Membrane-enveloped viruses carry dedicated proteins to catalyse the fusion of the viral and cellular membrane. Herpesviruses feature a set of essential, structurally diverse glycoproteins on the viral surface that form a multicomponent fusion machinery, necessary for the entry mechanism. For Herpes simplex virus 1, these essential glycoproteins are gD, gH, gL and gB. In this review we describe the functions of the individual components, the potential interactions between them as well as the influence of post-translational modifications on the fusion mechanism.


Journal Details

This article was published in the following journal.

Name: Current opinion in structural biology
ISSN: 1879-033X
Pages: 112-120


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A superfamily of small proteins which are involved in the MEMBRANE FUSION events, intracellular protein trafficking and secretory processes. They share a homologous SNARE motif. The SNARE proteins are divided into subfamilies: QA-SNARES; QB-SNARES; QC-SNARES; and R-SNARES. The formation of a SNARE complex (composed of one each of the four different types SNARE domains (Qa, Qb, Qc, and R)) mediates MEMBRANE FUSION. Following membrane fusion SNARE complexes are dissociated by the NSFs (N-ETHYLMALEIMIDE-SENSITIVE FACTORS), in conjunction with SOLUBLE NSF ATTACHMENT PROTEIN, i.e., SNAPs (no relation to SNAP 25.)

Proteins that catalyze MEMBRANE FUSION.

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A member of the vesicle-associated membrane protein family involved in the MEMBRANE FUSION of TRANSPORT VESICLES to their target membrane.

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