Unknown

Dataset Information

0

Herpesvirus gB: A Finely Tuned Fusion Machine.


ABSTRACT: Enveloped viruses employ a class of proteins known as fusogens to orchestrate the merger of their surrounding envelope and a target cell membrane. Most fusogens accomplish this task alone, by binding cellular receptors and subsequently catalyzing the membrane fusion process. Surprisingly, in herpesviruses, these functions are distributed among multiple proteins: the conserved fusogen gB, the conserved gH/gL heterodimer of poorly defined function, and various non-conserved receptor-binding proteins. We summarize what is currently known about gB from two closely related herpesviruses, HSV-1 and HSV-2, with emphasis on the structure of the largely uncharted membrane interacting regions of this fusogen. We propose that the unusual mechanism of herpesvirus fusion could be linked to the unique architecture of gB.

SUBMITTER: Cooper RS 

PROVIDER: S-EPMC4690880 | biostudies-literature | 2015 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Herpesvirus gB: A Finely Tuned Fusion Machine.

Cooper Rebecca S RS   Heldwein Ekaterina E EE  

Viruses 20151211 12


Enveloped viruses employ a class of proteins known as fusogens to orchestrate the merger of their surrounding envelope and a target cell membrane. Most fusogens accomplish this task alone, by binding cellular receptors and subsequently catalyzing the membrane fusion process. Surprisingly, in herpesviruses, these functions are distributed among multiple proteins: the conserved fusogen gB, the conserved gH/gL heterodimer of poorly defined function, and various non-conserved receptor-binding protei  ...[more]

Similar Datasets

| S-EPMC7005897 | biostudies-literature
| S-EPMC155071 | biostudies-literature
| S-EPMC10903058 | biostudies-literature
| S-EPMC6587158 | biostudies-literature
| S-EPMC9154744 | biostudies-literature
| S-EPMC7612436 | biostudies-literature
| S-EPMC5418064 | biostudies-literature
| S-EPMC3811602 | biostudies-literature
| S-EPMC11015636 | biostudies-literature
| S-EPMC10985590 | biostudies-literature