Ebolavirus VP40 redux. Or rather, redox

Luca Zinzula

doi:10.1016/j.str.2023.08.010

Ebolavirus VP40 redux. Or rather, redox

Structure. 2023 Sep 7;31(9):1008-1010. doi: 10.1016/j.str.2023.08.010.

Author

Luca Zinzula¹

Affiliation

¹ iHuman Institute, ShanghaiTech University, Shanghai 201210, China. Electronic address: zinzulal@shanghaitech.edu.cn.

PMID: 37683615
DOI: 10.1016/j.str.2023.08.010

Abstract

The virion protein 40 (VP40) forms the viral matrix, mediates budding, and downregulates viral RNA synthesis in ebolaviruses. In this issue of Structure, Werner et al. present a structure of VP40 from Sudan ebolavirus with a previously unresolved disulfide bridge that enables regulation of VP40 functions via human thioredoxin.

MeSH terms

Cell Division
Disulfides
Ebolavirus* / genetics
Humans
Oxidation-Reduction
Virion

Substances

Disulfides