Structural analysis of conformational changes in the mpox virus A7 protein

Virol Sin. 2024 Apr;39(2):331-334. doi: 10.1016/j.virs.2023.12.006. Epub 2023 Dec 28.

Authors

Xincheng Ni¹, Kai Wang¹, Yinze Han¹, Jian Lei²

Affiliations

¹ National Clinical Research Center for Geriatrics, and State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University, Chengdu, 610041, China.
² National Clinical Research Center for Geriatrics, and State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University, Chengdu, 610041, China. Electronic address: leijian@scu.edu.cn.

Abstract

•
Phospholipid-binding abilities of mpox virus A7 protein and its truncations are investigated.
•
The structures of the N-terminal truncations of A7 protein (A7N₁₂₁ and A7N₁₃₇) are determined.
•
Conformational changes of the conserved linking helix in A7 are illustrated.
•
A structural model of the full-length A7 protein is proposed.

Publication types

Letter

MeSH terms

Models, Molecular
Parapoxvirus / chemistry
Parapoxvirus / genetics
Protein Conformation*
Viral Proteins / chemistry
Viral Proteins / genetics

Substances

Viral Proteins