Crystal structure of the Měnglà virus VP30 C-terminal domain

Shishang Dong; Kangning Wen; Hongguan Chu; Hui Li; Qianqian Yu; Changhui Wang; Xiaochun Qin

doi:10.1016/j.bbrc.2020.02.089

Crystal structure of the Měnglà virus VP30 C-terminal domain

Biochem Biophys Res Commun. 2020 Apr 30;525(2):392-397. doi: 10.1016/j.bbrc.2020.02.089. Epub 2020 Feb 22.

Authors

Shishang Dong¹, Kangning Wen², Hongguan Chu², Hui Li², Qianqian Yu², Changhui Wang², Xiaochun Qin³

Affiliations

¹ School of Biological Science and Technology, University of Jinan, Jinan, China. Electronic address: bio_dongss@ujn.edu.cn.
² School of Biological Science and Technology, University of Jinan, Jinan, China.
³ School of Biological Science and Technology, University of Jinan, Jinan, China. Electronic address: bio_qinxc@ujn.edu.cn.

PMID: 32093889
DOI: 10.1016/j.bbrc.2020.02.089

Abstract

The family Filoviridae contains many important human viruses, including Marburg virus (MARV) and Ebola virus (EBOV). Měnglà virus (MLAV), a newly discovered filovirus, is considered a potential human pathogen. The VP30 C-terminal domain (CTD) of these filoviruses plays an essential role in virion assembly. In common with other filoviruses, MLAV VP30 CTD mainly exists as a dimer in solution. In this work, we determined the crystal structure of recombinant MLAV VP30 CTD monomer, verifying that C-terminal helix-7 (H7) is critical for the dimerization process. This study provides a preliminary model for investigation of MLAV VP30 CTD as an anti-filovirus drug development target.

Keywords: Crystal structure; MLAV; Structural homologs; VP30 CTD.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Crystallography, X-Ray
Drug Discovery
Filoviridae / chemistry*
Filoviridae Infections / virology*
Models, Molecular
Protein Conformation, alpha-Helical
Protein Domains
Protein Multimerization
Viral Proteins / chemistry*

Substances

Viral Proteins