Crystal structure of the Měnglà virus VP30 C-terminal domain

• Published in: Biochemical and biophysical research communications Vol. 525; no. 2; pp. 392 - 397
• Main Authors: Dong, Shishang, Wen, Kangning, Chu, Hongguan, Li, Hui, Yu, Qianqian, Wang, Changhui, Qin, Xiaochun
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 30.04.2020
• Subjects: Crystal structure; MLAV; Structural homologs; VP30 CTD; MLAV; VP30 CTD; Structural homologs; Crystal structure
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2020.02.089

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. •Měnglà virus VP30 C-terminal domain (MLAV VP30 CTD) structure in Filoviridae family was determined by X-ray.•The C-terminal helix-7 (H7) of MLAV VP30 CTD is verified critical for the dimerization process.•A preliminary model for investigation of MLAV VP30 CTD as an anti-filovirus drug development target was provided.