A highly conserved amino acid in VP1 regulates maturation of enterovirus 71

• DOI: 10.1371/journal.ppat.1006625
• Publication Date: 2017-09-22T17:38:02Z
• Authors: Yong-Xin Zhang; Yu-Ming Huang; Quan-Jie Li; Xiao-Yu Li; Yong-Dong Zhou; Fei Guo; Jin-Ming Zhou; Shan Cen
• Keywords: Enterovirus 71; Picornavirus; Infectivity; Viral protein

Enterovirus 71 (EV71) is the major causative agent of hand, foot and mouth disease (HFMD) in children, causing severe clinical outcomes even death. Here, we report an important role highly conserved alanine residue at position 107 capsid protein VP1 (VP1A107) efficient replication EV71. Substitutional mutations VP1A107 significantly diminish viral growth kinetics without significant effect on entry, expression genes production. The results mechanistic studies reveal that regulates cleavage VP0 precursor during EV71 assembly, which required, next round infection, for transformation mature virion (160S) into intermediate or A-particle (135S), a key step virus uncoating. Furthermore, molecular dynamic simulations hydrogen-bond networks analysis suggest flexibility BC loop region surrounding VP1107 directly correlates with infectivity. It possible sufficient favors conformational change required as well subsequent uncoating replication. Taken together, our data structural regulating maturation. Characterization this novel determinant virulence would promote study pathogenesis Enteroviruses.