Open AccessTwo polar residues within C ‐terminal domain of M 1 are critical for the formation of influenza A Virions
Author(s) -
Zhang Ke,
Wang Zhao,
Fan GuiZhen,
Wang Juan,
Gao Shengyan,
Li Yun,
Sun Lei,
Yin ChangCheng,
Liu WenJun
Publication year - 2015
Publication title -
cellular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.542
H-Index - 138
eISSN - 1462-5822
pISSN - 1462-5814
DOI - 10.1111/cmi.12457
Subject(s) - biology , virus , viral matrix protein , mutant , serine , influenza a virus , morphogenesis , threonine , microbiology and biotechnology , c terminus , protein domain , biochemistry , amino acid , virology , gene , phosphorylation
Summary The matrix protein 1 ( M 1) is the most abundant structural protein in influenza A virus particles. It oligomerizes to form the matrix layer under the lipid membrane, sustaining stabilization of the morphology of the virion. The present study indicates that M 1 forms oligomers based on a fourfold symmetrical oligomerization pattern. Further analysis revealed that the oligomerization pattern of M 1 was controlled by a highly conserved region within the C ‐terminal domain. Two polar residues of this region, serine‐183 ( S 183) and threonine‐185 ( T 185), were identified to be critical for the oligomerization pattern of M 1. M 1 point mutants suggest that single S183A or T185A substitution could result in the production of morphologically filamentous particles, while double substitutions, M1 ‐ S183A / T185A , totally disrupted the fourfold symmetry and resulted in the failure of virus production. These data indicate that the polar groups in these residues are essential to control the oligomerization pattern of M 1. Thus, the present study will aid in determining the mechanisms of influenza A virus matrix layer formation during virus morphogenesis.