Two polar residues within C-terminal domain of M1 are critical for the formation of influenza A Virions.
The matrix protein 1 (M1) 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 M1 forms oligomers based on a fourfold symmetrical oligomerization pattern. Further analysis revealed that the oligomerization pattern of M1 was controlled by a highly conserved region within the C-terminal domain. Two polar residues of this region, serine-183 (S183) and threonine-185 (T185), were identified to be critical for the oligomerization pattern of M1. M1 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 M1. Thus, the present study will aid in determining the mechanisms of influenza A virus matrix layer formation during virus morphogenesis.
Center for Molecular Virology, CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Ke
K
Zhang
Department of Biophysics, Health Science Center, Peking University, Beijing, 100191, China.|National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, 77030, USA.
Zhao
Z
Wang
Department of Biophysics, Health Science Center, Peking University, Beijing, 100191, China.
Gui-Zhen
GZ
Fan
Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX, 75390, USA.
Juan
J
Wang
Center for Molecular Virology, CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Shengyan
S
Gao
Center for Molecular Virology, CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Yun
Y
Li
Center for Molecular Virology, CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Lei
L
Sun
Department of Biophysics, Health Science Center, Peking University, Beijing, 100191, China.
Chang-Cheng
CC
Yin
Center for Molecular Virology, CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.|Center for Influenza Research and Early-warning, Chinese Academy of Sciences, Beijing, 100101, China.
Wen-Jun
WJ
Liu
D000596:Amino Acids / Q000235:genetics; D000818:Animals; D002460:Cell Line; D004252:DNA Mutational Analysis; D004285:Dogs; D006801:Humans; D009980:Influenza A virus / Q000235:genetics / Q000502:physiology*; D017354:Point Mutation; D055503:Protein Multimerization; D014763:Viral Matrix Proteins / Q000235:genetics / Q000378:metabolism*; D014771:Virion / Q000378:metabolism*; D019065:Virus Assembly
D000596:Amino Acids; C488936:M1 protein, Influenza A virus; D014763:Viral Matrix Proteins