dissection of influenza a virus m1 protein ph-dependent oligomerization of n-terminal domain and dimerization of c-terminal domain解剖的甲型流感病毒m1蛋白ph-dependent齐聚的n端结构域和二聚的c端域.pdfVIP

Dissection of Influenza A Virus M1 Protein: pH- Dependent Oligomerization of N-Terminal Domain and Dimerization of C-Terminal Domain 1,2 3 1 3 1 4 1,2 Ke Zhang , Zhao Wang , Xiaoling Liu , Changcheng Yin , Zeshan Basit , Bin Xia *, Wenjun Liu * 1 Center for Molecular Virology, CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China, 2 Graduate University of Chinese Academy of Sciences, Beijing, China, 3 Department of Biophysics, Health Science Center, Peking University, Beijing, China, 4 Beijing Nuclear Magnetic Resonance Center, Peking University, Beijing, China Abstract Background: The matrix 1 (M1) protein of Influenza A virus plays many critical roles throughout the virus life cycle. The oligomerization of M1 is essential for the formation of the viral matrix layer during the assembly and budding process. Methodology/Principal Findings: In the present study, we report that M1 can oligomerize in vitro, and that the oligomerization is pH-dependent. The N-terminal domain of M1 alone exists as multiple-order oligomers at pH 7.4, and the C-terminal domain alone forms an exclusively stable dimer. As a result, intact M1 can display different forms of oligomers and dimer is the smallest oligomerization state, at neutral pH. At pH 5.0, oligomers of the N-terminal domain completely dissociate into monomers, while the C-terminal domain remains in dimeric form. As a result, oligomers of intact M1 dissociate into a stable dimer at acidic pH. Conclusions/Significance: Oligomerization of M1 involves both the N- and C-terminal domains. The N-terminal