title: Cofilin-1 is involved in regulation of actin reorganization during influenza A virus assembly and budding.
abstract: Influenza A virus (IAV) assembly and budding on host cell surface plasma membrane requires actin cytoskeleton reorganization. The underlying molecular mechanism involving actin reorganization remains unclarified. In this study, we found that the natural antiviral compound petagalloyl glucose (PGG) inhibits F-actin reorganization in the host cell membrane during the late stage of IAV infection, which are associated with the suppression of total cofilin-1 level and its phosphorylation. Knock-down of cofilin-1 reduces viral yields. These findings provide the first evidence that cofilin-1 plays an important role in regulating actin reorganization during IAV assembly and budding.
authors.affiliation: Division of Molecular Pharmacology of Infectious Agents, Department of Molecular Microbiology and Immunology, Graduate School of Biomedical Sciences, Nagasaki University, 852-8521 Nagasaki, Japan.
authors.forename: Ge
authors.initials: G
authors.lastname: Liu
authors.affiliation: Guangzhou Jinan Biomedicine Research and Development Center, National Engineering Research Center of Genetic Medicine, Jinan University, Guangzhou 510632, Guangdong, China.
authors.forename: Yangfei
authors.initials: Y
authors.lastname: Xiang
authors.affiliation: Division of Molecular Pharmacology of Infectious Agents, Department of Molecular Microbiology and Immunology, Graduate School of Biomedical Sciences, Nagasaki University, 852-8521 Nagasaki, Japan.
authors.forename: Chaowan
authors.initials: C
authors.lastname: Guo
authors.affiliation: Guangzhou Jinan Biomedicine Research and Development Center, National Engineering Research Center of Genetic Medicine, Jinan University, Guangzhou 510632, Guangdong, China.
authors.forename: Ying
authors.initials: Y
authors.lastname: Pei
authors.affiliation: Guangzhou Jinan Biomedicine Research and Development Center, National Engineering Research Center of Genetic Medicine, Jinan University, Guangzhou 510632, Guangdong, China. Electronic address: twang-yf@163.com.
authors.forename: Yifei
authors.initials: Y
authors.lastname: Wang
authors.affiliation: Division of Molecular Pharmacology of Infectious Agents, Department of Molecular Microbiology and Immunology, Graduate School of Biomedical Sciences, Nagasaki University, 852-8521 Nagasaki, Japan. Electronic address: kkholi@nagasaki-u.ac.jp.
authors.forename: Kaio
authors.initials: K
authors.lastname: Kitazato
mesh_terms: D000199:Actins / Q000378:metabolism*; D051338:Cofilin 1 / Q000378:metabolism*; D015967:Gene Expression Regulation, Viral / Q000502:physiology; D009980:Influenza A virus / Q000254:growth & development* / Q000302:isolation & purification / Q000648:ultrastructure*; D014764:Viral Proteins / Q000378:metabolism*; D019065:Virus Assembly / Q000502:physiology*; D057074:Virus Release / Q000502:physiology*
chemical_list: D000199:Actins; D051338:Cofilin 1; D014764:Viral Proteins
keywords: Cofilin-1; F-actin; Influenza A virus; Pentagalloyl glucose; Viral assembly; Viral budding