title: The phosphorylation of Ser221 in VP2 of mink enteritis virus and its roles in virus amplification.
abstract: Recent reports have indicated that phosphorylation of capsid proteins plays an important role in virion assemblage. Autonomous parvoviruses are among the smallest known viruses with an ssDNA genome enclosed within an icosahedral capsid. Here, we demonstrate that a structural protein (VP2) of one member, mink enteritis virus (MEV), is phosphorylated at serine-221 (Ser221) in vivo. Mutant viruses containing an S221A non-phosphorylatable alanine substitution, or an S221E glutamic acid substitution to mimic serine phosphorylation, were able to express VP2 but had either limited ability or were unable to propagate in feline F81 cells. We propose a new mechanism whereby VP2 phosphorylation plays an essential role in amplification during MEV infection.
authors.affiliation: State Key Laboratory of Agrobiotechnology, Department of Biochemistry and Molecular Biology, College of Biological Sciences, China Agricultural University, Beijing 100193, PR China.
authors.forename: Qiang
authors.initials: Q
authors.lastname: Hou
authors.affiliation: State Key Laboratory of Agrobiotechnology, Department of Biochemistry and Molecular Biology, College of Biological Sciences, China Agricultural University, Beijing 100193, PR China.
authors.forename: Jun
authors.initials: J
authors.lastname: Su
authors.affiliation: State Key Laboratory of Agrobiotechnology, Department of Biochemistry and Molecular Biology, College of Biological Sciences, China Agricultural University, Beijing 100193, PR China.
authors.forename: Jigui
authors.initials: J
authors.lastname: Wang
authors.affiliation: State Key Laboratory of Agrobiotechnology, Department of Biochemistry and Molecular Biology, College of Biological Sciences, China Agricultural University, Beijing 100193, PR China.
authors.forename: Zhili
authors.initials: Z
authors.lastname: Li
authors.affiliation: State Key Laboratory of Agrobiotechnology, Department of Biochemistry and Molecular Biology, College of Biological Sciences, China Agricultural University, Beijing 100193, PR China.
authors.forename: Yaping
authors.initials: Y
authors.lastname: Mao
authors.affiliation: State Key Laboratory of Agrobiotechnology, Department of Biochemistry and Molecular Biology, College of Biological Sciences, China Agricultural University, Beijing 100193, PR China.
authors.forename: Shuang
authors.initials: S
authors.lastname: Wang
authors.affiliation: State Key Laboratory of Agrobiotechnology, Department of Biochemistry and Molecular Biology, College of Biological Sciences, China Agricultural University, Beijing 100193, PR China.
authors.forename: Ji
authors.initials: J
authors.lastname: Xi
authors.affiliation: State Key Laboratory of Agrobiotechnology, Department of Biochemistry and Molecular Biology, College of Biological Sciences, China Agricultural University, Beijing 100193, PR China. Electronic address: weiquan8@cau.edu.cn.
authors.forename: Weiquan
authors.initials: W
authors.lastname: Liu
mesh_terms: D000818:Animals; D002415:Cats; D002460:Cell Line; D053490:Mink enteritis virus / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D010766:Phosphorylation; D012694:Serine / Q000378:metabolism*; D015678:Viral Structural Proteins / Q000235:genetics / Q000378:metabolism*; D014776:Virus Cultivation; D014779:Virus Replication
chemical_list: D015678:Viral Structural Proteins; D012694:Serine
keywords: Mass spectrometry; Mink enteritis virus; Mutation; Phosphorylation; VP2