单纯疱疹病毒1型小衣壳蛋白VP26的功能受特定位点磷酸化的调控。
Function of the Herpes Simplex Virus 1 Small Capsid Protein VP26 Is Regulated by Phosphorylation at a Specific Site.
作者信息
Kobayashi Ryosuke, Kato Akihisa, Oda Shinya, Koyanagi Naoto, Oyama Masaaki, Kozuka-Hata Hiroko, Arii Jun, Kawaguchi Yasushi
机构信息
Division of Molecular Virology, Department of Microbiology and Immunology, Institute of Medical Science, The University of Tokyo, Tokyo, Japan Department of Infectious Disease Control, International Research Center for Infectious Diseases, Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
Division of Molecular Virology, Department of Microbiology and Immunology, Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
出版信息
J Virol. 2015 Jun;89(11):6141-7. doi: 10.1128/JVI.00547-15. Epub 2015 Mar 25.
Abstract
Replacement of the herpes simplex virus 1 small capsid protein VP26 phosphorylation site Thr-111 with alanine reduced viral replication and neurovirulence to levels observed with the VP26 null mutation. This mutation reduced VP26 expression and mislocalized VP26 and its binding partner, the major capsid protein VP5, in the nucleus. VP5 mislocalization was also observed with the VP26 null mutation. Thus, we postulate that phosphorylation of VP26 at Thr-111 regulates VP26 function in vitro and in vivo.
摘要
将单纯疱疹病毒1型小衣壳蛋白VP26的苏氨酸-111磷酸化位点替换为丙氨酸，可使病毒复制和神经毒性降低至VP26无效突变时所观察到的水平。该突变降低了VP26的表达，并使VP26及其结合伴侣主要衣壳蛋白VP5在细胞核中定位错误。在VP26无效突变中也观察到VP5定位错误。因此，我们推测VP26在苏氨酸-111处的磷酸化在体外和体内调节VP26的功能。
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