Function of the Herpes Simplex Virus 1 Small Capsid Protein VP26 Is Regulated by Phosphorylation at a Specific Site
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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 functionin vitroandin vivo.
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2006 ◽
Vol 80
(3)
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pp. 1110-1120
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2005 ◽
Vol 79
(6)
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pp. 3797-3806
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2009 ◽
Vol 22
(1)
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pp. 145-151