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.
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