Disruption of Herpes Simplex Virus Type 2 pUL21 Phosphorylation Impairs Secondary Envelopment of Cytoplasmic Nucleocapsids
Renée L. Finnen,
Jamil H. Muradov,
Valerie Le Sage
et al.
Abstract:The multifunctional tegument protein pUL21 of HSV-2 is phosphorylated in infected cells. We have identified two residues in the unstructured linker region of pUL21, serine 251 and serine 253, as sites of phosphorylation. Both phosphorylation sites are absent in HSV-1 pUL21, which likely explains why phosphorylated pUL21 was not detected in cells infected with HSV-1. Cells infected with HSV-2 strain 186 viruses deficient in pUL21 phosphorylation exhibited reductions in both cell-cell spread of virus infection a… Show more
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