Abstract:
:As a subunit of both the P-L polymerase complex and the P-N assembly complex, the vesicular stomatitis virus (VSV) P protein plays a pivotal role in transcription and replication of the viral genome. Constitutive phosphorylation of this protein is currently thought to be essential for formation of the P-L complex. We recently identified the three relevant phosphate acceptor sites in the VSV Indiana serotype P protein (R. L. Jackson, D. Spadafora, and J. Perrault, Virology 214:189-197, 1995). We now report the effects of substituting Ala at these acceptor sites on transcription reconstitution in vitro and replication of defective interfering virus (DI) templates in vivo. The singly substituted S60A, T62A, and S64A mutants and the doubly substituted S60A/T62A and T62A/S64A mutants, all of which retain some constitutive phosphorylation, were nearly as active as the wild type in both assays. Surprisingly, the nonphosphorylated S60A/S64A protein was also active in transcription (> or = 28%)) and replication (> or = 50%) under optimal conditions. However, this mutant was much less active in in vitro transcription (< or = 5% of wild type) at low P concentrations (<27 nM). In addition, S60A/S64A required higher concentrations of L protein than did the wild type for optimal DI replication in vivo. DI replication efficiency and intracellular accumulation of L, P, and N proteins in the transfected system were very similar to those in VSV-infected cells. We conclude that P protein constitutive phosphorylation is not essential for VSV RNA synthesis per se but likely plays an important role in vivo in facilitating P multimerization and possibly P-L complex formation.
journal_name
J Viroljournal_title
Journal of virologyauthors
Spadafora D,Canter DM,Jackson RL,Perrault Jdoi
10.1128/JVI.70.7.4538-4548.1996subject
Has Abstractpub_date
1996-07-01 00:00:00pages
4538-48issue
7eissn
0022-538Xissn
1098-5514journal_volume
70pub_type
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