Nuclear trafficking of the human cytomegalovirus pp71 (ppUL82) tegument protein

Journal Article · Fri Jun 20 04:00:00 EDT 2008 · Virology

DOI:https://doi.org/10.1016/j.virol.2008.03.007· OSTI ID:21141001

Weiping, Shen; Westgard, Elizabeth; Liqun, Huang; Ward, Michael D; Osborn, Jodi L; Chau, Nha H; Collins, Lindsay; Marcum, Benjamin; Koach, Margaret A; Bibbs, Jennifer; Semmes, O John ^[1]

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1. Department of Microbiology and Molecular Cell Biology, Eastern Virginia Medical School, Norfolk, VA 23507 (United States)

The human cytomegalovirus tegument protein pp71 localizes to the nucleus immediately upon infection, and functions to initiate viral gene expression. Analysis of a series of random insertion mutations revealed that sequences within the mid region (MR) of pp71 are important for localization to the nucleus. Fusion of MR sequences with eGFP revealed that amino acids 94 to 300 were sufficient to target proteins to the nucleus. Random substitution mutagenesis within this domain resulted in two double substitution mutants, pp71P203T/T223M and pp71T228M/L275Q, with a predominantly cytoplasmic localization. Disruption of nuclear targeting resulted in relocalization of the fusion proteins to a distinct perinuclear region. Using tandem mass spectrometry, we determined that threonine 223 can be phosphorylated. Mutation of this residue to a phosphomimetic amino acid resulted in abrogation of nuclear targeting. These results strongly suggest that the intracellular trafficking of pp71 is regulated by phosphorylation.

• OSTI ID: 21141001
• Journal Information: Virology, Journal Name: Virology Journal Issue: 1 Vol. 376; ISSN VIRLAX; ISSN 0042-6822
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
GENES
MASS SPECTROSCOPY
MUTAGENESIS
MUTANTS
MUTATIONS
PHOSPHORYLATION
PROTEINS
RANDOMNESS
THREONINE