Structural changes in human cytomegalovirus cytoplasmic assembly sites in the absence of UL97 kinase activity

Maysa Azzeh, Alik Honigman, Albert Taraboulos, Alexander Rouvinski, Dana G. Wolf*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

44 Scopus citations

Abstract

Studies of human cytomegalovirus (HCMV) UL97 kinase deletion mutant (ΔUL97) indicated a multi-step role for this kinase in early and late phases of the viral life cycle, namely, in DNA replication, capsid maturation and nuclear egress. Here, we addressed its possible involvement in cytoplasmic steps of HCMV assembly. Using the ΔUL97 and the UL97 kinase inhibitor NGIC-I, we demonstrate that the absence of UL97 kinase activity results in a modified subcellular distribution of the viral structural protein assembly sites, from compact structures impacting upon the nucleus to diffuse perinuclear structures punctuated by large vacuoles. Infection by either wild type or ΔUL97 viruses induced a profound reorganization of wheat germ agglutinin (WGA)-positive Golgi-related structures. Importantly, the viral-induced Golgi remodeling along with the reorganization of the nuclear architecture was substantially altered in the absence of UL97 kinase activity. These findings suggest that UL97 kinase activity might contribute to organization of the viral cytoplasmic assembly sites.

Original languageAmerican English
Pages (from-to)69-79
Number of pages11
JournalVirology
Volume354
Issue number1
DOIs
StatePublished - 10 Oct 2006

Bibliographical note

Funding Information:
Funding for this study was provided by the National Institute of Nursing Research (NR 030508) and the New York State Department of Health.

Keywords

  • Cytoplasmic assembly sites
  • Pp28
  • UL97 kinase

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