Herpes simplex virus 2 UL13 protein kinase disrupts nuclear lamins

Gina L. Cano-Monreal, Kristine M. Wylie, Feng Cao, John E. Tavis, Lynda A. Morrison

Research output: Contribution to journalArticlepeer-review

48 Scopus citations

Abstract

Herpesviruses must cross the inner nuclear membrane and underlying lamina to exit the nucleus. HSV-1 US3 and PKC can phosphorylate lamins and induce their dispersion but do not elicit all of the phosphorylated lamin species produced during infection. UL13 is a serine threonine protein kinase conserved among many herpesviruses. HSV-1 UL13 phosphorylates US3 and thereby controls UL31 and UL34 nuclear rim localization, indicating a role in nuclear egress. Here, we report that HSV-2 UL13 alone induced conformational changes in lamins A and C and redistributed lamin B1 from the nuclear rim to intranuclear granular structures. HSV-2 UL13 directly phosphorylated lamins A, C, and B1 in vitro, and the lamin A1 tail domain. HSV-2 infection recapitulated the lamin alterations seen upon expression of UL13 alone, and other alterations were also observed, indicating that additional viral and/or cellular proteins cooperate with UL13 to alter lamins during HSV-2 infection to allow nuclear egress.

Original languageEnglish
Pages (from-to)137-147
Number of pages11
JournalVirology
Volume392
Issue number1
DOIs
StatePublished - Sep 15 2009

Keywords

  • Egress
  • HSV-2
  • Herpes simplex virus
  • Lamin
  • Nuclear
  • Phosphorylation
  • UL13

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