Herpes simplex virus 2 UL13 protein kinase disrupts nuclear lamins

Journal Article · Tue Sep 15 04:00:00 EDT 2009 · Virology

DOI:https://doi.org/10.1016/j.virol.2009.06.051· OSTI ID:21357540

Cano-Monreal, Gina L; Wylie, Kristine M; Cao, Feng; Tavis, John E ^[1]

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1. Department of Molecular Microbiology and Immunology, Saint Louis University School of Medicine, 1100 South Grand Blvd., St. Louis, MO 63104 (United States)

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.

• OSTI ID: 21357540
• Journal Information: Virology, Journal Name: Virology Journal Issue: 1 Vol. 392; ISSN VIRLAX; ISSN 0042-6822
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
AMINO ACIDS
CARBOXYLIC ACIDS
CHEMICAL REACTIONS
CONFORMATIONAL CHANGES
DISEASES
HERPES SIMPLEX
HYDROXY ACIDS
INFECTIOUS DISEASES
MEMBRANES
MICROORGANISMS
ORGANIC ACIDS
ORGANIC COMPOUNDS
PARASITES
PHOSPHORYLATION
PROTEINS
SERINE
SKIN DISEASES
THREONINE
VIRAL DISEASES
VIRUSES