The α subunit of eucaryotic initiation factor 2 is phosphorylated in mengovirus-infected mouse L cells

J. DeStefano, E. Olmsted, R. Panniers, J. Lucas-Lenard

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

Infection of mouse L cells with mengovirus resulted in the activation of a protein kinase (PK) that selectively phosphorylated the small, 38,000-molecular-weight α subunit of eucaryotic initiation factor 2 (eIF-2) in vitro. The mengovirus-activated kinase was detected in vitro approximately 3 h after virus adsorption. The ratio of phosphorylated to unphosphorylated eIF-2 also increased in vivo between 3 and 7 h after adsorption. The virus-activated kinase fractionated with the ribosomal pellet and had a high affinity for DEAE-cellulose and Mono Q ion-exchange columns. Gel electrophoresis of the kinase activity eluting from the Mono Q column and silver staining of the gel revealed only one protein band with a molecular mass of 70 kilodaltons. The optimal assay conditions for the mengovirus-activated kinase paralleled those of the double-stranded RNA-activated PK (dsRNA-PK). Lysates from infected cells contained elements capable of activating partially purified dsRNA-PK. These elements were identified as double-stranded RNA by their sensitivity to double-stranded RNase. The phosphorylation of the α subunit of eIF-2 coincided with the synthesis of dsRNA in infected cells, suggesting that the mengovirus-activated kinase is the dsRNA-PK. The phosphorylation of the α subunit of eIF-2 correlated with the global inhibition of protein synthesis that occurs at late times after infection.

Original languageEnglish (US)
Pages (from-to)4445-4453
Number of pages9
JournalJournal of virology
Volume64
Issue number9
DOIs
StatePublished - 1990

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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