Adenovirus infection targets the cellular protein kinase CK2 and RNA-activated protein kinase (PKR) into viral inclusions of the cell nucleus

Microsc Res Tech. 2002 Mar 15;56(6):465-78. doi: 10.1002/jemt.10060.

Abstract

The effects of the adenovirus infection on the distribution of the cellular protein kinase CK2 and double-stranded RNA-activated protein kinase (PKR) were examined at the ultrastructural level. Immunogold labeling revealed the redistribution of CK2 subunits and PKR to morphologically distinct structures of the cell nucleus. The electron-clear amorphous structures, designated pIX nuclear bodies in our previous work (Rosa-Calatrava et al., 2001), contained CK2 alpha and PKR. The protein crystals, which result from the regular assembly of hexon, penton base, and fiber proteins [Boulanger et al. (1970) J Gen Virol 6:329-332], contained CK2 beta and PKR. Both viral structures were devoid of viral RNA, including the PKR-inhibitor VA1 RNA generated by the RNA polymerase III. Instead, VA1 RNA accumulated in PKR-free viral compact rings in which the viral RNA generated by the RNA polymerase II was excluded.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenoviruses, Human / genetics
  • Adenoviruses, Human / metabolism
  • Adenoviruses, Human / pathogenicity*
  • Casein Kinase II
  • Cell Nucleus / ultrastructure*
  • HeLa Cells / ultrastructure
  • HeLa Cells / virology
  • Humans
  • In Situ Hybridization
  • Inclusion Bodies, Viral / enzymology*
  • Microscopy, Electron
  • Protein Serine-Threonine Kinases / metabolism*
  • RNA, Double-Stranded / metabolism
  • RNA, Ribosomal / metabolism
  • RNA, Viral / metabolism
  • eIF-2 Kinase / metabolism*

Substances

  • RNA, Double-Stranded
  • RNA, Ribosomal
  • RNA, Viral
  • Casein Kinase II
  • Protein Serine-Threonine Kinases
  • eIF-2 Kinase