Adenovirus infection targets the cellular protein kinase CK2 and RNA-activated protein kinase (PKR) into viral inclusions of the cell nucleus.
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.
Souquere-Besse
Sylvie
S
Institut André Lwoff, UPR 1983 CNRS, Villejuif, France.
Pichard
Evelyne
E
Filhol
Odile
O
Legrand
Valerie
V
Rosa-Calatrava
Manuel
M
Hovanessian
Ara G
AG
Cochet
Claude
C
Puvion-Dutilleul
Francine
F
D000260:Adenoviruses, Human / Q000235:genetics / Q000378:metabolism / Q000472:pathogenicity*; D047390:Casein Kinase II; D002467:Cell Nucleus / Q000648:ultrastructure*; D006367:HeLa Cells / Q000648:ultrastructure / Q000821:virology; D006801:Humans; D017403:In Situ Hybridization; D007181:Inclusion Bodies, Viral / Q000201:enzymology*; D008854:Microscopy, Electron; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D012330:RNA, Double-Stranded / Q000378:metabolism; D012335:RNA, Ribosomal / Q000378:metabolism; D012367:RNA, Viral / Q000378:metabolism; D019892:eIF-2 Kinase / Q000378:metabolism*
D012330:RNA, Double-Stranded; D012335:RNA, Ribosomal; D012367:RNA, Viral; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases; D019892:eIF-2 Kinase