Open AccessStructure and Replication of Echovirus Type 12
Author(s) -
ROSENWIRTH Brigitte,
EGGERS Hans J.
Publication year - 1978
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1978.tb12723.x
Subject(s) - echovirus , cleavage (geology) , poliovirus , protein biosynthesis , biology , viral replication , polyacrylamide gel electrophoresis , rna , virus , nucleic acid , gel electrophoresis , microbiology and biotechnology , virology , viral protein , chemistry , biochemistry , enterovirus , gene , paleontology , enzyme , fracture (geology)
A technique as been devised which allows us to label predominantly echovirus‐12‐specific proteins: upon infection in the presence of d ‐(−)‐2‐(α‐hydroxybenzyl)benzimidazole plus actinomycin D the shut‐off of host‐cell protein synthesis takes place as in infected, untreated cells, but the bulk of viral protein synthesis is inhibited. Upon removal of 2‐(α‐hydroxybenzyl)benzimidazole a peak of viral protein synthesis is visible 3 h later. The time course of appearance of viral proteins is followed by dodecyl sulfate/polyacrylamide gel electrophoresis of the proteins which had been pulse‐labeled at different times post‐infection. The protein patterns induced in the infected cells by echovirus 12 and poliovirus 2 are compared; though they are different, some analogies are observed. The molecular weights of the polypeptides are determined. In the presence of amino acid analogs cleavage of viral proteins is impaired. A group of large proteins up to M r 220 000 is detectable in the infected cell which ordinarily is not observed. The 220 000‐ M r protein may represent the translation product of the total viral RNA. The hierarchy of the virus‐specific proteins originating from post‐translational cleavage is discussed.