The principal hydrogen donor for the herpes simplex virus type 1-encoded ribonucleotide reductase in infected cells is a cellular thioredoxin.
In this study herpes simplex virus type 1-encoded ribonucleotide reductase was shown to be able to utilize thioredoxin purified from the cyanobacterium Anabaena variabilis as a hydrogen donor for the enzyme. An assay has been developed to search for proteins which can function as a hydrogen donor for the viral ribonucleotide reductase. A protein has been identified and purified to homogeneity from infected cell extracts by a combination of fast protein liquid chromatography and gel filtration. This protein, which is also present in mock-infected cells, has been identified as a host cell thioredoxin by similarities in its physical characteristics with other thioredoxins. No evidence for the existence of a major virus-induced thioredoxin was obtained, suggesting that the host cell thioredoxin functions as the hydrogen donor for the herpes simplex virus type 1 ribonucleotide reductase in the infected cell.
Darling
A J
AJ
MRC Virology Unit, Institute of Virology, Glasgow, U.K.
D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D002460:Cell Line; D006224:Cricetinae; D000458:Cyanobacteria / Q000032:analysis; D005347:Fibroblasts / Q000378:metabolism; D007668:Kidney; D008647:Mesocricetus; D010084:Oxidation-Reduction; D012264:Ribonucleotide Reductases / Q000378:metabolism*; D018139:Simplexvirus / Q000201:enzymology*; D013879:Thioredoxins / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
D001426:Bacterial Proteins; D014764:Viral Proteins; D013879:Thioredoxins; D012264:Ribonucleotide Reductases