English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Benzhydrazone [BH; 1H-benz[f]indene-1,3(2H) -dionebis(amidinohydrazone)] significantly inhibits glycosylation of proteins, but only in cells infected with herpes simplex virus. We report on a herpes simplex virus type 1 (HSV-1) mutant resistant to BH. A syncytium-inducing mutant designated HSV-1(13)S11 was found to be biochemically resistant to BH in that [14C]glucosamine incorporation was not inhibited in infected HEp-2 cells exposed to the drug. Intertypic recombinants were obtained which showed that BH resistance is encoded in the DNA of the mutant virus and may be transferred into the genome of BH-sensitive HSV. In the recombinants the biochemical resistance marker segregated from the syncytial marker, suggesting that the two markers probably map in different loci. The BH-resistant mutant did not complement wild-type BH-sensitive HSV-1 and -2. Furthermore, resistance was apparent in HEp-2 but not in Vero cells. The paper discusses the hypothesis that inhibition of glycosylation of HSV proteins is the consequence of modification or selective transport of BH involving a HSV gene product.

Characterization of a herpes simplex virus type 1 mutant resistant to benzhydrazone, a selective inhibitor of herpesvirus glycosylation.