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Inhibition of glycosylation of bovine herpesvirus 1 glycoproteins by the thymidine analog (E)-5-(2 Bromovinyl)-2'-deoxyuridine.

Publication ,  Journal Article
Misra, V; Nelson, RC; Babiuk, LA
Published in: Antimicrob Agents Chemother
June 1983

(E)-5-(2-Bromovinyl)-2'-deoxyuridine (BVdU) was phosphorylated by the bovine herpesvirus 1 (BHV-1)-induced thymidine kinase and subsequently incorporated into viral DNA, resulting in DNA that was more dense than DNA from untreated cells. Incorporation of the drug did not result in the termination of replicating BHV-1 DNA molecules since radioactively labeled DNA synthesized in drug-treated and untreated cells sedimented at similar rates in alkaline sucrose gradients. No differences were observed in the electrophoretic mobility of [35S]methionine-labeled viral polypeptides synthesized in treated and untreated cells, although [3H]glucosamine-labeled viral glycoproteins synthesized in treated cells were of a lower molecular weight than those in untreated cells. In BVdU-treated cells, unlike untreated cells, immature neutral and basic precursors of the mature viral glycoproteins accumulated. Although BVdU-treated and untreated cells contained similar amounts of virus, very little virus was released into the culture supernatant from BVdU-treated cells. Our results suggest that BVdU partially inhibits the glycosylation of BHV-1 glycoproteins. BVdU-sensitive glycosylation, however, is not necessary for expression of these glycoproteins on the surface of infected cells since the glycoproteins could be labeled on intact cells with 125I and because BVdU-treated cells remained sensitive to antibody-dependent, cell-mediated cytotoxity mediated by anti-BHV-1 serum. The phosphorylation of BVdU was a prerequisite for its effect on glycosylation since the glycoproteins of a thymidine kinase-deficient mutant of BHV-1 were not affected.

Duke Scholars

Published In

Antimicrob Agents Chemother

DOI

ISSN

0066-4804

Publication Date

June 1983

Volume

23

Issue

6

Start / End Page

857 / 865

Location

United States

Related Subject Headings

  • Viral Proteins
  • Thymidine Kinase
  • Protein Biosynthesis
  • Phosphorylation
  • Microbiology
  • Herpesviridae
  • Glycoproteins
  • DNA, Viral
  • Cattle
  • Bromodeoxyuridine
 

Citation

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ICMJE
MLA
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Misra, V., Nelson, R. C., & Babiuk, L. A. (1983). Inhibition of glycosylation of bovine herpesvirus 1 glycoproteins by the thymidine analog (E)-5-(2 Bromovinyl)-2'-deoxyuridine. Antimicrob Agents Chemother, 23(6), 857–865. https://doi.org/10.1128/AAC.23.6.857
Misra, V., R. C. Nelson, and L. A. Babiuk. “Inhibition of glycosylation of bovine herpesvirus 1 glycoproteins by the thymidine analog (E)-5-(2 Bromovinyl)-2'-deoxyuridine.Antimicrob Agents Chemother 23, no. 6 (June 1983): 857–65. https://doi.org/10.1128/AAC.23.6.857.
Misra V, Nelson RC, Babiuk LA. Inhibition of glycosylation of bovine herpesvirus 1 glycoproteins by the thymidine analog (E)-5-(2 Bromovinyl)-2'-deoxyuridine. Antimicrob Agents Chemother. 1983 Jun;23(6):857–65.
Misra, V., et al. “Inhibition of glycosylation of bovine herpesvirus 1 glycoproteins by the thymidine analog (E)-5-(2 Bromovinyl)-2'-deoxyuridine.Antimicrob Agents Chemother, vol. 23, no. 6, June 1983, pp. 857–65. Pubmed, doi:10.1128/AAC.23.6.857.
Misra V, Nelson RC, Babiuk LA. Inhibition of glycosylation of bovine herpesvirus 1 glycoproteins by the thymidine analog (E)-5-(2 Bromovinyl)-2'-deoxyuridine. Antimicrob Agents Chemother. 1983 Jun;23(6):857–865.

Published In

Antimicrob Agents Chemother

DOI

ISSN

0066-4804

Publication Date

June 1983

Volume

23

Issue

6

Start / End Page

857 / 865

Location

United States

Related Subject Headings

  • Viral Proteins
  • Thymidine Kinase
  • Protein Biosynthesis
  • Phosphorylation
  • Microbiology
  • Herpesviridae
  • Glycoproteins
  • DNA, Viral
  • Cattle
  • Bromodeoxyuridine