Abstract:
:The antibiotic tunicamycin, which blocks the synthesis of glycoproteins, inhibited the production of infectious herpes simplex virus. In the presence of this drug, [14C]glucosamine and [3H]mannose incorporation was reduced in infected cells, whereas total protein synthesis was not affected. Gel electrophoresis of [2-3H]mannose-labeled polypeptides failed to detect glycoprotein D or any of the other herpes simplex virus glycoproteins. By use of specific antisera we demonstrated that in the presence of tunicamycin the normal precursors to viral glycoproteins failed to appear. Instead, lower-molecular-weight polypeptides were found which were antigenically and structurally related to the glycosylated proteins. Evidence is presented to show that blocking the addition of carbohydrate to glycoprotein precursors with tunicamycin results in the disappearance of molecules, possibly due to degradation of the unglycosylated polypeptides. We infer that the added carbohydrate either stabilizes the envelope proteins or provides the proper structure for correct processing of the molecules needed for infectivity.
journal_name
J Viroljournal_title
Journal of virologyauthors
Pizer LI,Cohen GH,Eisenberg RJdoi
10.1128/JVI.34.1.142-153.1980subject
Has Abstractpub_date
1980-04-01 00:00:00pages
142-53issue
1eissn
0022-538Xissn
1098-5514journal_volume
34pub_type
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doi:10.1128/JVI.68.1.400-410.1994
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doi:10.1128/JVI.24.1.401-405.1977
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journal_title:Journal of virology
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journal_title:Journal of virology
pub_type: 杂志文章
doi:10.1128/JVI.62.5.1606-1616.1988
更新日期:1988-05-01 00:00:00
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doi:10.1128/JVI.59.3.556-563.1986
更新日期:1986-09-01 00:00:00
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journal_title:Journal of virology
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