Show simple item record

dc.contributor.authorMorgan, A. J.
dc.contributor.authorSmith, Allan
dc.contributor.authorBarker, R. N.
dc.contributor.authorEpstein, M. A.
dc.date.accessioned2016-04-07T11:41:08Z
dc.date.available2016-04-07T11:41:08Z
dc.date.issued1984-02
dc.identifier.citationMorgan , A J , Smith , A , Barker , R N & Epstein , M A 1984 , ' A Structural Investigation of the Epstein—Barr (EB) Virus Membrane Antigen Glycoprotein, gp340 ' , Journal of General Virology , vol. 65 , pp. 397-404 . https://doi.org/10.1099/0022-1317-65-2-397
dc.identifier.issn1465-2099
dc.identifier.otherPURE: 9790623
dc.identifier.otherPURE UUID: 3a4ad209-62a6-4e7b-ab27-318a5bf698f4
dc.identifier.otherScopus: 0021368184
dc.identifier.urihttp://hdl.handle.net/2299/17063
dc.description.abstractEpstein—Barr (EB) virus membrane antigen (MA) glycoprotein (gp340) purified by a molecular weight-based technique has been subjected to biochemical analysis. Following treatment with glycosidases or tunicamycin during synthesis, the carbohydrate moiety was found to be made up of both O-linked and N-linked types and to constitute about 50% of the molecular mass. Digestion studies with neuraminidase and oligosaccharidase have indicated that the molecule is heavily sialated with most of the sialic acid located on the O-linked sugars. The high carbohydrate content of gp340 appears to confer resistance to proteolysis; thus, V8 protease was only effective at concentrations above 1 mg/ml when three large fragments of mol. wt. 330K, 190K and 160K were generated. Removal of sialic acid before V8 protease digestion did not alter this pattern nor affect the antigenicity of the digestion fragments. Antigenicity of the intact molecule was likewise unaffected by removal of sialic acid nor were the O-linked and N-linked carbohydrate moieties essential for this property. The binding of virus-neutralizing human sera and monoclonal antibody by gp340 from which either O-linked or N-linked sugars had been removed seems to indicate that the sites on the molecule that generate the neutralizing antibodies are present in the protein component. The significance of these results is discussed in relation to the development of a subunit vaccine against EB virus.en
dc.language.isoeng
dc.relation.ispartofJournal of General Virology
dc.subjectglycosylation
dc.subjectV8 protease digestion
dc.subjectMA polypeptide
dc.subjectEB virus
dc.titleA Structural Investigation of the Epstein—Barr (EB) Virus Membrane Antigen Glycoprotein, gp340en
dc.contributor.institutionSchool of Humanities
dc.description.statusPeer reviewed
dc.relation.schoolSchool of Humanities
dcterms.dateAccepted1984-02
rioxxterms.versionofrecordhttps://doi.org/10.1099/0022-1317-65-2-397
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record