Differences in antigenicity of E2 in Semliki Forest virus particles and in infected cells.
Using six monoclonal antibodies to epitopes a-f on the glycoprotein E2 of Semliki Forest virus (SFV) we found antigenic differences between E2 in infected cells and in virus particles, respectively, if glycosylation was impaired by 2-deoxy-D-glucose or inhibited by N-methyl-1-deoxynojirimycin. Furthermore we concluded that a conformational change of E2 takes place on virus budding.
Repges-Illguth
S
S
Institute of Medical Virology, Justus-Leibig University Giessen, Federal Republic of Germany.
Kaluza
G
G
D017485:1-Deoxynojirimycin / Q000031:analogs & derivatives / Q000494:pharmacology; D000818:Animals; D000911:Antibodies, Monoclonal; D000956:Antigens, Viral / Q000032:analysis* / Q000096:biosynthesis / Q000276:immunology; D000998:Antiviral Agents / Q000494:pharmacology; D002478:Cells, Cultured; D002642:Chick Embryo; D003847:Deoxyglucose / Q000494:pharmacology; D000939:Epitopes / Q000032:analysis*; D006031:Glycosylation / Q000187:drug effects; D011487:Protein Conformation; D012672:Semliki forest virus / Q000187:drug effects / Q000276:immunology* / Q000378:metabolism; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D000956:Antigens, Viral; D000998:Antiviral Agents; D000939:Epitopes; D014759:Viral Envelope Proteins; D017485:1-Deoxynojirimycin; D003847:Deoxyglucose; C033424:N-methyldeoxynojirimycin