Differences in antigenicity of E2 in Semliki Forest virus particles and in infected cells

Arch Virol. 1994;135(3-4):433-5. doi: 10.1007/BF01310027.

Abstract

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.

Publication types

  • Comparative Study

MeSH terms

  • 1-Deoxynojirimycin / analogs & derivatives
  • 1-Deoxynojirimycin / pharmacology
  • Animals
  • Antibodies, Monoclonal
  • Antigens, Viral / analysis*
  • Antigens, Viral / biosynthesis
  • Antigens, Viral / immunology
  • Antiviral Agents / pharmacology
  • Cells, Cultured
  • Chick Embryo
  • Deoxyglucose / pharmacology
  • Epitopes / analysis*
  • Glycosylation / drug effects
  • Protein Conformation
  • Semliki forest virus / drug effects
  • Semliki forest virus / immunology*
  • Semliki forest virus / metabolism
  • Viral Envelope Proteins / chemistry
  • Viral Envelope Proteins / immunology
  • Viral Envelope Proteins / metabolism*

Substances

  • Antibodies, Monoclonal
  • Antigens, Viral
  • Antiviral Agents
  • Epitopes
  • Viral Envelope Proteins
  • 1-Deoxynojirimycin
  • Deoxyglucose
  • N-methyldeoxynojirimycin