Serologically defined linear epitopes in the E2 envelope glycoprotein of Semliki Forest virus

Arch Virol. 1990;113(1-2):99-106. doi: 10.1007/BF01318358.

Abstract

A set of 41 overlapping peptides, representing the complete sequence of SFV-E2 protein were synthesized and analyzed in the ELISA test against murine anti-SFV sera. No single peptide was recognized by all antisera. Eight peptides were found to be highly reactive with hyperimmune anti-SFV sera. Six out of the eight peptide sequences coincide with the most hydrophilic regions of SFV-E2. Out of these, four peptides (amino acid positions 16-35, 61-80, 166-185, 286-305) that contain the least number of alphavirus conserved residues were selected. This panel constitutes the minimal number of peptides necessary and sufficient for specific recognition of hyperimmune mouse anti-SFV sera.

MeSH terms

  • Antigens, Viral / chemical synthesis
  • Antigens, Viral / immunology*
  • Ascitic Fluid / immunology
  • Blotting, Western
  • Enzyme-Linked Immunosorbent Assay
  • Epitopes / immunology*
  • Glycoproteins / immunology
  • Peptide Fragments / chemical synthesis
  • Peptide Fragments / immunology
  • Semliki forest virus / immunology*
  • Viral Envelope Proteins / chemical synthesis
  • Viral Envelope Proteins / immunology*
  • Viral Proteins / chemical synthesis
  • Viral Proteins / immunology*

Substances

  • Antigens, Viral
  • Epitopes
  • Glycoproteins
  • Peptide Fragments
  • Viral Envelope Proteins
  • Viral Proteins