Pathogenicity and immunogenicity of recombinant human retinal S-antigen fusion protein

Curr Eye Res. 1992;11 Suppl:113-7. doi: 10.3109/02713689208999520.

Abstract

A full-length cDNA clone to human S-antigen (HS-ag) was isolated from lambda gt 10 human retinal library and expressed as a fusion protein with glutathione S-transferase (GST) in E. Coli. Uveitogenicity and immunogenicity of recombinant GST-HS-ag fusion protein and native HS-ag were compared in EAU-susceptible Lewis rats. Recombinant HS-ag was found less uveitogenic than native HS-ag. Animals inoculated with recombinant HS-ag developed EAU on day 17, three days later than those inoculated with native HS-ag, the incidence of the disease was reduced from 80% to 58% and the score of clinical severity reduced from 2.2 to 1.3 points respectively. In contrast, rGST-HS-ag was more immunogenic than native HS-ag as it elicited four times higher levels of antibodies which reacted specifically with both antigens.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antigens / genetics
  • Antigens / immunology*
  • Arrestin
  • Autoantigens / immunology*
  • Disease Models, Animal
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme-Linked Immunosorbent Assay
  • Escherichia coli / genetics
  • Eye Proteins / genetics
  • Eye Proteins / immunology*
  • Gene Expression
  • Glutathione Transferase / immunology*
  • Humans
  • Incidence
  • Male
  • Rats
  • Rats, Inbred Lew
  • Recombinant Fusion Proteins / immunology*
  • Uveitis / immunology*
  • Uveitis / pathology*

Substances

  • Antigens
  • Arrestin
  • Autoantigens
  • Eye Proteins
  • Recombinant Fusion Proteins
  • Glutathione Transferase