Non-immune Fab- and Fc- mediated interactions of avian Ig with S. aureus and group C and G streptococci

APMIS. 1988 Mar;96(3):239-49. doi: 10.1111/j.1699-0463.1988.tb05297.x.

Abstract

Serum samples from 19 avian species representing 8 orders were tested for their capacity to inhibit the Fab- and Fc-mediated immunoglobulin binding to protein A-carrying S. aureus and protein G-carrying group C and G streptococci. Four species (mallard, dunlin, starling and blackbird) belonging to three different orders showed a high degree of Fc-mediated protein A- and protein G-reactivity. Five species demonstrated a high level and nine species exhibited a low level of Fab-mediated protein A-reactivity. The four species identified as Fc-reactive were capable of Fab-mediated immunoglobulin binding with streptococcal surface proteins but incapable of Fab-mediated protein A binding. SDS-PAGE analysis confirmed that the protein A-Sepharose affinity purified material contained proteins corresponding to immunoglobulin chains. Inhibition results by avian sera were confirmed by direct binding of protein A-reactive proteins to bacteria, by precipitation in gel and by Western blot analysis of binding to protein A and protein G, respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Bacterial / immunology*
  • Bacterial Proteins / immunology
  • Birds / immunology*
  • Immunodiffusion
  • Immunoglobulin Fab Fragments / immunology
  • Immunoglobulin Fc Fragments / immunology
  • Immunoglobulins / immunology*
  • Immunosorbent Techniques
  • Protein Binding
  • Staphylococcal Protein A / metabolism
  • Staphylococcus aureus / immunology*
  • Streptococcus / immunology*

Substances

  • Antibodies, Bacterial
  • Bacterial Proteins
  • Immunoglobulin Fab Fragments
  • Immunoglobulin Fc Fragments
  • Immunoglobulins
  • Staphylococcal Protein A