Identification of a small epitope in domain Ib of Pseudomonas aeruginosa exotoxin A that elicits enzyme-neutralizing antibodies

FEMS Microbiol Immunol. 1992 Jul;4(5):267-72. doi: 10.1111/j.1574-6968.1992.tb05005.x.

Abstract

A peptide corresponding to amino acids 392-404 of the amino acid sequence of Pseudomonas aeruginosa exotoxin A (the last 13 amino acids of domain Ib) was synthesized and coupled to thyroglobulin. The conjugate induced an antiserum in rabbits with high antibody titer against native toxin as measured by ELISA, and this antiserum was highly efficient in inhibiting the ADP-ribosyltransferase activity of exotoxin A. These data corroborate the potential importance of amino acids 400-404 in the enzymatic mechanism of exotoxin A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ADP Ribose Transferases*
  • Amino Acid Sequence
  • Animals
  • Antibodies, Bacterial / immunology*
  • Antigens, Bacterial / immunology*
  • Bacterial Toxins*
  • Epitopes / immunology*
  • Exotoxins / immunology*
  • Molecular Sequence Data
  • Peptide Fragments / chemical synthesis
  • Peptide Fragments / immunology*
  • Poly(ADP-ribose) Polymerase Inhibitors
  • Poly(ADP-ribose) Polymerases / immunology*
  • Pseudomonas aeruginosa / enzymology
  • Pseudomonas aeruginosa / immunology*
  • Pseudomonas aeruginosa Exotoxin A
  • Rabbits
  • Thyroglobulin
  • Virulence Factors*

Substances

  • Antibodies, Bacterial
  • Antigens, Bacterial
  • Bacterial Toxins
  • Epitopes
  • Exotoxins
  • Peptide Fragments
  • Poly(ADP-ribose) Polymerase Inhibitors
  • Virulence Factors
  • Thyroglobulin
  • ADP Ribose Transferases
  • Poly(ADP-ribose) Polymerases