Open AccessCharacterization of a Monoclonal Antibody That Binds to an Epitope on Soluble Bacterial Peptidoglycan Fragments
Author(s) -
Glenn J. Merkel,
Barbara A. Scofield
Publication year - 2001
Publication title -
clinical and diagnostic laboratory immunology
Language(s) - English
Resource type - Journals
eISSN - 1098-6588
pISSN - 1071-412X
DOI - 10.1128/cdli.8.3.647-651.2001
Subject(s) - epitope , peptidoglycan , monoclonal antibody , glycan , staphylococcus aureus , antibody , chemistry , bacteria , microbiology and biotechnology , biochemistry , enzyme , biology , glycoprotein , genetics , immunology
We employed an inhibition-type enzyme-linked immunosorbent assay (ELISA) to characterize a murine immunoglobulin M monoclonal antibody (MAb) that bound soluble macromolecular peptidoglycan (PG). With this ELISA, the MAb was capable of detecting soluble PG concentrations of less than 10 ng/ml. Enzymatic digestion of PG reduced binding by more than 100-fold, implying that the epitope recognized by this antibody depended on repeating subunits within the glycan backbone. Additionally, the MAb bound to epitopes on both O-acetylated and non-O-acetylated PG fragments from gram-negative bacteria, as well as PG fragments from Staphylococcus aureus and PG fragments released into the medium by a number of gram-positive and gram-negative bacteria.