Characterization of a monoclonal antibody that binds to an epitope on soluble bacterial peptidoglycan fragments.
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.
Merkel
G J
GJ
Department of Microbiology and Immunology, Indiana University School of Medicine, Fort Wayne, Indiana 46805, USA. merkel@ipfw.edu
Scofield
B A
BA
D000818:Animals; D000907:Antibodies, Bacterial / Q000276:immunology; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000918:Antibody Specificity; D000937:Antigen-Antibody Reactions; D000942:Antigens, Bacterial / Q000276:immunology*; D000939:Epitopes; D009344:Neisseria gonorrhoeae / Q000276:immunology*; D010457:Peptidoglycan / Q000276:immunology*
D000907:Antibodies, Bacterial; D000911:Antibodies, Monoclonal; D000942:Antigens, Bacterial; D000939:Epitopes; D010457:Peptidoglycan