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Clinical and Diagnostic Laboratory Immunology, May 2001, p. 647-651, Vol. 8, No. 3
1071-412X/01/$04.00+0   DOI: 10.1128/CDLI.8.3.647-651.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Characterization of a Monoclonal Antibody That Binds to an Epitope on Soluble Bacterial Peptidoglycan Fragments

Glenn J. Merkel* and Barbara A. Scofield

Department of Microbiology and Immunology, Indiana University School of Medicine, Fort Wayne, Indiana 46805

Received 2 November 2000/Returned for modification 9 January 2001/Accepted 22 January 2001

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.

* Corresponding author. Mailing address: Indiana University School of Medicine, Fort Wayne Center, CM 345, 2101 East Coliseum Blvd., Fort Wayne, IN 46805-1499. Phone: (219) 481-6735. Fax: (219) 481-6408. E-mail: merkel{at}ipfw.edu.

Clinical and Diagnostic Laboratory Immunology, May 2001, p. 647-651, Vol. 8, No. 3
1071-412X/01/$04.00+0   DOI: 10.1128/CDLI.8.3.647-651.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.




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