Anti-Lipid A Monoclonal Antibody Centoxin (HA-1A) Binds to a Wide Variety of Hydrophobic Ligands

Author:

Helmerhorst E. J.1,Maaskant J. J.2,Appelmelk B. J.2

Affiliation:

1. Department of Oral Biochemistry1 and

2. Department of Medical Microbiology,2 Vrije Universiteit, 1081 BT Amsterdam, The Netherlands

Abstract

ABSTRACT This note describes the binding specificities of four lipid A monoclonal antibodies (MAbs) including Centoxin (HA-1A); these MAbs display similar binding properties. MAbs reacted with lipid A and heat-killed smooth bacteria, whereas no reactivity was observed with smooth lipopolysaccharide (LPS). Immunoblotting of bacterial extracts separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the MAbs bound to many polypeptide bands including the molecular weight markers. Denaturation of bovine serum albumin (BSA) by boiling or dithiothreitol treatment unmasked antibody epitopes. In addition, binding both to a hydrophobic aliphatic C12 chain covalently coupled to BSA and to single-stranded DNA was observed. The polyreactivity of these clones is most likely mediated by a preferential reactivity with hydrophobic molecular patches.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

Reference20 articles.

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2. Monoclonal antibodies detecting novel structures in the core region of Salmonella minnesota lipopolysaccharide.;Appelmelk B. J.;FEMS Microbiol. Lett.,1987

3. Production and characterization of mouse monoclonal antibodies reacting with the lipopolysaccharide core region of Gram-negative bacilli.;Appelmelk B. J.;J. Med. Microbiol.,1988

4. Diversity in lipid A binding ligands: comparison of lipid A monoclonal antibodies with BPI.;Appelmelk B. J.;Prog. Clin. Biol. Res.,1995

5. Immunotherapy of endotoxemia and septicemia.;Baumgartner J. D.;Immunobiology,1993

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