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Infect Immun, February 1998, p. 870-873, Vol. 66, No. 2
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

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

E. J. Helmerhorst,1 J. J. Maaskant,2 and B. J. Appelmelk2,*

Department of Oral Biochemistry1 and Department of Medical Microbiology,2 Vrije Universiteit, 1081 BT Amsterdam, The Netherlands

Received 19 September 1997/Returned for modification 27 October 1997/Accepted 26 November 1997

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.

* Corresponding author. Mailing address: Department of Medical Microbiology Vrije Universiteit, van der Boechorststraat 7, 1081 BT Amsterdam, The Netherlands. Phone: 31 20 4448297. Fax: 31 20 4448318. E-mail: BJ.Appelmelk.mm{at}med.vu.nl.




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