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Infection and Immunity, October 1999, p. 4983-4987, Vol. 67, No. 10
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Binding of Actinobacillus pleuropneumoniae Lipopolysaccharides to Glycosphingolipids Evaluated by Thin-Layer Chromatography

Maan Abul-Milh, Sonia-Élaine Paradis, J. Daniel Dubreuil, and Mario Jacques*

Groupe de Recherche sur les Maladies Infectieuses du Porc and Départément de Pathologie et Microbiologie, Faculté de Médecine Vétérinaire, Université de Montréal, St-Hyacinthe, Québec, Canada J2S 7C6

Received 14 January 1999/Returned for modification 1 April 1999/Accepted 7 July 1999

The binding profile of Actinobacillus pleuropneumoniae serotypes 1 and 2 to various glycosphingolipids was evaluated by using thin-layer chromatogram overlay. A. pleuropneumoniae whole cells recognized glucosylceramide (Glcbeta 1Cer), galactosylceramide (Galbeta 1Cer) with hydroxy and nonhydroxy fatty acids, sulfatide (SO3-3Galbeta 1Cer), lactosylceramide (Galbeta 1-4Glcbeta 1Cer), gangliotriaosylceramide GgO3 (GalNAcbeta 1-4Galbeta 1-4Glcbeta 1Cer), and gangliotetraosylceramide GgO4 (Galbeta 1-3GalNAcbeta 1-4Galbeta 1-4Glcbeta 1Cer) glycosphingolipids. We observed no binding to globoseries, globotriaosylceramide Gb3, globoside Gb4, or Forssman Gb5 glycosphingolipids or to gangliosides GM1, GM2, GM3, GD1a, GD1b, GD3, and GT1b. The A. pleuropneumoniae strains tested also failed to detect phosphatidylethanolamine or ceramide. Interestingly, extracted lipopolysaccharide (LPS) of serotype 1 and serotype 2 as well as detoxified LPS of serotype 1 showed binding patterns similar to that of whole bacterial cells. Binding to GlcCer, GalCer, sulfatide, and LacCer, but not to GgO3 and GgO4 glycosphingolipids, was inhibited after incubation of the bacteria with monoclonal antibodies against LPS O antigen. These findings indicate the involvement of LPS in recognition of three groups of glycosphingolipids: (i) GlcCer and LacCer, where glucose is probably an important saccharide sequence required for LPS binding; (ii) GalCer and sulfatide glycosphingolipids, where the sulfate group is part of the binding epitope of the isoreceptor; and (iii) GgO3 and GgO4, where GalNacbeta 1-4Gal disaccharide represents the minimal common binding epitope. Taken together, our results indicate that A. pleuropneumoniae LPS recognize various saccharide sequences found in different glycosphingolipids, which probably represents a strong virulence attribute.

* Corresponding author. Mailing address: Groupe de Recherche sur les Maladies Infectieuses du Porc, Départément de Pathologie et Microbiologie, Faculté de Médecine Vétérinaire, Université de Montréal, 3200 rue Sicotte, C.P. 5000, St-Hyacinthe, Québec, Canada J2S 7C6. Phone: (450) 773-8521, ext. 8348. Fax: (450) 778-8108. E-mail: jacqum{at}medvet.umontreal.ca.

Infection and Immunity, October 1999, p. 4983-4987, Vol. 67, No. 10
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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