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Structural variability and originality of the Bordetella endotoxins

Equipe 'Endotoxines', UMR 8619, Centre National de la Recherche Scientifique, Biochimie, Université de Paris-Sud, Orsay, France, martine.caroff{at}bbmpc.u-psud. fr

Laurent Aussel

Equipe 'Endotoxines', UMR 8619, Centre National de la Recherche Scientifique, Biochimie, Université de Paris-Sud, Orsay, France

Hassan Zarrouk

Equipe 'Endotoxines', UMR 8619, Centre National de la Recherche Scientifique, Biochimie, Université de Paris-Sud, Orsay, France

Adèle Martin

Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada

James C. Richards

Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada

Hélène Thérisod

Equipe 'Endotoxines', UMR 8619, Centre National de la Recherche Scientifique, Biochimie, Université de Paris-Sud, Orsay, France

Malcolm B. Perry

Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada

Doris Karibian

Equipe 'Endotoxines', UMR 8619, Centre National de la Recherche Scientifique, Biochimie, Université de Paris-Sud, Orsay, France

Structural studies of Bordetella endotoxins (LPSs) have revealed remarkable differences: (i) between their LPSs and those of other bacterial pathogens; (ii) among the LPSs of the seven identified Bordetella species; and (iii) among the LPSs of some Bordetella strains. The lipid As have the `classical' bisphosphorylated diglucosamine backbone but tend to have fewer and species-specific fatty acid components compared to those of other genera. Nevertheless, three strains of B. bronchiseptica have at least three different fatty acid distributions; however, the recently identified B. hinzii and B. trematum LPSs had identical lipid A structures. The B. pertussis core is a dodecasaccharide multi-branched structure bearing amino and carboxylic groups. Another unusual feature is the presence of free amino sugars in the central core region and a complex distal trisaccharide unit containing five amino groups of which four are acetylated and one is methylated. The B. pertussis LPS does not have O-chains and that of B. trematum had only a single O-unit, unlike the LPSs of all the other species of the smooth-type. The O-chain-free cores of non-B. pertussis LPSs were always built on the B. pertussis core model but most were species-specifically incomplete. The LPS structures of three B. bronchiseptica strains were found to be different from each other. The O-chains of B. bronchiseptica and B. parapertussis were almost identical and had some features in common with B. hinzii O-chain. Serological analyses are consistent with the determined LPS structures.

Journal of Endotoxin Research, Vol. 7, No. 1, 63-68 (2001)
DOI: 10.1177/09680519010070011101


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