Structural characterization of Bordetella parapertussis lipid A.
Bordetella parapertussis like B. pertussis, is a causal agent of whooping cough but is not a strictly human pathogen. Because its endotoxin, a major structural component of the Gram-negative outer membrane, is an important virulence factor, we have analyzed the structure of its toxic lipid domain, in one rough and two smooth bacterial strains. Chemical analyses and mass spectra obtained before and after recently developed mild-alkali treatments revealed that the lipids A have the common bisphosphorylated beta-(1-->6)-linked D-glucosamine disaccharide with hydroxytetradecanoic acid in amide linkages. All three strains have two major molecular species: a tetraacyl and a pentaacyl species. The rough strain is richer in a minor hexaacyl species. Acylation at the C-2, C-3, and C-3' positions was different from that of the B. pertussis lipid A. The C-2 position carries a secondary hexadecanoic acid, the C-3 position is free, and the C-3' position is substituted with hydroxydecanoic acid (not at C-3 as in B. pertussis), and the rough strain hexaacyl species carries a second secondary hexadecanoic acid. Like the lipid A of B. pertussis, the hydroxytetradecanoic acid at the C-2' position was substituted by tetradecanoic acid.
El Hamidi
Asmaa
A
Equipe Endotoxines, UMR 8619 du Centre National de la Recherche Scientifique, Université de Paris-Sud, Orsay, France.
Novikov
Alexey
A
Karibian
Doris
D
Perry
Malcolm B
MB
Caroff
Martine
M
D042483:Bordetella parapertussis / Q000737:chemistry*; D004952:Esters / Q000737:chemistry; D005227:Fatty Acids / Q000737:chemistry; D005944:Glucosamine / Q000737:chemistry; D006801:Humans; D008050:Lipid A / Q000737:chemistry*; D015394:Molecular Structure; D011487:Protein Conformation
D004952:Esters; D005227:Fatty Acids; D008050:Lipid A; D005944:Glucosamine