Structure of a pertussis toxin-sugar complex as a model for receptor binding

• Published in: Nature structural biology Vol. 1; no. 9; pp. 591 - 596
• Main Authors: Stein, Penelope E, Boodhoo, Amechand, Armstrong, Glen D, Heerze, Louis D, Cockle, Stephen A, Klein, Michel H, Read, Randy J
• Format: Journal Article
• Language: English
• Published: United States 01-09-1994
• Subjects: Bacterial Vaccines - chemical synthesis; Carbohydrate Sequence; Crystallography, X-Ray; Molecular Conformation; Molecular Sequence Data; Oligosaccharides - chemistry; Oligosaccharides - metabolism; Pertussis Toxin; Receptors, Cell Surface - metabolism; Transferrin - chemistry; Virulence Factors, Bordetella - chemistry; Virulence Factors, Bordetella - metabolism; Whooping Cough - prevention & control
• ISSN: 1072-8368; 2331-365X
• DOI: 10.1038/nsb0994-591

Pertussis toxin is an exotoxin from the bacterium Bordetella pertussis which is important the pathogenesis of whooping cough and the generation of a protective immune response. The diverse biological activities of the toxin depend on its ability to recognize carbohydrate-containing receptors on a wide variety of eukaryotic cells. We present here the crystal structure of pertussis toxin complexed with a soluble oligosaccharide from transferrin. Binding sites for the terminal sialic acid-galactose moiety are revealed on both subunits S2 and S3 of the B-oligomer. Identification of amino acid residues involved in receptor binding will improve the design of genetically inactivated toxins for use in new acellular whooping cough vaccines.