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