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Decay-accelerating factor (CD55), a regulator of the alternative and classical pathways of complement activation, is expressed on all serum-exposed cells. It is used by pathogens, including many enteroviruses and uropathogenic Escherichia coli, as a receptor prior to infection. We describe the x-ray structure of a pathogen-binding fragment of human CD55 at 1.7 A resolution containing two of the three domains required for regulation of human complement. We have used mutagenesis to map biological functions onto the molecule; decay-accelerating activity maps to a single face of the molecule, whereas bacterial and viral pathogens recognize a variety of different sites on CD55.

Original publication




Journal article


J Biol Chem

Publication Date





10691 - 10696


Animals, Bacterial Adhesion, Binding Sites, CD55 Antigens, CHO Cells, Complement Activation, Cricetinae, Crystallography, X-Ray, Humans, Receptors, Virus, Recombinant Proteins