Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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

DOI

10.1074/jbc.M212561200

Type

Journal article

Journal

J Biol Chem

Publication Date

21/03/2003

Volume

278

Pages

10691 - 10696

Keywords

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