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Mapping CD55 function. The structure of two pathogen-binding domains at 1.7 A.

Pamela Williams·Yasmin Chaudhry·Ian G Goodfellow·Jason Billington·Robert Powell·O Brad Spiller·David J Evans·Susan Lea
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Abstract

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.

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AnimalsBacterial AdhesionBinding SitesCD55 AntigensCHO CellsComplement ActivationCricetinaeCrystallography, X-RayHumansReceptors, VirusRecombinant ProteinsJournal ArticleResearch Support, Non-U.S. Gov't

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Pamela Williams, Yasmin Chaudhry, Ian G Goodfellow, Jason Billington, Robert Powell, O Brad Spiller, David J Evans, Susan Lea. 2002-12-22. Mapping CD55 function. The structure of two pathogen-binding domains at 1.7 A.. https://doi.org/10.1074/jbc.m212561200

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