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Related Experiment Videos

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

Pamela Williams1, Yasmin Chaudhry, Ian G Goodfellow

  • 1Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, United Kingdom.

The Journal of Biological Chemistry
|December 25, 2002
PubMed
Summary
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The crystal structure of decay-accelerating factor (CD55) reveals how it regulates complement activation and serves as a pathogen receptor. Mutagenesis mapped its decay-accelerating function to one face and pathogen binding sites to various locations.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Immunology

Background:

  • Decay-accelerating factor (CD55) regulates complement pathways and acts as a cellular receptor for pathogens.
  • Pathogens like enteroviruses and E. coli utilize CD55 for host cell entry.
  • Understanding CD55 structure is crucial for comprehending complement regulation and host-pathogen interactions.

Purpose of the Study:

  • To determine the x-ray structure of a pathogen-binding fragment of human CD55.
  • To map the functional regions of CD55 using mutagenesis.
  • To elucidate the structural basis for CD55's dual role in complement regulation and pathogen recognition.

Main Methods:

  • X-ray crystallography was used to obtain the structure of a CD55 fragment at 1.7 A resolution.

Related Experiment Videos

  • Site-directed mutagenesis was employed to identify key residues involved in CD55 function.
  • Biochemical assays were likely used to assess decay-accelerating activity and pathogen binding.

    • Main Results:

    • The x-ray structure of a two-domain fragment of human CD55 was determined.
    • Mutagenesis studies localized the decay-accelerating activity to a specific molecular face.
    • Distinct binding sites for bacterial and viral pathogens were identified on the CD55 molecule.

    Conclusions:

    • The structure provides insights into the mechanism of complement regulation by CD55.
    • CD55 employs different surfaces for complement inhibition and pathogen interaction.
    • This structural information can inform the development of therapeutics targeting complement-mediated diseases or pathogen entry.