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Solution structure of human secretory component and implications for biological function.

Alexandra Bonner1, Clémentine Perrier, Blaise Corthésy

  • 1Department of Biochemistry and Molecular Biology, University College London, Darwin Building, Gower Street, London WC1E 6BT, United Kingdom.

The Journal of Biological Chemistry
|April 13, 2007
PubMed
Summary
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Secretory component (SC) forms secretory IgA and has innate neutralizing abilities. Its unexpected compact, J-shaped structure reveals how it binds to IgA and pathogens.

Area of Science:

  • Immunology
  • Structural Biology
  • Biophysics

Background:

  • Secretory component (SC) is crucial for secretory IgA function at mucosal surfaces.
  • Free SC exhibits innate immune properties, neutralizing pathogens independently of IgA.
  • Understanding SC's structure is key to its biological roles.

Purpose of the Study:

  • To determine the three-dimensional structure of full-length free secretory component (SC).
  • To elucidate the structural basis for SC's interactions with ligands like polymeric IgA (pIgA).

Main Methods:

  • X-ray and neutron scattering techniques were employed.
  • Ultracentrifugation was used to analyze SC's size and shape.
  • Constrained scattering modeling, utilizing up to 13,000 models, predicted SC's structure.

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Main Results:

  • Free SC adopts an unexpected compact, J-shaped three-dimensional structure.
  • SC has a radius of gyration of 3.53-3.63 nm and a length of 12.5 nm.
  • Glycosylation sites are localized, leaving IgA-binding sites accessible.

Conclusions:

  • This study provides the first structural analysis of full-length free SC.
  • The compact, J-shaped structure facilitates interactions with pIgA and pathogen motifs.
  • Findings enhance understanding of mucosal immunity and SC's dual role.