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Related Experiment Videos

Function-blocking antithrombospondin-1 monoclonal antibodies.

D S Annis1, J E Murphy-Ullrich, D F Mosher

  • 1Department of Medicine, University of Wisconsin, Madison, WI 53706, USA.

Journal of Thrombosis and Haemostasis : JTH
|January 20, 2006
PubMed
Summary
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This study maps the binding sites of 13 anti-thrombospondin-1 (TSP-1) monoclonal antibodies (mAbs). Findings reveal TSP-1

Area of Science:

  • Immunology and Molecular Biology
  • Protein Structure and Function

Background:

  • Thrombospondin-1 (TSP-1) is involved in various biological processes.
  • Inhibitory activities of anti-TSP-1 monoclonal antibodies (mAbs) suggest functional roles for TSP-1 domains.

Purpose of the Study:

  • To precisely map the epitopes of 13 anti-TSP-1 mAbs.
  • To identify which TSP-1 or TSP-2 modules these epitopes reside in.

Main Methods:

  • Epitope mapping of 13 anti-TSP-1 monoclonal antibodies (mAbs).
  • Analysis of antibody binding to different TSP-1 and TSP-2 modules.

Main Results:

  • Epitopes for 13 anti-TSP-1 mAbs were assigned or refined across TSP-1 domains: N-terminal, properdin, EGF-like, and calcium-binding wire modules.

Related Experiment Videos

  • One antibody (A6.1) recognized a conserved region in the calcium-binding wire, cross-reacting with mouse and human TSP-1 and weakly with TSP-2.
  • Several antibodies showed cross-reactivity with mouse TSP-1.

    • Conclusions:

    • Biological activities of TSP-1 are distributed throughout its structure, including EGF-like modules previously not implicated.
    • Steric hindrance likely contributes to the inhibitory effects of some mAbs, particularly those binding near each other in calcium-bound TSP-1.
    • One mAb (mAb133) binding the calcium-binding wire interferes with TGF-beta activation by properdin modules, suggesting complex functional interactions.