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Structure of the measles virus hemagglutinin bound to the CD46 receptor

César Santiago1, María L Celma, Thilo Stehle

  • 1Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, Campus Universidad Autónoma, Madrid, Spain.

Nature Structural & Molecular Biology
|December 17, 2009
PubMed

Insights

The measles virus hemagglutinin (MV-H) protein binds host cells via CD46 or SLAM receptors. Structural analysis reveals a unique groove in MV-H interacting with a proline-rich motif on CD46 and SLAM, crucial for measles virus entry.

Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • Measles virus is highly contagious, causing significant disease globally, especially in children.
  • Viral entry is mediated by the measles virus hemagglutinin (MV-H) glycoprotein binding to host cell receptors CD46 or signaling lymphocyte activation molecule (SLAM).

Purpose of the Study:

  • To determine the crystal structure of MV-H in complex with CD46.
  • To elucidate the molecular interactions driving measles virus attachment to host cells.

Main Methods:

  • X-ray crystallography was used to obtain the structure of MV-H bound to CD46.
  • Bioinformatic analysis was performed to compare interaction motifs with SLAM.

Main Results:

  • The crystal structure revealed a unique groove on the MV-H beta-propeller domain that interacts with CD46.
  • A key interaction involves a proline-rich (PP) motif on CD46 penetrating a hydrophobic pocket in MV-H.
  • A similar PP motif was identified in SLAM, indicating a common recognition epitope.

Conclusions:

  • The identified groove and PP motif interaction are critical for measles virus binding to CD46 and SLAM.
  • This structural insight provides a basis for understanding measles virus tropism and developing antiviral strategies.

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