Measles virus hemagglutinin: structural insights into cell entry and measles vaccine

Takao Hashiguchi1, Katsumi Maenaka, Yusuke Yanagi

  • 1Department of Virology, Faculty of Medicine, Kyushu University Fukuoka, Japan.

Frontiers in Microbiology
|February 10, 2012
PubMed

Insights

Measles virus enters cells using hemagglutinin (H) and fusion (F) proteins. New crystal structures reveal how the H protein binds receptors, aiding measles vaccine development.

Area of Science:

  • Virology
  • Immunology
  • Structural Biology

Background:

  • Measles virus (MV) is a highly contagious pathogen causing significant global childhood illness and death.
  • MV entry into host cells is facilitated by its envelope glycoproteins: hemagglutinin (H) and fusion (F) protein.
  • Cellular receptors targeted by MV include signaling lymphocyte activation molecule (SLAM), CD46, and nectin-4.

Purpose of the Study:

  • To elucidate the structural mechanisms of MV entry into host cells.
  • To understand the interaction between MV-H protein and its cellular receptors (SLAM, CD46).
  • To provide insights relevant to the development and effectiveness of measles vaccines.

Main Methods:

  • X-ray crystallography was employed to determine the structures of the MV-H protein.
  • Structures were determined for both unbound MV-H protein and MV-H in complex with SLAM and CD46 receptors.

Main Results:

  • Detailed crystal structures of the MV-H protein, both alone and bound to SLAM or CD46, were obtained.
  • These structures illuminate the molecular details of receptor binding mediated by the H protein.
  • The findings highlight the critical role of the H-F protein interaction in initiating MV cell entry.

Conclusions:

  • Structural insights into MV-H protein-receptor interactions are crucial for understanding paramyxovirus entry mechanisms.
  • This research provides a foundation for improving the efficacy of existing measles vaccines and developing novel antiviral strategies.