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[Entry mechanism of morbillivirus family]

Hideo Fukuhara1, Surui Chen, Shin Takeda

  • 1Laboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University.

Yakugaku Zasshi : Journal of the Pharmaceutical Society of Japan
|May 8, 2013
PubMed

Insights

Morbilliviruses like measles use hemagglutinin (H) to enter cells via SLAM and Nectin 4. This review details Nectin 4, H-receptor structures, and H-F communication, aiding understanding of morbillivirus entry and drug development.

Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • Morbilliviruses, including measles virus, are highly contagious and lethal.
  • Viral entry mechanisms are crucial for understanding infection and developing antivirals.
  • The hemagglutinin (H) glycoprotein mediates morbillivirus entry via specific cellular receptors.

Purpose of the Study:

  • To summarize current knowledge on morbillivirus entry mechanisms.
  • To highlight the role of the newly identified receptor, Nectin 4.
  • To provide insights into the molecular interactions governing virus-host cell binding and fusion.

Main Methods:

  • Review of recent literature on morbillivirus entry.
  • Analysis of crystal structures of H-receptor complexes.
  • Summary of biochemical studies on hemagglutinin-fusion (H-F) protein communication.

Main Results:

  • Nectin 4 is a newly identified cellular receptor for morbilliviruses.
  • Crystal structures reveal the binding interfaces between H and its receptors (SLAM and Nectin 4).
  • Biochemical studies elucidate the communication pathway between H and the fusion (F) protein, essential for viral entry.

Conclusions:

  • Understanding morbillivirus entry requires detailed knowledge of receptor interactions and H-F protein dynamics.
  • Structural and biochemical data provide a foundation for designing novel antiviral strategies.
  • Further research into these molecular mechanisms can lead to effective drug development against morbillivirus infections.

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