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Structural basis of efficient contagion: measles variations on a theme by parainfluenza viruses

Mathieu Mateo1, Chanakha K Navaratnarajah1, Roberto Cattaneo1

  • 1Department of Molecular Medicine, Mayo Clinic, and Virology and Gene Therapy Track, Mayo Graduate School, 200 First Street SW, Rochester, MN 55905, USA.

Current Opinion in Virology
|February 5, 2014
PubMed

Insights

Measles virus uses specific proteins, SLAM and nectin-4, for cell entry, unlike other parainfluenza viruses. Vaccine strains bind CD46, contributing to their reduced virulence.

Area of Science:

  • Virology
  • Molecular Biology
  • Immunology

Background:

  • Parainfluenza viruses utilize attachment and fusion proteins for cell entry.
  • Wild type measles virus exhibits specific cell entry mechanisms distinct from other parainfluenza viruses.

Purpose of the Study:

  • To elucidate the specific host cell receptors targeted by wild type and vaccine strains of measles virus.
  • To understand the molecular interactions governing measles virus cell entry.

Main Methods:

  • Analysis of measles virus hemagglutinin protein interactions with host cell receptors.
  • Identification of binding sites for SLAM, nectin-4, and CD46 on the hemagglutinin protein.

Main Results:

  • Wild type measles virus exclusively binds to signaling lymphocytic activation molecule (SLAM) and nectin-4.
  • SLAM binds near the hemagglutinin stalk-head junction, while nectin-4 binds to a hydrophobic groove on the head.
  • Mutated vaccine strains of measles virus hemagglutinin additionally bind CD46, correlating with viral attenuation.

Conclusions:

  • Measles virus employs a specific, multi-receptor engagement strategy for cell entry.
  • The interaction with CD46 by vaccine strains provides a molecular basis for their attenuated phenotype.

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