Measles pp 59-76 | Cite as

Measles Virus Glycoprotein Complex Assembly, Receptor Attachment, and Cell Entry

  • C. K. Navaratnarajah
  • V. H. J. Leonard
  • R. CattaneoEmail author
Part of the Current Topics in Microbiology and Immunology book series (CT MICROBIOLOGY, volume 329)

Measles virus (MV) enters cells by membrane fusion at the cell surface at neutral pH. Two glycoproteins mediate this process: the hemagglutinin (H) and fusion (F) proteins. The H-protein binds to receptors, while the F-protein mediates fusion of the viral and cellular membranes. H naturally interacts with at least three different receptors. The wild-type virus primarily uses the signaling lymphocyte activation molecule (SLAM, CD150) expressed on certain lymphatic cells, while the vaccine strain has gained the ability to also use the ubiquitous membrane cofactor protein (MCP, CD46), a regulator of complement activation. Additionally, MV infects polarized epithelial cells through an unidentified receptor (EpR). The footprints of the three receptors on H have been characterized, and the focus of research is shifting to the characterization of receptor-specific conformational changes that occur in the H-protein dimer and how these are transmitted to the F-protein trimer. It was also shown that MV attachment and cell entry can be readily targeted to designated receptors by adding specificity determinants to the H-protein. These studies have contributed to our understanding of membrane fusion by the glycopro-tein complex of paramyxoviruses in general.


Newcastle Disease Virus Measle Virus Cell Entry Purine Nucleoside Phosphorylase Fusion Activation 
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Copyright information

© Springer-Verlag Berlin Heidelberg 2009

Authors and Affiliations

  • C. K. Navaratnarajah
    • 1
  • V. H. J. Leonard
    • 1
  • R. Cattaneo
    • 1
    Email author
  1. 1.Mayo Clinic College of Medicine, Dept. of Molecular MedicineVirology and Gene Therapy Graduate Track, 200 1st St SWRochesterUSA

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