Measles virus glycoprotein complex assembly, receptor attachment, and cell entry

C. K. Navaratnarajah, V. H.J. Leonard, R. Cattaneo

Research output: Chapter in Book/Report/Conference proceedingChapter

55 Scopus citations


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.

Original languageEnglish (US)
Title of host publicationMeasles
Subtitle of host publicationHistory and Basic Biology
PublisherSpringer Verlag
Number of pages18
ISBN (Print)9783540705222
StatePublished - 2009

Publication series

NameCurrent Topics in Microbiology and Immunology
ISSN (Print)0070-217X

ASJC Scopus subject areas

  • Immunology and Allergy
  • Microbiology
  • Immunology
  • Microbiology (medical)


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