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Updated: Jun 25, 2026

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
Published on: July 27, 2021
Measles virus glycoprotein complex assembly, receptor attachment, and cell entry
C K Navaratnarajah1, V H J Leonard, R Cattaneo
1Mayo Clinic of Medicine, Dept. of Molecular Medicne, Virology and Gene Therapy Graduate Track, Rochester, MN 55905, USA.
Abstract:
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 glycoprotein complex of paramyxoviruses in general.
Insights
Measles virus uses hemagglutinin (H) and fusion (F) proteins to enter cells. Research focuses on how H protein receptor binding triggers conformational changes for cell entry, advancing paramyxovirus fusion understanding.
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- Measles virus (MV) entry involves cell surface membrane fusion mediated by hemagglutinin (H) and fusion (F) glycoproteins.
- The H protein binds to cellular receptors, initiating fusion via the F protein.
Purpose of the Study:
- To characterize receptor-specific conformational changes in the MV H protein dimer.
- To understand how these changes transmit to the F protein trimer, mediating viral entry.
- To explore targeting MV attachment and entry via engineered H proteins.
Main Methods:
- Characterization of receptor binding footprints on the H protein.
- Analysis of conformational changes in the H protein dimer upon receptor interaction.
- Investigating the transmission of these changes to the F protein trimer.
Main Results:
- MV H protein interacts with at least three receptors: signaling lymphocyte activation molecule (SLAM, CD150), membrane cofactor protein (MCP, CD46), and an unidentified epithelial cell receptor (EpR).
- Receptor-specific conformational alterations in the H protein dimer are crucial for triggering membrane fusion.
- Engineered H proteins can direct MV entry to specific receptors.
Conclusions:
- Understanding receptor-H protein interactions is key to deciphering MV cell entry mechanisms.
- These findings advance the general understanding of paramyxovirus glycoprotein-mediated membrane fusion.
- Targeting H protein-receptor interactions offers potential strategies for controlling MV infection.
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