Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Functional and structural interactions between measles virus hemagglutinin and CD46

O Nussbaum1, C C Broder, B Moss

  • 1Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892, USA.

Journal of Virology
|June 1, 1995
PubMed
Summary

The measles virus (MV) hemagglutinin (H) glycoprotein specifically binds human CD46, mediating viral entry into primate cells. This interaction dictates MV fusion specificity, unlike canine distemper virus (CDV) glycoproteins.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Analysis of the monkeypox virus genome.

Virology·2002
Same author

Systemic cancer therapy with a tumor-selective vaccinia virus mutant lacking thymidine kinase and vaccinia growth factor genes.

Cancer research·2001
Same author

Oligomeric structure of virion-associated and soluble forms of the simian immunodeficiency virus envelope protein in the prefusion activated conformation.

Proceedings of the National Academy of Sciences of the United States of America·2001
Same author

Human monkeypox and smallpox viruses: genomic comparison.

FEBS letters·2001
Same author

High-speed mass transit for poxviruses on microtubules.

Nature cell biology·2001
Same author

Vaccinia virus intracellular movement is associated with microtubules and independent of actin tails.

Journal of virology·2001

Area of Science:

  • Virology
  • Molecular Biology
  • Immunology

Background:

  • Measles virus (MV) and canine distemper virus (CDV) are morbilliviruses that utilize cell surface receptors for entry.
  • Human CD46 serves as the primary receptor for MV.
  • The roles of MV surface glycoproteins, hemagglutinin (H) and fusion (F), in receptor interaction and cell fusion are not fully elucidated.

Purpose of the Study:

  • To analyze the specific roles of MV H and F glycoproteins in functional and structural interactions with human CD46.
  • To determine which glycoprotein dictates MV fusion specificity and CD46 dependence.
  • To compare the interaction and specificity of MV glycoproteins with those of CDV.

Main Methods:

  • Recombinant vaccinia virus vectors were used to express MV and CDV H and F glycoproteins in cell populations.

Related Experiment Videos

  • Cell-cell fusion assays, including reporter gene activation and syncytium formation, were employed.
  • Flow cytometry and antibody coprecipitation were used to assess glycoprotein-receptor interactions.
  • Main Results:

    • MV glycoproteins mediated fusion with primate cells but not nonprimate cells, unless CD46 was present.
    • CDV glycoproteins mediated fusion with both primate and nonprimate cells independently of CD46.
    • The H glycoprotein, not F, determined the fusion specificity for both MV and CDV, with MV H specifically interacting with CD46.

    Conclusions:

    • The measles virus hemagglutinin (H) glycoprotein is critical for determining MV specificity for CD46-positive cells.
    • A direct functional and structural interaction exists between MV H and human CD46.
    • Fusion specificity in morbilliviruses is dictated by the H glycoprotein, highlighting its role in host range and entry.