Mutations in the stalk region of the measles virus hemagglutinin inhibit syncytium formation but not virus entry

Matthew K. Ennis, Chunling Hu, Shruthi K. Naik, Louay K. Hallak, Kah-Whye Peng, Stephen J Russell, David M Dingli

Research output: Contribution to journalArticle

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Abstract

Measles virus (MV) entry requires at least 2 viral proteins, the hemagglutinin (H) and fusion (F) proteins. We describe the rescue and characterization of a measles virus with a specific mutation in the stalk region of H (I98A) that is able to bind normally to cells but infects at a lower rate than the wild type due to a reduction in fusion triggering. The mutant H protein binds to F more avidly than the parent H protein does, and the corresponding virus is more sensitive to inhibition by fusion-inhibitory peptide. We show that after binding of MV to its receptor, H-F dissociation is required for productive infection.

Original languageEnglish (US)
Pages (from-to)10913-10917
Number of pages5
JournalJournal of Virology
Volume84
Issue number20
DOIs
StatePublished - Oct 2010

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Measles virus
Virus Internalization
Hemagglutinins
giant cells
hemagglutinins
Giant Cells
mutation
viruses
Mutation
Viral Hemagglutinins
proteins
viral proteins
Viral Proteins
Mutant Proteins
Proteins
peptides
Viruses
mutants
Peptides
receptors

ASJC Scopus subject areas

  • Immunology
  • Virology

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Mutations in the stalk region of the measles virus hemagglutinin inhibit syncytium formation but not virus entry. / Ennis, Matthew K.; Hu, Chunling; Naik, Shruthi K.; Hallak, Louay K.; Peng, Kah-Whye; Russell, Stephen J; Dingli, David M.

In: Journal of Virology, Vol. 84, No. 20, 10.2010, p. 10913-10917.

Research output: Contribution to journalArticle

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