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 language | English (US) |
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Pages (from-to) | 10913-10917 |
Number of pages | 5 |
Journal | Journal of virology |
Volume | 84 |
Issue number | 20 |
DOIs | |
State | Published - Oct 2010 |
ASJC Scopus subject areas
- Microbiology
- Immunology
- Insect Science
- Virology