| Autor: |
Ennis MK; Department of Molecular Medicine, Mayo Clinic College of Medicine, 200 First Street SW, Rochester, MN 55905, USA., Hu C, Naik SK, Hallak LK, Peng KW, Russell SJ, Dingli D |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of virology [J Virol] 2010 Oct; Vol. 84 (20), pp. 10913-7. Date of Electronic Publication: 2010 Aug 11. |
| DOI: |
10.1128/JVI.00789-10 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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