Journal
JOURNAL OF VIROLOGY
Volume 81, Issue 16, Pages 8821-8826Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.00754-07
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Funding
- NIAID NIH HHS [AI 071002, R21 AI056179, R01 AI071002-03, R01 AI071002, AI 056179] Funding Source: Medline
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In search of target sites for the development of paramyxovirus inhibitors, we have engineered disulfide bridges to introduce covalent links into the prefusion F protein trimer of measles virus. F-Edm-452C/460C, predicted to bridge head and stalk domains of different F monomers, shows a high degree of proteolytic maturation and surface expression, predominantly as stable, dithiothreitol-sensitive trimers, but no fusion activity. Reduction of disulfide bridges partially restores activity. These findings underscore the importance of reversible intersubunit interactions between the stalk and head domains for F activity. Noncovalent small molecules mimicking this behavior may constitute a potent strategy for preventing paramyxovirus entry.
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