Key result
Crystal structures of the prefusion measles virus fusion protein revealed that inhibitors AS-48 and a fusion inhibitor peptide bind the same hydrophobic pocket, suppressing membrane fusion.
Population
Measles virus fusion (F) protein (prefusion form)
Comparison
Small compound AS-48 or a fusion inhibitor peptide vs Prefusion MeV-F alone
Design
Preclinical
Authors
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May inform MeV fusion inhibitor design; leaves open translation to neurodegenerative disease therapy.
Structural analysis reveals a common hydrophobic binding pocket for MeV fusion inhibitors, providing a basis for developing treatments for MeV-induced neurodegenerative diseases.
Hashiguchi et al. (2018) studied Measles virus infection. AS-48 or fusion inhibitor peptide was evaluated on Crystal structures of prefusion MeV-F alone and in complex with inhibitors. Crystal structures of the prefusion measles virus fusion protein revealed that inhibitors AS-48 and a fusion inhibitor peptide bind the same hydrophobic pocket, suppressing membrane fusion.
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