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Canine distemper virus envelope protein interactions modulated by hydrophobic residues in the fusion protein globular head.
Type of publication
Peer-reviewed
Publikationsform
Original article (peer-reviewed)
Author
Avila Mislay, Khosravi Mojtaba, Alves Lisa, Ader-Ebert Nadine, Bringolf Fanny, Zurbriggen Andreas, Plemper Richard K, Plattet Philippe,
Project
Unraveling Paramyxovirus Cell Entry
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Original article (peer-reviewed)
Journal
Journal of virology
Volume (Issue)
89(2)
Page(s)
1445 - 51
Title of proceedings
Journal of virology
DOI
10.1128/jvi.01828-14
Abstract
Membrane fusion for morbillivirus cell entry relies on critical interactions between the viral fusion (F) and attachment (H) envelope glycoproteins. Through extensive mutagenesis of an F cavity recently proposed to contribute to F's interaction with the H protein, we identified two neighboring hydrophobic residues responsible for severe F-to-H binding and fusion-triggering deficiencies when they were mutated in combination. Since both residues reside on one side of the F cavity, the data suggest that H binds the F globular head domain sideways.
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