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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


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.