Canine distemper virus envelope protein interactions modulated by hydrophobic residues in the fusion protein globular head.

Avila Sanchez, Mislay; Khosravi, Mojtaba; Alves, Lisa; Ader-Ebert, Nadine; Bringolf, Fanny Anne; Zurbriggen, Andreas; Plemper, Richard K; Plattet, Philippe (2015). Canine distemper virus envelope protein interactions modulated by hydrophobic residues in the fusion protein globular head. Journal of virology, 89(2), pp. 1445-1451. American Society for Microbiology 10.1128/JVI.01828-14

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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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