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


Avila, Mislay; Khosravi, Mojtaba; Alves, Lisa; Ader-Ebert, Nadine; Bringolf, Fanny; 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):1445-1451.

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.

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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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:05 Vetsuisse Faculty > Institute of Virology
Dewey Decimal Classification:570 Life sciences; biology
Language:English
Date:15 January 2015
Deposited On:30 Oct 2015 07:10
Last Modified:05 Apr 2016 19:28
Publisher:American Society for Microbiology
ISSN:0022-538X
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.1128/JVI.01828-14
PubMed ID:25355896

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