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

DOI
Publisher DOI
PubMed ID
25355896
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.
Date Issued
2015-01-15
Publication Type
Article
Subject(s)
Language(s)
en
Author(s)
Alves, Lisa
Ader-Ebert, Nadine
Plemper, Richard K
Additional Credits
Journal
Journal of virology
Publisher
American Society for Microbiology
ISSN
0022-538X
Access(Rights)
restricted
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