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.

Item Type:

Journal Article (Original Article)

Division/Institute:

05 Veterinary Medicine > Department of Clinical Research and Veterinary Public Health (DCR-VPH) > Experimental Clinical Research
05 Veterinary Medicine > Department of Clinical Research and Veterinary Public Health (DCR-VPH)
05 Veterinary Medicine > Research Foci > NeuroCenter

Graduate School:

Graduate School for Cellular and Biomedical Sciences (GCB)

UniBE Contributor:

Avila Sanchez, Mislay; Khosravi, Mojtaba; Bringolf, Fanny Anne; Zurbriggen, Andreas and Plattet, Philippe

Subjects:

600 Technology > 630 Agriculture
500 Science > 570 Life sciences; biology

ISSN:

0022-538X

Publisher:

American Society for Microbiology

Language:

English

Submitter:

Philippe Plattet

Date Deposited:

05 Sep 2018 17:47

Last Modified:

05 Sep 2018 17:47

Publisher DOI:

10.1128/JVI.01828-14

PubMed ID:

25355896

BORIS DOI:

10.7892/boris.119803

URI:

https://boris.unibe.ch/id/eprint/119803

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