Cardiff University | Prifysgol Caerdydd ORCA
Online Research @ Cardiff 
WelshClear Cookie - decide language by browser settings

Biochemical, biophysical and preliminary X-ray crystallographic analyses of the fusion core of Sendai virus F protein

Wang, Xiaojia, Xu, Yanhui, Cole, David ORCID: https://orcid.org/0000-0003-0028-9396, Lou, Zhiyong, Liu, Yiwei, Rao, Zihe, Wang, Ming and Gao, George F. 2004. Biochemical, biophysical and preliminary X-ray crystallographic analyses of the fusion core of Sendai virus F protein. Acta Crystallographica Section D: Biological Crystallography 60 (9) , pp. 1632-1635. 10.1107/S0907444904015872

Full text not available from this repository.

Abstract

It is emerging that enveloped viruses may adopt a unique entry/fusion mechanism; in paramyxoviruses, including Sendai virus (SeV), the attachment protein HN (or its homologue H or G) binds a cellular receptor which triggers conformational changes of its fusion protein, F. There are at least three conformations of the F protein in the current fusion model: the pre-fusion native conformation, the pre-hairpin intermediate conformation and the post-fusion coiled-coil conformation. The fusion mechanism of SeV, a member of the Paramyxoviridae family, has been well established and several structural and functional domains or modules have been proposed from studies of its F protein. However, biochemical and biophysical studies of the heptad-repeat (HR) regions (HR1 and HR2) have not been systematically carried out. HR1 and HR2 strongly interact with each other to form a stable six-helix coiled-coil bundle as the post-fusion conformation. In this study, a single-chain HR1–linker–HR2 protein of SeV was prepared in an Escherichia coli expression system and biochemical and biophysical analyses showed it to form a typical six-helix coiled-coil bundle; its trigonal crystals diffracted X-rays to 2.5 Å resolution. The crystal structure will help to reveal the structural requirements of the post-fusion coiled-coil conformation of SeV F protein.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Medicine
Systems Immunity Research Institute (SIURI)
Subjects: R Medicine > R Medicine (General)
Uncontrolled Keywords: Sendai virus; fusion core
Publisher: International Union of Crystallography
ISSN: 0907-4449
Last Modified: 25 Oct 2022 09:55
URI: https://orca.cardiff.ac.uk/id/eprint/60524

Citation Data

Cited 3 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item Edit Item