Maurer, U.E. and Zeev-Ben-Mordehai, T. and Pandurangan, Arun and Cairns, T.M. and Hannah, B.P. and Whitbeck, J.C. and Eisenberg, R.J. and Cohen, G.H. and Topf, Maya and Huiskonen, J.T. and Grünewald, K. (2013) The structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex reveals the protein-membrane and lateral protein-protein interaction. Structure 21 (8), pp. 1396-1405. ISSN 0969-2126.
|
Text
7994.pdf - Published Version of Record Available under License Creative Commons Attribution. Download (3MB) | Preview |
Abstract
Glycoprotein B (gB) is a key component of the complex herpesvirus fusion machinery. We studied membrane interaction of two gB ectodomain forms and present an electron cryotomography structure of the gB-bilayer complex. The two forms differed in presence or absence of the membrane proximal region (MPR) but showed an overall similar trimeric shape. The presence of the MPR impeded interaction with liposomes. In contrast, the MPR-lacking form interacted efficiently with liposomes. Lateral interaction resulted in coat formation on the membranes. The structure revealed that interaction of gB with membranes was mediated by the fusion loops and limited to the outer membrane leaflet. The observed intrinsic propensity of gB to cluster on membranes indicates an additional role of gB in driving the fusion process forward beyond the transient fusion pore opening and subsequently leading to fusion pore expansion.
Metadata
| Item Type: | Article |
|---|---|
| School: | Birkbeck Faculties and Schools > Faculty of Science > School of Psychological Sciences |
| Research Centres and Institutes: | Bioinformatics, Bloomsbury Centre for (Closed), Structural Molecular Biology, Institute of (ISMB) |
| Depositing User: | Administrator |
| Date Deposited: | 12 Aug 2013 11:41 |
| Last Modified: | 02 Aug 2023 17:06 |
| URI: | https://eprints.bbk.ac.uk/id/eprint/7994 |
Statistics
Additional statistics are available via IRStats2.
Archive Staff Only (login required)
