期刊
STRUCTURE
卷 21, 期 8, 页码 1396-1405出版社
CELL PRESS
DOI: 10.1016/j.str.2013.05.018
关键词
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资金
- Deutsche Forschungsgemeinschaft (DFG) [GR1990/1-2, GR1990/1-3, GR1990/1-4, GR1990/3-1]
- Human Frontiers Science Programme (HFSP) [RGY0079/2009-C]
- Wellcome Trust [060208/Z/00/Z, 093305/Z/10/Z, 090532/Z109/Z]
- Medical Research Council Career Development Award [G0600084]
- European Molecular Biology Organisation [ALTF 820-2006]
- Academy of Finland [114649, 218080]
- National Institutes of Health USA [T32-AI07234, AI076231, AI056045, AI18289]
- Academy of Finland (AKA) [114649, 114649] Funding Source: Academy of Finland (AKA)
- Medical Research Council [G0600084] Funding Source: researchfish
- MRC [G0600084] Funding Source: UKRI
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.
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