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-Structure paper
Title | Acidic pH-Induced Conformations and LAMP1 Binding of the Lassa Virus Glycoprotein Spike. |
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Journal, issue, pages | PLoS Pathog, Vol. 12, Issue 2, Page e1005418, Year 2016 |
Publish date | Feb 5, 2016 |
Authors | Sai Li / Zhaoyang Sun / Rhys Pryce / Marie-Laure Parsy / Sarah K Fehling / Katrin Schlie / C Alistair Siebert / Wolfgang Garten / Thomas A Bowden / Thomas Strecker / Juha T Huiskonen / |
PubMed Abstract | Lassa virus is an enveloped, bi-segmented RNA virus and the most prevalent and fatal of all Old World arenaviruses. Virus entry into the host cell is mediated by a tripartite surface spike complex, ...Lassa virus is an enveloped, bi-segmented RNA virus and the most prevalent and fatal of all Old World arenaviruses. Virus entry into the host cell is mediated by a tripartite surface spike complex, which is composed of two viral glycoprotein subunits, GP1 and GP2, and the stable signal peptide. Of these, GP1 binds to cellular receptors and GP2 catalyzes fusion between the viral envelope and the host cell membrane during endocytosis. The molecular structure of the spike and conformational rearrangements induced by low pH, prior to fusion, remain poorly understood. Here, we analyzed the three-dimensional ultrastructure of Lassa virus using electron cryotomography. Sub-tomogram averaging yielded a structure of the glycoprotein spike at 14-Å resolution. The spikes are trimeric, cover the virion envelope, and connect to the underlying matrix. Structural changes to the spike, following acidification, support a viral entry mechanism dependent on binding to the lysosome-resident receptor LAMP1 and further dissociation of the membrane-distal GP1 subunits. |
External links | PLoS Pathog / PubMed:26849049 / PubMed Central |
Methods | EM (subtomogram averaging) / EM (tomography) |
Resolution | 13.6 - 16.7 Å |
Structure data | EMDB-3290: EMDB-3291: EMDB-3292: Sub-tomogram averaging of Lassa virus glycoprotein spike from virus-like particles at pH 5 EMDB-3293: EMDB-3294: |
Chemicals | ChemComp-NAG: ChemComp-HOH: |
Source |
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Keywords | CELL ADHESION / MEMBRANE PROTEIN / GLYCOPROTEIN / RECEPTOR BINDING / MEMBRANE FUSION |