5FT2
Sub-tomogram averaging of Lassa virus glycoprotein spike from virus- like particles at pH 5
Summary for 5FT2
| Entry DOI | 10.2210/pdb5ft2/pdb |
| EMDB information | 3292 |
| Descriptor | PRE-GLYCOPROTEIN POLYPROTEIN GP COMPLEX, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | cell adhesion, membrane protein, glycoprotein, receptor binding, membrane fusion |
| Biological source | LASSA VIRUS (LASSA MAMMARENAVIRUS, LASV) |
| Cellular location | Stable signal peptide: Virion membrane ; Multi-pass membrane protein . Glycoprotein G2: Virion membrane ; Single-pass membrane protein : P08669 |
| Total number of polymer chains | 1 |
| Total formula weight | 20670.91 |
| Authors | Li, S.,Zhaoyang, S.,Pryce, R.,Parsy, M.L.,Fehling, S.K.,Schlie, K.,Siebert, C.A.,Garten, W.,Bowden, T.A.,Strecker, T.,Huiskonen, J.T. (deposition date: 2016-01-09, release date: 2016-03-02, Last modification date: 2020-07-29) |
| Primary citation | Li, S.,Sun, Z.,Pryce, R.,Parsy, M.,Fehling, S.K.,Schlie, K.,Siebert, C.A.,Garten, W.,Bowden, T.A.,Strecker, T.,Huiskonen, J.T. Acidic Ph-Induced Conformations and Lamp1 Binding of the Lassa Virus Glycoprotein Spike. Plos Pathog., 12:5418-, 2016 Cited by 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, 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. PubMed: 26849049DOI: 10.1371/JOURNAL.PPAT.1005418 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (16.4 Å) |
Structure validation
Download full validation report
