5VK2
Structural basis for antibody-mediated neutralization of Lassa virus
Summary for 5VK2
Entry DOI | 10.2210/pdb5vk2/pdb |
Descriptor | Pre-glycoprotein polyprotein GP complex, Fab 37.7H heavy chain, Fab 37.7H light chain, ... (9 entities in total) |
Functional Keywords | lassa, glycoprotein, arenavirus, antibody, viral protein-immune system complex, viral protein/immune system |
Biological source | Lassa virus (LASV) More |
Total number of polymer chains | 12 |
Total formula weight | 299802.02 |
Authors | Hastie, K.M.,Zandonatti, M.A.,Kleinfelter, L.M.,Rowland, M.L.,Rowland, M.M.,Chandra, K.,Branco, L.M.,Robinson, J.E.,Garry, R.F.,Saphire, E.O. (deposition date: 2017-04-20, release date: 2017-05-31, Last modification date: 2024-10-23) |
Primary citation | Hastie, K.M.,Zandonatti, M.A.,Kleinfelter, L.M.,Heinrich, M.L.,Rowland, M.M.,Chandran, K.,Branco, L.M.,Robinson, J.E.,Garry, R.F.,Saphire, E.O. Structural basis for antibody-mediated neutralization of Lassa virus. Science, 356:923-928, 2017 Cited by PubMed Abstract: The arenavirus Lassa causes severe hemorrhagic fever and a significant disease burden in West Africa every year. The glycoprotein, GPC, is the sole antigen expressed on the viral surface and the critical target for antibody-mediated neutralization. Here we present the crystal structure of the trimeric, prefusion ectodomain of Lassa GP bound to a neutralizing antibody from a human survivor at 3.2-angstrom resolution. The antibody extensively anchors two monomers together at the base of the trimer, and biochemical analysis suggests that it neutralizes by inhibiting conformational changes required for entry. This work illuminates pH-driven conformational changes in both receptor-binding and fusion subunits of Lassa virus, illustrates the unique assembly of the arenavirus glycoprotein spike, and provides a much-needed template for vaccine design against these threats to global health. PubMed: 28572385DOI: 10.1126/science.aam7260 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.201 Å) |
Structure validation
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