5FHB
Crystal Structure of Protective Ebola Virus Antibody 100
Summary for 5FHB
| Entry DOI | 10.2210/pdb5fhb/pdb |
| Related | 5FHA 5FHC |
| Descriptor | Antibody 100 Fab heavy chain, Antibody 100 Fab light chain, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | ig domain, fab, immune system |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 2 |
| Total formula weight | 47460.65 |
| Authors | Gilman, M.S.A.,McLellan, J.S. (deposition date: 2015-12-21, release date: 2016-03-16, Last modification date: 2024-10-23) |
| Primary citation | Misasi, J.,Gilman, M.S.,Kanekiyo, M.,Gui, M.,Cagigi, A.,Mulangu, S.,Corti, D.,Ledgerwood, J.E.,Lanzavecchia, A.,Cunningham, J.,Muyembe-Tamfun, J.J.,Baxa, U.,Graham, B.S.,Xiang, Y.,Sullivan, N.J.,McLellan, J.S. Structural and molecular basis for Ebola virus neutralization by protective human antibodies. Science, 351:1343-1346, 2016 Cited by PubMed Abstract: Ebola virus causes hemorrhagic fever with a high case fatality rate for which there is no approved therapy. Two human monoclonal antibodies, mAb100 and mAb114, in combination, protect nonhuman primates against all signs of Ebola virus disease, including viremia. Here, we demonstrate that mAb100 recognizes the base of the Ebola virus glycoprotein (GP) trimer, occludes access to the cathepsin-cleavage loop, and prevents the proteolytic cleavage of GP that is required for virus entry. We show that mAb114 interacts with the glycan cap and inner chalice of GP, remains associated after proteolytic removal of the glycan cap, and inhibits binding of cleaved GP to its receptor. These results define the basis of neutralization for two protective antibodies and may facilitate development of therapies and vaccines. PubMed: 26917592DOI: 10.1126/science.aad6117 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.973 Å) |
Structure validation
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