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-Structure paper
Title | Structural and molecular basis for Ebola virus neutralization by protective human antibodies. |
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Journal, issue, pages | Science, Vol. 351, Issue 6279, Page 1343-1346, Year 2016 |
Publish date | Mar 18, 2016 |
![]() | John Misasi / Morgan S A Gilman / Masaru Kanekiyo / Miao Gui / Alberto Cagigi / Sabue Mulangu / Davide Corti / Julie E Ledgerwood / Antonio Lanzavecchia / James Cunningham / Jean Jacques Muyembe-Tamfun / Ulrich Baxa / Barney S Graham / Ye Xiang / Nancy J Sullivan / Jason S McLellan / ![]() ![]() ![]() ![]() |
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 ...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. |
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Methods | EM (single particle) / X-ray diffraction |
Resolution | 1.973 - 7.2 Å |
Structure data | ![]() EMDB-3310: ![]() EMDB-3311: ![]() PDB-5fha: ![]() PDB-5fhb: ![]() PDB-5fhc: |
Chemicals | ![]() ChemComp-HOH: ![]() ChemComp-EDO: ![]() ChemComp-ACT: |
Source |
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![]() | IMMUNE SYSTEM / Ig domain / Fab / VIRAL PROTEIN/IMMUNE SYSTEM / fusion / ebola virus / glycoprotein / GP / VIRAL PROTEIN-IMMUNE SYSTEM complex |