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Structural and molecular basis for Ebola virus neutralization by protective human antibodies.

Misasi J, Gilman MS, Kanekiyo M, Gui M, Cagigi A, Mulangu S, Corti D, Ledgerwood JE, Lanzavecchia A, Cunningham J, Muyembe-Tamfun JJ, Baxa U, Graham BS, Xiang Y, Sullivan NJ, McLellan JS
Science 351 1343-6 (2016)
Related entries: 5fha, 5fhb

Cited: 114 times
EuropePMC logo PMID: 26917592

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.

Reviews - 5fhc mentioned but not cited (2)

  1. Antibodies to combat viral infections: development strategies and progress. Pantaleo G, Correia B, Fenwick C, Joo VS, Perez L. Nat Rev Drug Discov 21 676-696 (2022)
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Articles - 5fhc mentioned but not cited (8)

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Reviews citing this publication (28)

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