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

Misasi, J.; Gilman, M. A.; 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.

doi:10.1126/science.aad6117

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

Journal Article · Thu Feb 25 00:00:00 EST 2016 · Science

DOI:https://doi.org/10.1126/science.aad6117· OSTI ID:1249224

Misasi, J. ^[1]; Gilman, M. A. ^[2]; Kanekiyo, M. ^[3]; Gui, M. ^[4]; Cagigi, A. ^[3]; Mulangu, S. ^[3]; Corti, D. ^[5]; Ledgerwood, J. E. ^[3]; Lanzavecchia, A. ^[6]; Cunningham, J. ^[7]; Muyembe-Tamfun, J. J. ^[8]; Baxa, U. ^[9]; Graham, B. S. ^[3]; Xiang, Y. ^[4]; Sullivan, N. J. ^[3]; McLellan, J. S. ^[2]

National Institutes of Health, Bethesda, MD (United States); Harvard Medical School, Boston, MA (United States)
Geisel School of Medicine at Dartmouth, Hanover, NH (United States)
National Institutes of Health, Bethesda, MD (United States)
Tsinghua Univ., Beijing (China)
Università della Svizzera Italiana (Switzerland)
Università della Svizzera Italiana (Switzerland); Eidgenoessische Technische Hochschule, Zurich (Switzerland)
Harvard Medical School, Boston, MA (United States)
National Laboratory of Public Health (Democratic Republic of the Congo)
Frederick National Lab. for Cancer Research, Frederick, MD (United States)

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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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: USDOE Office of Science (SC)

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1249224

Journal Information:: Science, Vol. 351, Issue 6279; ISSN 0036-8075

Publisher:: AAASCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 133 works

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