Journal: Science / Year: 2016 Title: Structural and molecular basis for Ebola virus neutralization by protective human antibodies. Authors: 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 ...Authors: 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 / 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.
History
Deposition
Jan 29, 2016
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Header (metadata) release
Feb 24, 2016
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Map release
Mar 2, 2016
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Update
Apr 13, 2016
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Current status
Apr 13, 2016
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Download / File: emd_3311.map.gz / Format: CCP4 / Size: 51.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotation
Cryo-EM reconstruction of Ebola GP-Fab100-Fab114 ternary complex at pH 5
Voxel size
X=Y=Z: 1.32 Å
Density
Contour Level
By AUTHOR: 0.0213 / Movie #1: 0.0213
Minimum - Maximum
-0.05702131 - 0.09657204
Average (Standard dev.)
0.00038889 (±0.00414544)
Symmetry
Space group: 1
Details
EMDB XML:
Map geometry
Axis order
X
Y
Z
Origin
0
0
0
Dimensions
240
240
240
Spacing
240
240
240
Cell
A=B=C: 316.80002 Å α=β=γ: 90.0 °
CCP4 map header:
mode
Image stored as Reals
Å/pix. X/Y/Z
1.32
1.32
1.32
M x/y/z
240
240
240
origin x/y/z
0.000
0.000
0.000
length x/y/z
316.800
316.800
316.800
α/β/γ
90.000
90.000
90.000
start NX/NY/NZ
-30
0
-64
NX/NY/NZ
61
61
129
MAP C/R/S
1
2
3
start NC/NR/NS
0
0
0
NC/NR/NS
240
240
240
D min/max/mean
-0.057
0.097
0.000
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Supplemental data
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Sample components
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Entire : Ebola GP binds to Fab Fragments of mAb100 and mAb114
Entire
Name: Ebola GP binds to Fab Fragments of mAb100 and mAb114
Components
Sample: Ebola GP binds to Fab Fragments of mAb100 and mAb114
Protein or peptide: Ebola virus glycoprotein
Protein or peptide: mAb100
Protein or peptide: mAb114
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Supramolecule #1000: Ebola GP binds to Fab Fragments of mAb100 and mAb114
Supramolecule
Name: Ebola GP binds to Fab Fragments of mAb100 and mAb114 / type: sample / ID: 1000 Oligomeric state: One trimer of Ebola GP binds to three fab fragments of mAb100 and three fab fragments of mAb114 Number unique components: 3
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