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-Structure paper
タイトル | Structural and molecular basis for Ebola virus neutralization by protective human antibodies. |
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ジャーナル・号・ページ | Science, Vol. 351, Issue 6279, Page 1343-1346, Year 2016 |
掲載日 | 2016年3月18日 |
著者 | 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 要旨 | 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. |
リンク | Science / PubMed:26917592 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 1.973 - 7.2 Å |
構造データ | EMDB-3310: EMDB-3311: PDB-5fha: PDB-5fhb: PDB-5fhc: |
化合物 | ChemComp-HOH: ChemComp-EDO: ChemComp-ACT: |
由来 |
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キーワード | IMMUNE SYSTEM / Ig domain / Fab / VIRAL PROTEIN/IMMUNE SYSTEM / fusion / ebola virus / glycoprotein / GP / VIRAL PROTEIN-IMMUNE SYSTEM complex |