5FHB

Crystal Structure of Protective Ebola Virus Antibody 100

5FHB の概要

• エントリーDOI: 10.2210/pdb5fhb/pdb
• 関連するPDBエントリー: 5FHA 5FHC
• 分子名称: Antibody 100 Fab heavy chain, Antibody 100 Fab light chain, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: ig domain, fab, immune system
• 由来する生物種: Homo sapiens; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47460.65

構造登録者

Gilman, M.S.A.,McLellan, J.S. (登録日: 2015-12-21, 公開日: 2016-03-16, 最終更新日: 2024-10-23)

主引用文献

Misasi, J.,Gilman, M.S.,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.
Structural and molecular basis for Ebola virus neutralization by protective human antibodies.
Science, 351:1343-1346, 2016

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 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.

PubMed: 26917592
DOI: 10.1126/science.aad6117

実験手法

X-RAY DIFFRACTION (1.973 Å)