5VK2

Structural basis for antibody-mediated neutralization of Lassa virus

5VK2 の概要

• エントリーDOI: 10.2210/pdb5vk2/pdb
• 分子名称: Pre-glycoprotein polyprotein GP complex, Fab 37.7H heavy chain, Fab 37.7H light chain, ... (9 entities in total)
• 機能のキーワード: lassa, glycoprotein, arenavirus, antibody, viral protein-immune system complex, viral protein/immune system
• 由来する生物種: Lassa virus (LASV); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 299802.02

構造登録者

Hastie, K.M.,Zandonatti, M.A.,Kleinfelter, L.M.,Rowland, M.L.,Rowland, M.M.,Chandra, K.,Branco, L.M.,Robinson, J.E.,Garry, R.F.,Saphire, E.O. (登録日: 2017-04-20, 公開日: 2017-05-31, 最終更新日: 2024-10-23)

主引用文献

Hastie, K.M.,Zandonatti, M.A.,Kleinfelter, L.M.,Heinrich, M.L.,Rowland, M.M.,Chandran, K.,Branco, L.M.,Robinson, J.E.,Garry, R.F.,Saphire, E.O.
Structural basis for antibody-mediated neutralization of Lassa virus.
Science, 356:923-928, 2017

PubMed Abstract: The arenavirus Lassa causes severe hemorrhagic fever and a significant disease burden in West Africa every year. The glycoprotein, GPC, is the sole antigen expressed on the viral surface and the critical target for antibody-mediated neutralization. Here we present the crystal structure of the trimeric, prefusion ectodomain of Lassa GP bound to a neutralizing antibody from a human survivor at 3.2-angstrom resolution. The antibody extensively anchors two monomers together at the base of the trimer, and biochemical analysis suggests that it neutralizes by inhibiting conformational changes required for entry. This work illuminates pH-driven conformational changes in both receptor-binding and fusion subunits of Lassa virus, illustrates the unique assembly of the arenavirus glycoprotein spike, and provides a much-needed template for vaccine design against these threats to global health.

PubMed: 28572385
DOI: 10.1126/science.aam7260

実験手法

X-RAY DIFFRACTION (3.201 Å)