3JCX

Canine Parvovirus complexed with Fab E

3JCX の概要

• エントリーDOI: 10.2210/pdb3jcx/pdb
• EMDBエントリー: 6629
• 分子名称: Capsid protein 2, Fab E heavy chain, Fab E light chain (3 entities in total)
• 機能のキーワード: parvovirus, antibody, virus-immune system complex, virus/immune system
• 由来する生物種: Canine parvovirus (CPV-2); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 89267.99

構造登録者

Organtini, L.J.,Iketani, S.,Huang, K.,Ashley, R.E.,Makhov, A.M.,Conway, J.F.,Parrish, C.R.,Hafenstein, S. (登録日: 2016-03-21, 公開日: 2016-07-20, 最終更新日: 2024-11-06)

主引用文献

Organtini, L.J.,Lee, H.,Iketani, S.,Huang, K.,Ashley, R.E.,Makhov, A.M.,Conway, J.F.,Parrish, C.R.,Hafenstein, S.
Near-Atomic Resolution Structure of a Highly Neutralizing Fab Bound to Canine Parvovirus.
J.Virol., 90:9733-9742, 2016

PubMed Abstract: Canine parvovirus (CPV) is a highly contagious pathogen that causes severe disease in dogs and wildlife. Previously, a panel of neutralizing monoclonal antibodies (MAb) raised against CPV was characterized. An antibody fragment (Fab) of MAb E was found to neutralize the virus at low molar ratios. Using recent advances in cryo-electron microscopy (cryo-EM), we determined the structure of CPV in complex with Fab E to 4.1 Å resolution, which allowed de novo building of the Fab structure. The footprint identified was significantly different from the footprint obtained previously from models fitted into lower-resolution maps. Using single-chain variable fragments, we tested antibody residues that control capsid binding. The near-atomic structure also revealed that Fab binding had caused capsid destabilization in regions containing key residues conferring receptor binding and tropism, which suggests a mechanism for efficient virus neutralization by antibody. Furthermore, a general technical approach to solving the structures of small molecules is demonstrated, as binding the Fab to the capsid allowed us to determine the 50-kDa Fab structure by cryo-EM.

PubMed: 27535057
DOI: 10.1128/JVI.01112-16

実験手法

ELECTRON MICROSCOPY (4.1 Å)