6A9S

The crystal structure of vaccinia virus A26 (residues 1-397)

6A9S の概要

• エントリーDOI: 10.2210/pdb6a9s/pdb
• 分子名称: Protein A26, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: vaccinia virus, virus entry, acid sensitive, viral protein
• 由来する生物種: Vaccinia virus (strain Western Reserve) (VACV)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47287.76

構造登録者

Wang, H.C.,Ko, T.Z.,Luo, Y.C.,Liao, Y.T.,Chang, W. (登録日: 2018-07-16, 公開日: 2019-06-12, 最終更新日: 2024-11-20)

主引用文献

Chang, H.W.,Yang, C.H.,Luo, Y.C.,Su, B.G.,Cheng, H.Y.,Tung, S.Y.,Carillo, K.J.D.,Liao, Y.T.,Tzou, D.M.,Wang, H.C.,Chang, W.
Vaccinia viral A26 protein is a fusion suppressor of mature virus and triggers membrane fusion through conformational change at low pH.
Plos Pathog., 15:e1007826-e1007826, 2019

PubMed Abstract: Vaccinia mature virus requires A26 envelope protein to mediate acid-dependent endocytosis into HeLa cells in which we hypothesized that A26 protein functions as an acid-sensitive membrane fusion suppressor. Here, we provide evidence showing that N-terminal domain (aa1-75) of A26 protein is an acid-sensitive region that regulates membrane fusion. Crystal structure of A26 protein revealed that His48 and His53 are in close contact with Lys47, Arg57, His314 and Arg312, suggesting that at low pH these His-cation pairs could initiate conformational changes through protonation of His48 and His53 and subsequent electrostatic repulsion. All the A26 mutant mature viruses that interrupted His-cation pair interactions of His48 and His 53 indeed have lost virion infectivity. Isolation of revertant viruses revealed that second site mutations caused frame shifts and premature termination of A26 protein such that reverent viruses regained cell entry through plasma membrane fusion. Together, we conclude that viral A26 protein functions as an acid-sensitive fusion suppressor during vaccinia mature virus endocytosis.

PubMed: 31220181
DOI: 10.1371/journal.ppat.1007826

実験手法

X-RAY DIFFRACTION (1.18 Å)