6CV3

CryoEM structure of human enterovirus D68 emptied particle

6CV3 の概要

• エントリーDOI: 10.2210/pdb6cv3/pdb
• EMDBエントリー: 7632 7633 7634 7635 7636
• 分子名称: viral protein 1, viral protein 3, viral protein 2 (3 entities in total)
• 機能のキーワード: virus, genome release, receptor
• 由来する生物種: Enterovirus D68; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 87723.56

構造登録者

Liu, Y.,Rossmann, M.G. (登録日: 2018-03-27, 公開日: 2019-07-24, 最終更新日: 2024-03-13)

主引用文献

Baggen, J.,Liu, Y.,Lyoo, H.,van Vliet, A.L.W.,Wahedi, M.,de Bruin, J.W.,Roberts, R.W.,Overduin, P.,Meijer, A.,Rossmann, M.G.,Thibaut, H.J.,van Kuppeveld, F.J.M.
Bypassing pan-enterovirus host factor PLA2G16.
Nat Commun, 10:3171-3171, 2019

PubMed Abstract: Enteroviruses are a major cause of human disease. Adipose-specific phospholipase A2 (PLA2G16) was recently identified as a pan-enterovirus host factor and potential drug target. In this study, we identify a possible mechanism of PLA2G16 evasion by employing a dual glycan receptor-binding enterovirus D68 (EV-D68) strain. We previously showed that this strain does not strictly require the canonical EV-D68 receptor sialic acid. Here, we employ a haploid screen to identify sulfated glycosaminoglycans (sGAGs) as its second glycan receptor. Remarkably, engagement of sGAGs enables this virus to bypass PLA2G16. Using cryo-EM analysis, we reveal that, in contrast to sialic acid, sGAGs stimulate genome release from virions via structural changes that enlarge the putative openings for genome egress. Together, we describe an enterovirus that can bypass PLA2G16 and identify additional virion destabilization as a potential mechanism to circumvent PLA2G16.

PubMed: 31320648
DOI: 10.1038/s41467-019-11256-z

実験手法

ELECTRON MICROSCOPY (3.56 Å)