7L30

Binjari virus (BinJV)

7L30 の概要

• エントリーDOI: 10.2210/pdb7l30/pdb
• EMDBエントリー: 23147
• 分子名称: Envelope protein E, prM protein (2 entities in total)
• 機能のキーワード: flavivirus, glycoprotein, fusion, virus
• 由来する生物種: Binjari virus; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 217325.68

構造登録者

Hardy, J.M.,Venugopal, H.V.,Newton, N.D.,Watterson, D.,Coulibaly, F.J. (登録日: 2020-12-17, 公開日: 2021-03-10, 最終更新日: 2024-11-20)

主引用文献

Newton, N.D.,Hardy, J.M.,Modhiran, N.,Hugo, L.E.,Amarilla, A.A.,Bibby, S.,Venugopal, H.,Harrison, J.J.,Traves, R.J.,Hall, R.A.,Hobson-Peters, J.,Coulibaly, F.,Watterson, D.
The structure of an infectious immature flavivirus redefines viral architecture and maturation.
Sci Adv, 7:-, 2021

PubMed Abstract: Flaviviruses are the cause of severe human diseases transmitted by mosquitoes and ticks. These viruses use a potent fusion machinery to enter target cells that needs to be restrained during viral assembly and egress. A molecular chaperone, premembrane (prM) maintains the virus particles in an immature, fusion-incompetent state until they exit the cell. Taking advantage of an insect virus that produces particles that are both immature and infectious, we determined the structure of the first immature flavivirus with a complete spike by cryo-electron microscopy. Unexpectedly, the prM chaperone forms a supporting pillar that maintains the immature spike in an asymmetric and upright state, primed for large rearrangements upon acidification. The collapse of the spike along a path defined by the prM chaperone is required, and its inhibition by a multivalent immunoglobulin M blocks infection. The revised architecture and collapse model are likely to be conserved across flaviviruses.

PubMed: 33990320
DOI: 10.1126/sciadv.abe4507

実験手法

ELECTRON MICROSCOPY (4.4 Å)