6GSI

Feline Calicivirus Strain F9 bound to a soluble ectodomain fragment of feline junctional adhesion molecule A - leading to assembly of a portal structure at a unique three-fold axis.

6GSI の概要

• エントリーDOI: 10.2210/pdb6gsi/pdb
• 関連するPDBエントリー: 6GSH
• EMDBエントリー: 0054 0056
• 分子名称: Capsid protein, Junctional adhesion molecule A, VP2, ... (4 entities in total)
• 機能のキーワード: capsid, calicivirus, vesivirus, vp1, portal, vp2, junctional-adhesion molecule a, virus
• 由来する生物種: Felis catus (Domestic cat); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 431105.00

構造登録者

Conley, M.J.,Bhella, D. (登録日: 2018-06-14, 公開日: 2019-01-16, 最終更新日: 2025-07-09)

主引用文献

Conley, M.J.,McElwee, M.,Azmi, L.,Gabrielsen, M.,Byron, O.,Goodfellow, I.G.,Bhella, D.
Calicivirus VP2 forms a portal-like assembly following receptor engagement.
Nature, 565:377-381, 2019

PubMed Abstract: To initiate infection, many viruses enter their host cells by triggering endocytosis following receptor engagement. However, the mechanisms by which non-enveloped viruses escape the endosome are poorly understood. Here we present near-atomic-resolution cryo-electron microscopy structures for feline calicivirus both undecorated and labelled with a soluble fragment of its cellular receptor, feline junctional adhesion molecule A. We show that VP2, a minor capsid protein encoded by all caliciviruses, forms a large portal-like assembly at a unique three-fold axis of symmetry, following receptor engagement. This assembly-which was not detected in undecorated virions-is formed of twelve copies of VP2, arranged with their hydrophobic N termini pointing away from the virion surface. Local rearrangement at the portal site leads to the opening of a pore in the capsid shell. We hypothesize that the portal-like assembly functions as a channel for the delivery of the calicivirus genome, through the endosomal membrane, into the cytoplasm of a host cell, thereby initiating infection. VP2 was previously known to be critical for the production of infectious virus; our findings provide insights into its structure and function that advance our understanding of the Caliciviridae.

PubMed: 30626974
DOI: 10.1038/s41586-018-0852-1

実験手法

ELECTRON MICROSCOPY (3.75 Å)