7NXR

Structure of the C-terminal domain of the pORF19 capsid protein from murid gammaherpesvirus 68 (MuHV-68)

7NXR の概要

• エントリーDOI: 10.2210/pdb7nxr/pdb
• 関連するPDBエントリー: 7NXP 7NXQ
• 分子名称: Capsid vertex component 2 (2 entities in total)
• 機能のキーワード: herpesvirus, capsid, muhv-68, assembly, viral protein
• 由来する生物種: Murid herpesvirus 4 (MuHV-4, Murine gammaherpesvirus 68, Murid herpesvirus 68)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47935.61

構造登録者

Naniima, P.,Legrand, P.,Krey, T. (登録日: 2021-03-19, 公開日: 2021-10-13, 最終更新日: 2024-05-01)

主引用文献

Naniima, P.,Naimo, E.,Koch, S.,Curth, U.,Alkharsah, K.R.,Stroh, L.J.,Binz, A.,Beneke, J.M.,Vollmer, B.,Boning, H.,Borst, E.M.,Desai, P.,Bohne, J.,Messerle, M.,Bauerfeind, R.,Legrand, P.,Sodeik, B.,Schulz, T.F.,Krey, T.
Assembly of infectious Kaposi's sarcoma-associated herpesvirus progeny requires formation of a pORF19 pentamer.
Plos Biol., 19:e3001423-e3001423, 2021

PubMed Abstract: Herpesviruses cause severe diseases particularly in immunocompromised patients. Both genome packaging and release from the capsid require a unique portal channel occupying one of the 12 capsid vertices. Here, we report the 2.6 Å crystal structure of the pentameric pORF19 of the γ-herpesvirus Kaposi's sarcoma-associated herpesvirus (KSHV) resembling the portal cap that seals this portal channel. We also present the structure of its β-herpesviral ortholog, revealing a striking structural similarity to its α- and γ-herpesviral counterparts despite apparent differences in capsid association. We demonstrate pORF19 pentamer formation in solution and provide insights into how pentamerization is triggered in infected cells. Mutagenesis in its lateral interfaces blocked pORF19 pentamerization and severely affected KSHV capsid assembly and production of infectious progeny. Our results pave the way to better understand the role of pORF19 in capsid assembly and identify a potential novel drug target for the treatment of herpesvirus-induced diseases.

PubMed: 34735435
DOI: 10.1371/journal.pbio.3001423

実験手法

X-RAY DIFFRACTION (1.9 Å)