7A56

Schmallenberg Virus Envelope Glycoprotein Gc Fusion Domains in Postfusion Conformation

7A56 の概要

• エントリーDOI: 10.2210/pdb7a56/pdb
• 分子名称: Envelopment polyprotein, CHLORIDE ION, PHOSPHATE ION, ... (6 entities in total)
• 機能のキーワード: virus entry, class ii membrane fusion protein, viral protein
• 由来する生物種: Bovine Schmallenberg virus BH80/Germany/2011
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48928.67

構造登録者

Hellert, J.,Guardado-Calvo, P.,Rey, F.A. (登録日: 2020-08-20, 公開日: 2021-09-01, 最終更新日: 2024-10-16)

主引用文献

Hellert, J.,Aebischer, A.,Haouz, A.,Guardado-Calvo, P.,Reiche, S.,Beer, M.,Rey, F.A.
Structure, function, and evolution of the Orthobunyavirus membrane fusion glycoprotein.
Cell Rep, 42:112142-112142, 2023

PubMed Abstract: La Crosse virus, responsible for pediatric encephalitis in the United States, and Schmallenberg virus, a highly teratogenic veterinary virus in Europe, belong to the large Orthobunyavirus genus of zoonotic arthropod-borne pathogens distributed worldwide. Viruses in this under-studied genus cause CNS infections or fever with debilitating arthralgia/myalgia syndromes, with no effective treatment. The main surface antigen, glycoprotein Gc (∼1,000 residues), has a variable N-terminal half (Gc) targeted by the patients' antibody response and a conserved C-terminal moiety (Gc) responsible for membrane fusion during cell entry. Here, we report the X-ray structure of post-fusion La Crosse and Schmallenberg virus Gc, revealing the molecular determinants for hairpin formation and trimerization required to drive membrane fusion. We further experimentally confirm the role of residues in the fusion loops and in a vestigial endoplasmic reticulum (ER) translocation sequence at the Gc-Gc junction. The resulting knowledge provides essential molecular underpinnings for future development of potential therapeutic treatments and vaccines.

PubMed: 36827185
DOI: 10.1016/j.celrep.2023.112142

実験手法

X-RAY DIFFRACTION (1.85 Å)