8ROQ

FAdV-C4 Aviadenovirus structure, strain KR5

8ROQ の概要

• エントリーDOI: 10.2210/pdb8roq/pdb
• EMDBエントリー: 19401
• 分子名称: Hexon protein, Penton protein, PIIIa, ... (4 entities in total)
• 機能のキーワード: adenovirus, fowl, highly thermostable, virus
• 由来する生物種: Fowl aviadenovirus C; 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 1450096.32

構造登録者

Perez-Illana, M.P.,Schachnner, A.,Condezo, G.N.,Hernando-Perez, M.,Martinez, M.,Marabini, R.,Hess, M.,San Martin, C. (登録日: 2024-01-12, 公開日: 2025-01-29, 最終更新日: 2025-10-22)

主引用文献

Perez-Illana, M.,Schachner, A.,Hernando-Perez, M.,Condezo, G.N.,Paradela, A.,Martinez, M.,Marabini, R.,Hess, M.,San Martin, C.
Aviadenovirus structure: A highly thermostable capsid in the absence of stabilizing proteins.
Plos Pathog., 21:e1013553-e1013553, 2025

PubMed Abstract: High-resolution structural studies have mainly focused on two out of the six adenovirus genera: mastadenoviruses and atadenoviruses. Here we report the high-resolution structure of an aviadenovirus, the poultry pathogen fowl adenovirus serotype 4 (FAdV-C4). FAdV-C4 virions are highly thermostable, despite lacking minor coat and core proteins shown to stabilize the mast- and atadenovirus particles, having no genus-specific cementing proteins, and packaging a 25% longer genome. Unique structural features of the FAdV-C4 hexon include a large insertion at the trimer equatorial region, and a long N-terminal tail. Protein IIIa conformation is closer to atadenoviruses than to mastadenoviruses, while protein VIII diverges from all previously reported structures. We interpret these differences in light of adenovirus evolution. Finally, we discuss the possible role of core composition in determining capsid stability properties. These results enlarge our view on the structural diversity of adenoviruses, and provide useful information to counteract fowl pathogens or use non-human adenoviruses as vectors.

PubMed: 41066551
DOI: 10.1371/journal.ppat.1013553

実験手法

ELECTRON MICROSCOPY (3.4 Å)