Aviadenovirus structure: A highly thermostable capsid in the absence of stabilizing proteins

Title (eng)
Aviadenovirus structure: A highly thermostable capsid in the absence of stabilizing proteins
Author
Marta Pérez-Illana
Author
Mercedes Hernando-Pérez
Author
Gabriela N. Condezo
Author
Alberto Paradela
Author
Marta Martínez
Author
Roberto Marabini
Abstract (eng)
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.
Keywords (eng)
Viral StructureProtein InteractionsMonomersBird GenomicsProtein StructureVirionsAdenovirusesViral Packaging
Type (eng)
Language
[eng]
Is in series
Title (eng)
PLOS Pathogens
Volume
21
Issue
10
ISSN
1553-7374
Issued
2025
Number of pages
29
Publication
Public Library of Science
Date issued
2025
Access rights (eng)
Rights statement (eng)
© 2025 Pérez-Illana et al