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8ROQ

FAdV-C4 Aviadenovirus structure, strain KR5

Summary for 8ROQ
Entry DOI10.2210/pdb8roq/pdb
EMDB information19401
DescriptorHexon protein, Penton protein, PIIIa, ... (4 entities in total)
Functional Keywordsadenovirus, fowl, highly thermostable, virus
Biological sourceFowl aviadenovirus C
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Total number of polymer chains16
Total formula weight1450096.32
Authors
Perez-Illana, M.P.,Schachnner, A.,Condezo, G.N.,Hernando-Perez, M.,Martinez, M.,Marabini, R.,Hess, M.,San Martin, C. (deposition date: 2024-01-12, release date: 2025-01-29, Last modification date: 2025-10-22)
Primary citationPerez-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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

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