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

High-resolution structural studies have mainly focused on two out of the six adenovi¬rus 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,...

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Detalles Bibliográficos
Autores: Pérez-Illana, Marta, Schachner, Anna, Hernando-Pérez, Mercedes, Condezo, Gabriela N., Paradela, Alberto, Martínez, Marta, Marabini Ruiz, Roberto, Hess, Michael, San Martín, Carmen
Tipo de recurso: artículo
Fecha de publicación:2025
País:España
Institución:Universidad Autónoma de Madrid
Repositorio:Biblos-e Archivo. Repositorio Institucional de la UAM
Idioma:inglés
OAI Identifier:oai:dnet:biblosearchi::192a4e2ea81354c7bb6be53c93b033d1
Acceso en línea:https://hdl.handle.net/10486/777420
https://dx.doi.org/10.1371/journal.ppat.1013553
Access Level:acceso abierto
Palabra clave:Adenoviridae Infections
Animals
Aviadenovirus
Capsid
Capsid Proteins
Virion
Informática
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spelling Aviadenovirus structure: a highly thermostable capsid in the absence of stabilizing proteinsPérez-Illana, MartaSchachner, AnnaHernando-Pérez, MercedesCondezo, Gabriela N.Paradela, AlbertoMartínez, MartaMarabini Ruiz, RobertoHess, MichaelSan Martín, CarmenAdenoviridae InfectionsAnimalsAviadenovirusCapsidCapsid ProteinsVirionInformáticaHigh-resolution structural studies have mainly focused on two out of the six adenovi¬rus 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 parti¬cles, 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 vectorsWork supported by grants from the Spanish State Research Agency (Agencia Estatal de Investigación), with co-funding from the European Regional Development Fund (BFU2013-41249-P/AEI/10.13039/501100011033, BFU2016-74868-P/AEI/10.13039/501100011033, PID2019-104098GB-I00/AEI/10.13039/501100011033 and PID2022-136456NB-I00/AEI/10.13039/501100011033) to CSM., and the Christian Doppler Research Association (grant no: 189) to MH (IPOV). CSM further acknowledges support by the European Innovation Council (Horizon Europe) under grant agreement No 101098647 (project iAds), and Marie Skłodowska-Curie Actions (grant agreement 101129778, project INVECTA). The CSM group is a member of the Spanish Adenovirus Network (RED2022-134221-T/AEI/10.13039/501100011033), CSIC LifeHub, and CSIC BCBHub. The CNB-CSIC was further supported by AEI Severo Ochoa Excellence grants SEV-2013-0347/AEI/10.13039/501100011033, SEV-2017-0712/AEI/10.13039/501100011033 and CEX2023-001386-S/AEI/10.13039/501100011033. MP-I was supported by a predoctoral contract from La Caixa Foundation (ID 100010434), under agreement LCF/BQ/SO16/52270032), and by the VIRMAT project from the Madrid Regional Government and the REACT-EU program. MH-P holds a Ramón y Cajal posi¬tion (RyC2021-030929-I) funded by MCIN/AEI/10.13039/501100011033 and European Union NextGeneration EU/PRTR. MH-P also acknowledges grant PID2023-151078OB-I00 funded by MCIN/AEI/10.13039/501100011033 and the European Union NextGenerationEU/PRTR. The funders had no role in study design, data collection and analysis, decision to pub¬lish, or preparation of the manuscriptPublic Library of ScienceDepartamento de Ingeniería InformáticaEscuela Politécnica SuperiorGobierno de EspañaEuropean Commission20252025-10-09research articlehttp://purl.org/coar/resource_type/c_2df8fbb1VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/10486/777420https://dx.doi.org/10.1371/journal.ppat.101355341066551reponame:Biblos-e Archivo. Repositorio Institucional de la UAMinstname:Universidad Autónoma de MadridInglésengopen accesshttp://purl.org/coar/access_right/c_abf2info:eu-repo/semantics/openAccessoai:dnet:biblosearchi::192a4e2ea81354c7bb6be53c93b033d12026-06-23T12:46:27Z
dc.title.none.fl_str_mv Aviadenovirus structure: a highly thermostable capsid in the absence of stabilizing proteins
title Aviadenovirus structure: a highly thermostable capsid in the absence of stabilizing proteins
spellingShingle Aviadenovirus structure: a highly thermostable capsid in the absence of stabilizing proteins
Pérez-Illana, Marta
Adenoviridae Infections
Animals
Aviadenovirus
Capsid
Capsid Proteins
Virion
Informática
title_short Aviadenovirus structure: a highly thermostable capsid in the absence of stabilizing proteins
title_full Aviadenovirus structure: a highly thermostable capsid in the absence of stabilizing proteins
title_fullStr Aviadenovirus structure: a highly thermostable capsid in the absence of stabilizing proteins
title_full_unstemmed Aviadenovirus structure: a highly thermostable capsid in the absence of stabilizing proteins
title_sort Aviadenovirus structure: a highly thermostable capsid in the absence of stabilizing proteins
dc.creator.none.fl_str_mv Pérez-Illana, Marta
Schachner, Anna
Hernando-Pérez, Mercedes
Condezo, Gabriela N.
Paradela, Alberto
Martínez, Marta
Marabini Ruiz, Roberto
Hess, Michael
San Martín, Carmen
author Pérez-Illana, Marta
author_facet Pérez-Illana, Marta
Schachner, Anna
Hernando-Pérez, Mercedes
Condezo, Gabriela N.
Paradela, Alberto
Martínez, Marta
Marabini Ruiz, Roberto
Hess, Michael
San Martín, Carmen
author_role author
author2 Schachner, Anna
Hernando-Pérez, Mercedes
Condezo, Gabriela N.
Paradela, Alberto
Martínez, Marta
Marabini Ruiz, Roberto
Hess, Michael
San Martín, Carmen
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Departamento de Ingeniería Informática
Escuela Politécnica Superior
Gobierno de España
European Commission
dc.subject.none.fl_str_mv Adenoviridae Infections
Animals
Aviadenovirus
Capsid
Capsid Proteins
Virion
Informática
topic Adenoviridae Infections
Animals
Aviadenovirus
Capsid
Capsid Proteins
Virion
Informática
description High-resolution structural studies have mainly focused on two out of the six adenovi¬rus 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 parti¬cles, 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
publishDate 2025
dc.date.none.fl_str_mv 2025
2025-10-09
dc.type.none.fl_str_mv research article
http://purl.org/coar/resource_type/c_2df8fbb1
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/10486/777420
https://dx.doi.org/10.1371/journal.ppat.1013553
41066551
url https://hdl.handle.net/10486/777420
https://dx.doi.org/10.1371/journal.ppat.1013553
identifier_str_mv 41066551
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Public Library of Science
publisher.none.fl_str_mv Public Library of Science
dc.source.none.fl_str_mv reponame:Biblos-e Archivo. Repositorio Institucional de la UAM
instname:Universidad Autónoma de Madrid
instname_str Universidad Autónoma de Madrid
reponame_str Biblos-e Archivo. Repositorio Institucional de la UAM
collection Biblos-e Archivo. Repositorio Institucional de la UAM
repository.name.fl_str_mv
repository.mail.fl_str_mv
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