<resource xmlns:datacite="http://datacite.org/schema/kernel-4">
<creators>
<creator>
<creatorName nameType="Personal">Marta Pérez-Illana</creatorName>
<givenName>Marta</givenName>
<familyName>Pérez-Illana</familyName>
</creator>
<creator>
<creatorName nameType="Personal">Anna Schachner</creatorName>
<givenName>Anna</givenName>
<familyName>Schachner</familyName>
</creator>
<creator>
<creatorName nameType="Personal">Mercedes Hernando-Pérez</creatorName>
<givenName>Mercedes</givenName>
<familyName>Hernando-Pérez</familyName>
</creator>
<creator>
<creatorName nameType="Personal">Gabriela N. Condezo</creatorName>
<givenName>Gabriela N.</givenName>
<familyName>Condezo</familyName>
</creator>
<creator>
<creatorName nameType="Personal">Alberto Paradela</creatorName>
<givenName>Alberto</givenName>
<familyName>Paradela</familyName>
</creator>
<creator>
<creatorName nameType="Personal">Marta Martínez</creatorName>
<givenName>Marta</givenName>
<familyName>Martínez</familyName>
</creator>
<creator>
<creatorName nameType="Personal">Roberto Marabini</creatorName>
<givenName>Roberto</givenName>
<familyName>Marabini</familyName>
</creator>
<creator>
<creatorName nameType="Personal">Michael Hess</creatorName>
<givenName>Michael</givenName>
<familyName>Hess</familyName>
</creator>
<creator>
<creatorName nameType="Personal">Carmen San Martín</creatorName>
<givenName>Carmen</givenName>
<familyName>San Martín</familyName>
</creator>
</creators>
<titles>
<title>Aviadenovirus structure: A highly thermostable capsid in the absence of stabilizing proteins</title>
</titles>
<publisher>Public Library of Science</publisher>
<publicationYear>2025</publicationYear>
<descriptions>
<description descriptionType="Other">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.</description>
</descriptions>
<resourceType resourceTypeGeneral="Text">PDFDocument</resourceType>
<language>eng</language>
<dates>
<date dateType="Created">2026-04-28T09:00:58.651751Z</date>
<date dateType="Issued">2025</date>
</dates>
<subjects>
<subject>Viral Structure</subject>
<subject>Protein Interactions</subject>
<subject>Monomers</subject>
<subject>Bird Genomics</subject>
<subject>Protein Structure</subject>
<subject>Virions</subject>
<subject>Adenoviruses</subject>
<subject>Viral Packaging</subject>
</subjects>
<sizes>
<size>3277753 b</size>
</sizes>
<formats>
<format>application/pdf</format>
</formats>
<rightsList>
<rights rightsURI="http://creativecommons.org/licenses/by/4.0/">http://creativecommons.org/licenses/by/4.0/</rights>
</rightsList>
</resource>
