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Near-atomic structure of an atadenovirus reveals a conserved capsid-binding motif and intergenera variations in cementing proteins

Of five known adenovirus genera, high-resolution structures are available only for mammalian-infecting mastadenoviruses. We present the first high-resolution structure of an adenovirus with nonmammalian host: lizard atadenovirus LAdV-2. We find a large conformational difference in the internal verte...

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Autores principales: Marabini, Roberto, Condezo, Gabriela N., Krupovic, Mart, Menéndez-Conejero, Rosa, Gómez-Blanco, Josué, San Martín, Carmen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Association for the Advancement of Science 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8011978/
https://www.ncbi.nlm.nih.gov/pubmed/33789897
http://dx.doi.org/10.1126/sciadv.abe6008
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author Marabini, Roberto
Condezo, Gabriela N.
Krupovic, Mart
Menéndez-Conejero, Rosa
Gómez-Blanco, Josué
San Martín, Carmen
author_facet Marabini, Roberto
Condezo, Gabriela N.
Krupovic, Mart
Menéndez-Conejero, Rosa
Gómez-Blanco, Josué
San Martín, Carmen
author_sort Marabini, Roberto
collection PubMed
description Of five known adenovirus genera, high-resolution structures are available only for mammalian-infecting mastadenoviruses. We present the first high-resolution structure of an adenovirus with nonmammalian host: lizard atadenovirus LAdV-2. We find a large conformational difference in the internal vertex protein IIIa between mast- and atadenoviruses, induced by the presence of an extended polypeptide. This polypeptide, and α-helical clusters beneath the facet, likely correspond to genus-specific proteins LH2 and p32k. Another genus-specific protein, LH3, with a fold typical of bacteriophage tailspikes, contacts the capsid surface via a triskelion structure identical to that used by mastadenovirus protein IX, revealing a conserved capsid-binding motif and an ancient gene duplication event. Our data also suggest that mastadenovirus E1B-55 K was exapted from the atadenovirus-like LH3 protein. This work provides new information on the evolution of adenoviruses, emphasizing the importance of minor coat proteins for determining specific physicochemical properties of virions and most likely their tropism.
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spelling pubmed-80119782021-04-13 Near-atomic structure of an atadenovirus reveals a conserved capsid-binding motif and intergenera variations in cementing proteins Marabini, Roberto Condezo, Gabriela N. Krupovic, Mart Menéndez-Conejero, Rosa Gómez-Blanco, Josué San Martín, Carmen Sci Adv Research Articles Of five known adenovirus genera, high-resolution structures are available only for mammalian-infecting mastadenoviruses. We present the first high-resolution structure of an adenovirus with nonmammalian host: lizard atadenovirus LAdV-2. We find a large conformational difference in the internal vertex protein IIIa between mast- and atadenoviruses, induced by the presence of an extended polypeptide. This polypeptide, and α-helical clusters beneath the facet, likely correspond to genus-specific proteins LH2 and p32k. Another genus-specific protein, LH3, with a fold typical of bacteriophage tailspikes, contacts the capsid surface via a triskelion structure identical to that used by mastadenovirus protein IX, revealing a conserved capsid-binding motif and an ancient gene duplication event. Our data also suggest that mastadenovirus E1B-55 K was exapted from the atadenovirus-like LH3 protein. This work provides new information on the evolution of adenoviruses, emphasizing the importance of minor coat proteins for determining specific physicochemical properties of virions and most likely their tropism. American Association for the Advancement of Science 2021-03-31 /pmc/articles/PMC8011978/ /pubmed/33789897 http://dx.doi.org/10.1126/sciadv.abe6008 Text en Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). https://creativecommons.org/licenses/by-nc/4.0/ https://creativecommons.org/licenses/by-nc/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (https://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited.
spellingShingle Research Articles
Marabini, Roberto
Condezo, Gabriela N.
Krupovic, Mart
Menéndez-Conejero, Rosa
Gómez-Blanco, Josué
San Martín, Carmen
Near-atomic structure of an atadenovirus reveals a conserved capsid-binding motif and intergenera variations in cementing proteins
title Near-atomic structure of an atadenovirus reveals a conserved capsid-binding motif and intergenera variations in cementing proteins
title_full Near-atomic structure of an atadenovirus reveals a conserved capsid-binding motif and intergenera variations in cementing proteins
title_fullStr Near-atomic structure of an atadenovirus reveals a conserved capsid-binding motif and intergenera variations in cementing proteins
title_full_unstemmed Near-atomic structure of an atadenovirus reveals a conserved capsid-binding motif and intergenera variations in cementing proteins
title_short Near-atomic structure of an atadenovirus reveals a conserved capsid-binding motif and intergenera variations in cementing proteins
title_sort near-atomic structure of an atadenovirus reveals a conserved capsid-binding motif and intergenera variations in cementing proteins
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8011978/
https://www.ncbi.nlm.nih.gov/pubmed/33789897
http://dx.doi.org/10.1126/sciadv.abe6008
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