Near-atomic structure of an atadenovirus reveals a conserved capsid-binding motif and intergenera variations in cementing proteins
| Autor: | Carmen San Martín, Roberto Marabini, Mart Krupovic, Josué Gómez-Blanco, Rosa Menéndez-Conejero, Gabriela N. Condezo |
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| Přispěvatelé: | Universidad Autónoma de Madrid (UAM), Centro Nacional de Biotecnología [Madrid] (CNB-CSIC), Consejo Superior de Investigaciones Científicas [Madrid] (CSIC), Virologie des archées - Archaeal Virology, Institut Pasteur [Paris] (IP), This work is supported by the Spanish Agencia Estatal de Investigación and European Regional Development Fund (BFU2016-74868-P and PID2019-104098GB-I00/AEI/10.13039/501100011033), the Ministerio de Economía y Competitividad of Spain (BFU2013-41249-P and BIO2015-68990-REDT), and the Agencia Estatal CSIC (2019AEP045). The CNB-CSIC is further supported by a Severo Ochoa Excellence grant (SEV 2017-0712). M.K. was supported by the Emergence(s) program from City of Paris (grant MEMREMA)., Universidad Autonoma de Madrid (UAM), Institut Pasteur [Paris], UAM. Departamento de Ingeniería Informática, Tratamiento de Señales Biomédicas (ING EPS-011) |
| Rok vydání: | 2021 |
| Předmět: |
viruses
Atadenovirus Bacteriophage 03 medical and health sciences Structural Biology Virology Gene duplication Coat Proteins Research Articles Tropism 030304 developmental biology Informática 0303 health sciences Multidisciplinary biology Chemistry 030302 biochemistry & molecular biology SciAdv r-articles biology.organism_classification 3. Good health Cell biology Mastadenovirus Capsid [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology sense organs Research Article |
| Zdroj: | Science Advances Science Advances, 2021, 7 (14), pp.eabe6008. ⟨10.1126/sciadv.abe6008⟩ Science Advances, American Association for the Advancement of Science (AAAS), 2021, 7 (14), pp.eabe6008. ⟨10.1126/sciadv.abe6008⟩ Biblos-e Archivo. Repositorio Institucional de la UAM instname |
| ISSN: | 2375-2548 |
| DOI: | 10.1126/sciadv.abe6008 |
| Popis: | The first high-resolution structure of an adenovirus with nonmammalian host provides information on adenovirus evolution. 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. |
| Databáze: | OpenAIRE |
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