2026-06-14T03:35:55Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/99942024-09-27T21:55:17Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609
Repisalud
author
Luque, Daniel
author
Gómez-Blanco, Josué
author
Garriga, Damiá
author
Brilot, Axel F
author
González, José M
author
Havens, Wendy M
author
Carrascosa, José L
author
Trus, Benes L
author
Verdaguer, Nuria
author
Ghabrial, Said A
author
Castón, José R
funder
National Institutes of Health (Estados Unidos)
funder
Instituto de Salud Carlos III
2020-05-08T12:34:16Z
2020-05-08T12:34:16Z
2014-05-27
Proc Natl Acad Sci U S A. 2014 May 27;111(21):7641-6.
10.1073/pnas.1404330111
1091-6490
0027-8424
Proceedings of the National Academy of Sciences of the United States of America
24821769
http://hdl.handle.net/20.500.12105/9994
Viruses evolve so rapidly that sequence-based comparison is not suitable for detecting relatedness among distant viruses. Structure-based comparisons suggest that evolution led to a small number of viral classes or lineages that can be grouped by capsid protein (CP) folds. Here, we report that the CP structure of the fungal dsRNA Penicillium chrysogenum virus (PcV) shows the progenitor fold of the dsRNA virus lineage and suggests a relationship between lineages. Cryo-EM structure at near-atomic resolution showed that the 982-aa PcV CP is formed by a repeated α-helical core, indicative of gene duplication despite lack of sequence similarity between the two halves. Superimposition of secondary structure elements identified a single "hotspot" at which variation is introduced by insertion of peptide segments. Structural comparison of PcV and other distantly related dsRNA viruses detected preferential insertion sites at which the complexity of the conserved α-helical core, made up of ancestral structural motifs that have acted as a skeleton, might have increased, leading to evolution of the highly varied current structures. Analyses of structural motifs only apparent after systematic structural comparisons indicated that the hallmark fold preserved in the dsRNA virus lineage shares a long (spinal) α-helix tangential to the capsid surface with the head-tailed phage and herpesvirus viral lineage.
eng
3D cryo-EM
chrysovirus
structural homology
virus evolution
Cryo-EM near-atomic structure of a dsRNA fungal virus shows ancient structural motifs preserved in the dsRNA viral lineage
journal article
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CryoEMNearAtomic_2014.pdf.txt