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Review

Superimposition of Viral Protein Structures: A Means to Decipher the Phylogenies of Viruses

1
Molecular and Integrative Biosciences Research Programme, Faculty of Biological and Environmental Sciences, University of Helsinki, FI-00014 Helsinki, Finland
2
Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, 48160 Derio, Spain
3
IKERBASQUE, Basque Foundation for Science, 48013 Bilbao, Spain
4
Centro de Investigación Biomédica en Red de Enfermedades Hepáticas y Digestivas (CIBERehd), Instituto de Salud Carlos III, 28029 Madrid, Spain
*
Author to whom correspondence should be addressed.
Received: 10 September 2020 / Revised: 2 October 2020 / Accepted: 2 October 2020 / Published: 9 October 2020
(This article belongs to the Special Issue In Memory of Michael Rossmann)
Superimposition of protein structures is key in unravelling structural homology across proteins whose sequence similarity is lost. Structural comparison provides insights into protein function and evolution. Here, we review some of the original findings and thoughts that have led to the current established structure-based phylogeny of viruses: starting from the original observation that the major capsid proteins of plant and animal viruses possess similar folds, to the idea that each virus has an innate “self”. This latter idea fueled the conceptualization of the PRD1-adenovirus lineage whose members possess a major capsid protein (innate “self”) with a double jelly roll fold. Based on this approach, long-range viral evolutionary relationships can be detected allowing the virosphere to be classified in four structure-based lineages. However, this process is not without its challenges or limitations. As an example of these hurdles, we finally touch on the difficulty of establishing structural “self” traits for enveloped viruses showcasing the coronaviruses but also the power of structure-based analysis in the understanding of emerging viruses View Full-Text
Keywords: virus evolution; structural similarity; double β-barrel fold; structure-based phylogeny virus evolution; structural similarity; double β-barrel fold; structure-based phylogeny
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MDPI and ACS Style

Ravantti, J.J.; Martinez-Castillo, A.; Abrescia, N.G.A. Superimposition of Viral Protein Structures: A Means to Decipher the Phylogenies of Viruses. Viruses 2020, 12, 1146. https://0-doi-org.brum.beds.ac.uk/10.3390/v12101146

AMA Style

Ravantti JJ, Martinez-Castillo A, Abrescia NGA. Superimposition of Viral Protein Structures: A Means to Decipher the Phylogenies of Viruses. Viruses. 2020; 12(10):1146. https://0-doi-org.brum.beds.ac.uk/10.3390/v12101146

Chicago/Turabian Style

Ravantti, Janne J., Ane Martinez-Castillo, and Nicola G.A. Abrescia 2020. "Superimposition of Viral Protein Structures: A Means to Decipher the Phylogenies of Viruses" Viruses 12, no. 10: 1146. https://0-doi-org.brum.beds.ac.uk/10.3390/v12101146

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