Avoidance of Protein Fold Disruption in Natural Virus Recombinants

 

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dc.contributor.author Lefeuvre, Pierre en_ZA
dc.contributor.author Lett, Jean-Michel en_ZA
dc.contributor.author Reynaud, Bernard en_ZA
dc.contributor.author Martin, Darren P en_ZA
dc.date.accessioned 2015-11-09T13:17:40Z
dc.date.available 2015-11-09T13:17:40Z
dc.date.issued 2007 en_ZA
dc.identifier.citation Lefeuvre, P., Lett, J. M., Reynaud, B., & Martin, D. P. (2007). Avoidance of protein fold disruption in natural virus recombinants. PLoS Pathog, 3(11), e181. doi:10.1371/journal.ppat.0030181 en_ZA
dc.identifier.uri http://hdl.handle.net/11427/14785
dc.identifier.uri http://dx.doi.org/10.1371/journal.ppat.0030181
dc.description.abstract Author Summary The exchange of genetic material between different virus species, called inter-species recombination, has the potential to generate, within a single genome replication cycle, an almost unimaginable number of genetically distinct virus strains, including many that might cause deadly new human, animal, or plant diseases. Many fear that inter-species recombination could provide viruses with quick access to evolutionary innovations such as broader host ranges, altered tissue tropisms, or increased severities. However, mounting evidence suggests that recombination is not an unconstrained process and that most inter-species recombinants that occur in nature are probably defective. It is suspected that networks of coevolved interactions between different parts of virus genomes and their encoded proteins must be kept intact for newly formed inter-species recombinants to have any chance of out-competing their parents. One category of coevolved interaction is that between contacting amino acids within the 3-D structures of folded proteins. Here we examine the distributions of recombination events across the genomes of a group of rampantly recombining plant viruses and find very good evidence that this class of interaction tends to be preserved amongst recombinant sequences sampled from nature. This indicates that selection against misfolded proteins strongly influences the survival of natural recombinants. en_ZA
dc.language.iso eng en_ZA
dc.publisher Public Library of Science en_ZA
dc.rights This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. en_ZA
dc.rights.uri http://creativecommons.org/licenses/by/4.0 en_ZA
dc.source PLoS One en_ZA
dc.source.uri http://journals.plos.org/plospathogens en_ZA
dc.subject.other Recombinant proteins en_ZA
dc.subject.other DNA recombination en_ZA
dc.subject.other DNA sequence analysis en_ZA
dc.subject.other Plant genomics en_ZA
dc.subject.other Sequence alignment en_ZA
dc.subject.other Structural genomics en_ZA
dc.subject.other Viral genomics en_ZA
dc.subject.other Genome evolution en_ZA
dc.title Avoidance of Protein Fold Disruption in Natural Virus Recombinants en_ZA
dc.type Journal Article en_ZA
dc.rights.holder © 2007 Lefeuvre et al en_ZA
uct.type.publication Research en_ZA
uct.type.resource Article en_ZA
dc.publisher.institution University of Cape Town
dc.publisher.faculty Faculty of Health Sciences en_ZA
dc.publisher.department Institute of Infectious Disease and Molecular Medicine en_ZA
uct.type.filetype Text
uct.type.filetype Image
dc.identifier.apacitation Lefeuvre, P., Lett, J., Reynaud, B., & Martin, D. P. (2007). Avoidance of Protein Fold Disruption in Natural Virus Recombinants. <i>PLoS One</i>, http://hdl.handle.net/11427/14785 en_ZA
dc.identifier.chicagocitation Lefeuvre, Pierre, Jean-Michel Lett, Bernard Reynaud, and Darren P Martin "Avoidance of Protein Fold Disruption in Natural Virus Recombinants." <i>PLoS One</i> (2007) http://hdl.handle.net/11427/14785 en_ZA
dc.identifier.vancouvercitation Lefeuvre P, Lett J, Reynaud B, Martin DP. Avoidance of Protein Fold Disruption in Natural Virus Recombinants. PLoS One. 2007; http://hdl.handle.net/11427/14785. en_ZA
dc.identifier.ris TY - Journal Article AU - Lefeuvre, Pierre AU - Lett, Jean-Michel AU - Reynaud, Bernard AU - Martin, Darren P AB - Author Summary The exchange of genetic material between different virus species, called inter-species recombination, has the potential to generate, within a single genome replication cycle, an almost unimaginable number of genetically distinct virus strains, including many that might cause deadly new human, animal, or plant diseases. Many fear that inter-species recombination could provide viruses with quick access to evolutionary innovations such as broader host ranges, altered tissue tropisms, or increased severities. However, mounting evidence suggests that recombination is not an unconstrained process and that most inter-species recombinants that occur in nature are probably defective. It is suspected that networks of coevolved interactions between different parts of virus genomes and their encoded proteins must be kept intact for newly formed inter-species recombinants to have any chance of out-competing their parents. One category of coevolved interaction is that between contacting amino acids within the 3-D structures of folded proteins. Here we examine the distributions of recombination events across the genomes of a group of rampantly recombining plant viruses and find very good evidence that this class of interaction tends to be preserved amongst recombinant sequences sampled from nature. This indicates that selection against misfolded proteins strongly influences the survival of natural recombinants. DA - 2007 DB - OpenUCT DO - 10.1371/journal.ppat.0030181 DP - University of Cape Town J1 - PLoS One LK - https://open.uct.ac.za PB - University of Cape Town PY - 2007 T1 - Avoidance of Protein Fold Disruption in Natural Virus Recombinants TI - Avoidance of Protein Fold Disruption in Natural Virus Recombinants UR - http://hdl.handle.net/11427/14785 ER - en_ZA


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This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Except where otherwise noted, this item's license is described as This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.