Literature DB >> 1856686

Phylogeny of capsid proteins of small icosahedral RNA plant viruses.

V V Dolja1, E V Koonin.   

Abstract

Statistically significant alignment was generated between the amino acid sequences of the (putative) shell (S) domains of the capsid proteins of small RNA plant viruses with icosahedral capsids in the tombusvirus, carmovirus, dianthovirus, sobemovirus and luteovirus groups. Inspection of the alignment showed good correspondence between the experimentally defined beta-strands and alpha-helices of the capsid proteins of tomato bushy stunt, southern bean mosaic and turnip crinkle viruses, allowing prediction of the secondary structure elements in proteins with unresolved tertiary structure. It is concluded that this set of viral capsid proteins forms a tight evolutionary cluster. Comparison of the alignment of the proteins of this family with the sequences of other capsid proteins of icosahedral RNA viruses revealed more distant similarities to the satellites of tobacco necrosis, panicum mosaic, tobacco mosaic and maize white line mosaic viruses, as well as to nepo- and comoviruses. The tentative phylogenetic tree derived from the capsid protein alignment separated into three main lineages: (I) carmo-, tombus- and dianthoviruses, (II) southern bean mosaic, tobacco necrosis and maize chlorotic mottle viruses, and (III) luteoviruses. Comparison of this tree topology with the tentative evolutionary schemes for the respective virus RNA-dependent RNA polymerases suggested that gene shuffling is the universal trend in the evolution of small RNA plant virus genomes.

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Year:  1991        PMID: 1856686     DOI: 10.1099/0022-1317-72-7-1481

Source DB:  PubMed          Journal:  J Gen Virol        ISSN: 0022-1317            Impact factor:   3.891


  19 in total

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Authors:  Lawrence Lee; Igor B Kaplan; Daniel R Ripoll; Delin Liang; Peter Palukaitis; Stewart M Gray
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5.  Insights into the selective pressures restricting Pelargonium flower break virus genome variability: Evidence for host adaptation.

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6.  A multiple alignment of the capsid protein sequences of nepoviruses and comoviruses suggests a common structure.

Authors:  O Le Gall; T Candresse; J Dunez
Journal:  Arch Virol       Date:  1995       Impact factor: 2.574

7.  Cross-linking measurements of the Potato leafroll virus reveal protein interaction topologies required for virion stability, aphid transmission, and virus-plant interactions.

Authors:  Juan D Chavez; Michelle Cilia; Chad R Weisbrod; Ho-Jong Ju; Jimmy K Eng; Stewart M Gray; James E Bruce
Journal:  J Proteome Res       Date:  2012-03-30       Impact factor: 4.466

8.  Molecular cloning and sequencing of the coat protein gene of a Nebraskan isolate of tobacco necrosis virus: the deduced coat protein sequence has only moderate homology with those of strain A and strain D.

Authors:  L Zhang; R French; W G Langenberg
Journal:  Arch Virol       Date:  1993       Impact factor: 2.574

9.  Capsid protein-mediated recruitment of host DnaJ-like proteins is required for Potato virus Y infection in tobacco plants.

Authors:  Daniel Hofius; Annette T Maier; Christof Dietrich; Isabel Jungkunz; Frederik Börnke; Edgar Maiss; Uwe Sonnewald
Journal:  J Virol       Date:  2007-08-22       Impact factor: 5.103

10.  Visualization of Host-Polerovirus Interaction Topologies Using Protein Interaction Reporter Technology.

Authors:  Stacy L DeBlasio; Juan D Chavez; Mariko M Alexander; John Ramsey; Jimmy K Eng; Jaclyn Mahoney; Stewart M Gray; James E Bruce; Michelle Cilia
Journal:  J Virol       Date:  2015-12-09       Impact factor: 5.103

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