Solenopsis invicta virus 3: Mapping of Structural Proteins, Ribosomal Frameshifting, and Similarities to Acyrthosiphon pisum virus and Kelp fly virus

Solenopsis invicta virus 3 (SINV-3) is a positive-sense single-stranded RNA virus that infects the red imported fire ant, Solenopsis invicta. We show that the second open reading frame (ORF) of the dicistronic genome is expressed via a frameshifting mechanism and that the sequences encoding the str...

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Main Authors: Valles, Steven M., Bell, Susanne, Firth, Andrew E.
Format: Online
Language:English
Published: Public Library of Science 2014
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3970965/
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recordtype oai_dc
spelling pubmed-39709652014-04-04 Solenopsis invicta virus 3: Mapping of Structural Proteins, Ribosomal Frameshifting, and Similarities to Acyrthosiphon pisum virus and Kelp fly virus Valles, Steven M. Bell, Susanne Firth, Andrew E. Research Article Solenopsis invicta virus 3 (SINV-3) is a positive-sense single-stranded RNA virus that infects the red imported fire ant, Solenopsis invicta. We show that the second open reading frame (ORF) of the dicistronic genome is expressed via a frameshifting mechanism and that the sequences encoding the structural proteins map to both ORF2 and the 3' end of ORF1, downstream of the sequence that encodes the RNA-dependent RNA polymerase. The genome organization and structural protein expression strategy resemble those of Acyrthosiphon pisum virus (APV), an aphid virus. The capsid protein that is encoded by the 3' end of ORF1 in SINV-3 and APV is predicted to have a jelly-roll fold similar to the capsid proteins of picornaviruses and caliciviruses. The capsid-extension protein that is produced by frameshifting, includes the jelly-roll fold domain encoded by ORF1 as its N-terminus, while the C-terminus encoded by the 5' half of ORF2 has no clear homology with other viral structural proteins. A third protein, encoded by the 3' half of ORF2, is associated with purified virions at sub-stoichiometric ratios. Although the structural proteins can be translated from the genomic RNA, we show that SINV-3 also produces a subgenomic RNA encoding the structural proteins. Circumstantial evidence suggests that APV may also produce such a subgenomic RNA. Both SINV-3 and APV are unclassified picorna-like viruses distantly related to members of the order Picornavirales and the family Caliciviridae. Within this grouping, features of the genome organization and capsid domain structure of SINV-3 and APV appear more similar to caliciviruses, perhaps suggesting the basis for a "Calicivirales" order. Public Library of Science 2014-03-31 /pmc/articles/PMC3970965/ /pubmed/24686475 http://dx.doi.org/10.1371/journal.pone.0093497 Text en https://creativecommons.org/publicdomain/zero/1.0/ This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Valles, Steven M.
Bell, Susanne
Firth, Andrew E.
spellingShingle Valles, Steven M.
Bell, Susanne
Firth, Andrew E.
Solenopsis invicta virus 3: Mapping of Structural Proteins, Ribosomal Frameshifting, and Similarities to Acyrthosiphon pisum virus and Kelp fly virus
author_facet Valles, Steven M.
Bell, Susanne
Firth, Andrew E.
author_sort Valles, Steven M.
title Solenopsis invicta virus 3: Mapping of Structural Proteins, Ribosomal Frameshifting, and Similarities to Acyrthosiphon pisum virus and Kelp fly virus
title_short Solenopsis invicta virus 3: Mapping of Structural Proteins, Ribosomal Frameshifting, and Similarities to Acyrthosiphon pisum virus and Kelp fly virus
title_full Solenopsis invicta virus 3: Mapping of Structural Proteins, Ribosomal Frameshifting, and Similarities to Acyrthosiphon pisum virus and Kelp fly virus
title_fullStr Solenopsis invicta virus 3: Mapping of Structural Proteins, Ribosomal Frameshifting, and Similarities to Acyrthosiphon pisum virus and Kelp fly virus
title_full_unstemmed Solenopsis invicta virus 3: Mapping of Structural Proteins, Ribosomal Frameshifting, and Similarities to Acyrthosiphon pisum virus and Kelp fly virus
title_sort solenopsis invicta virus 3: mapping of structural proteins, ribosomal frameshifting, and similarities to acyrthosiphon pisum virus and kelp fly virus
description Solenopsis invicta virus 3 (SINV-3) is a positive-sense single-stranded RNA virus that infects the red imported fire ant, Solenopsis invicta. We show that the second open reading frame (ORF) of the dicistronic genome is expressed via a frameshifting mechanism and that the sequences encoding the structural proteins map to both ORF2 and the 3' end of ORF1, downstream of the sequence that encodes the RNA-dependent RNA polymerase. The genome organization and structural protein expression strategy resemble those of Acyrthosiphon pisum virus (APV), an aphid virus. The capsid protein that is encoded by the 3' end of ORF1 in SINV-3 and APV is predicted to have a jelly-roll fold similar to the capsid proteins of picornaviruses and caliciviruses. The capsid-extension protein that is produced by frameshifting, includes the jelly-roll fold domain encoded by ORF1 as its N-terminus, while the C-terminus encoded by the 5' half of ORF2 has no clear homology with other viral structural proteins. A third protein, encoded by the 3' half of ORF2, is associated with purified virions at sub-stoichiometric ratios. Although the structural proteins can be translated from the genomic RNA, we show that SINV-3 also produces a subgenomic RNA encoding the structural proteins. Circumstantial evidence suggests that APV may also produce such a subgenomic RNA. Both SINV-3 and APV are unclassified picorna-like viruses distantly related to members of the order Picornavirales and the family Caliciviridae. Within this grouping, features of the genome organization and capsid domain structure of SINV-3 and APV appear more similar to caliciviruses, perhaps suggesting the basis for a "Calicivirales" order.
publisher Public Library of Science
publishDate 2014
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3970965/
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