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Protein composition of the occlusion bodies of Epinotia aporema granulovirus
Within family Baculoviridae, members of the Betabaculovirus genus are employed as biocontrol agents against lepidopteran pests, either alone or in combination with selected members of the Alphabaculovirus genus. Epinotia aporema granulovirus (EpapGV) is a fast killing betabaculovirus that infects th...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6372164/ https://www.ncbi.nlm.nih.gov/pubmed/30753194 http://dx.doi.org/10.1371/journal.pone.0207735 |
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author | Masson, Tomás Fabre, María Laura Ferrelli, María Leticia Pidre, Matías Luis Romanowski, Víctor |
author_facet | Masson, Tomás Fabre, María Laura Ferrelli, María Leticia Pidre, Matías Luis Romanowski, Víctor |
author_sort | Masson, Tomás |
collection | PubMed |
description | Within family Baculoviridae, members of the Betabaculovirus genus are employed as biocontrol agents against lepidopteran pests, either alone or in combination with selected members of the Alphabaculovirus genus. Epinotia aporema granulovirus (EpapGV) is a fast killing betabaculovirus that infects the bean shoot borer (E. aporema) and is a promising biopesticide. Because occlusion bodies (OBs) play a key role in baculovirus horizontal transmission, we investigated the composition of EpapGV OBs. Using mass spectrometry-based proteomics we could identify 56 proteins that are included in the OBs during the final stages of larval infection. Our data provides experimental validation of several annotated hypothetical coding sequences. Proteogenomic mapping against genomic sequence detected a previously unannotated ac110-like core gene and a putative translation fusion product of ORFs epap48 and epap49. Comparative studies of the proteomes available for the family Baculoviridae highlight the conservation of core gene products as parts of the occluded virion. Two proteins specific for betabaculoviruses (Epap48 and Epap95) are incorporated into OBs. Moreover, quantification based on emPAI values showed that Epap95 is one of the most abundant components of EpapGV OBs. |
format | Online Article Text |
id | pubmed-6372164 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-63721642019-03-01 Protein composition of the occlusion bodies of Epinotia aporema granulovirus Masson, Tomás Fabre, María Laura Ferrelli, María Leticia Pidre, Matías Luis Romanowski, Víctor PLoS One Research Article Within family Baculoviridae, members of the Betabaculovirus genus are employed as biocontrol agents against lepidopteran pests, either alone or in combination with selected members of the Alphabaculovirus genus. Epinotia aporema granulovirus (EpapGV) is a fast killing betabaculovirus that infects the bean shoot borer (E. aporema) and is a promising biopesticide. Because occlusion bodies (OBs) play a key role in baculovirus horizontal transmission, we investigated the composition of EpapGV OBs. Using mass spectrometry-based proteomics we could identify 56 proteins that are included in the OBs during the final stages of larval infection. Our data provides experimental validation of several annotated hypothetical coding sequences. Proteogenomic mapping against genomic sequence detected a previously unannotated ac110-like core gene and a putative translation fusion product of ORFs epap48 and epap49. Comparative studies of the proteomes available for the family Baculoviridae highlight the conservation of core gene products as parts of the occluded virion. Two proteins specific for betabaculoviruses (Epap48 and Epap95) are incorporated into OBs. Moreover, quantification based on emPAI values showed that Epap95 is one of the most abundant components of EpapGV OBs. Public Library of Science 2019-02-12 /pmc/articles/PMC6372164/ /pubmed/30753194 http://dx.doi.org/10.1371/journal.pone.0207735 Text en © 2019 Masson et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Masson, Tomás Fabre, María Laura Ferrelli, María Leticia Pidre, Matías Luis Romanowski, Víctor Protein composition of the occlusion bodies of Epinotia aporema granulovirus |
title | Protein composition of the occlusion bodies of Epinotia aporema granulovirus |
title_full | Protein composition of the occlusion bodies of Epinotia aporema granulovirus |
title_fullStr | Protein composition of the occlusion bodies of Epinotia aporema granulovirus |
title_full_unstemmed | Protein composition of the occlusion bodies of Epinotia aporema granulovirus |
title_short | Protein composition of the occlusion bodies of Epinotia aporema granulovirus |
title_sort | protein composition of the occlusion bodies of epinotia aporema granulovirus |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6372164/ https://www.ncbi.nlm.nih.gov/pubmed/30753194 http://dx.doi.org/10.1371/journal.pone.0207735 |
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