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...

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Main Authors: Tomás Masson, María Laura Fabre, María Leticia Ferrelli, Matías Luis Pidre, Víctor Romanowski
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2019-01-01
Series:PLoS ONE
Online Access:https://doi.org/10.1371/journal.pone.0207735
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author Tomás Masson
María Laura Fabre
María Leticia Ferrelli
Matías Luis Pidre
Víctor Romanowski
author_facet Tomás Masson
María Laura Fabre
María Leticia Ferrelli
Matías Luis Pidre
Víctor Romanowski
author_sort Tomás Masson
collection DOAJ
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.
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spelling doaj.art-62d6eb0844764d8a9c838809278925872022-12-21T19:56:19ZengPublic Library of Science (PLoS)PLoS ONE1932-62032019-01-01142e020773510.1371/journal.pone.0207735Protein composition of the occlusion bodies of Epinotia aporema granulovirus.Tomás MassonMaría Laura FabreMaría Leticia FerrelliMatías Luis PidreVíctor RomanowskiWithin 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.https://doi.org/10.1371/journal.pone.0207735
spellingShingle Tomás Masson
María Laura Fabre
María Leticia Ferrelli
Matías Luis Pidre
Víctor Romanowski
Protein composition of the occlusion bodies of Epinotia aporema granulovirus.
PLoS ONE
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
url https://doi.org/10.1371/journal.pone.0207735
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