Protein composition of the occlusion bodies of <i>Epinotia aporema</i> granulovirus

Autores
Masson, Tomás; Fabre, María Laura; Ferrelli, María Leticia; Pidre, Matías Luis; Romanowski, Víctor
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Facultad de Ciencias Exactas
Instituto de Biotecnologia y Biologia Molecular
Materia
Ciencias Exactas
Biología
proteomes
virions
Genomics
proteomic databases
gene prediction
baculoviruses
larvae
invertebrate genomics
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/107807
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/107807
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Protein composition of the occlusion bodies of <i>Epinotia aporema</i> granulovirusMasson, TomásFabre, María LauraFerrelli, María LeticiaPidre, Matías LuisRomanowski, VíctorCiencias ExactasBiologíaproteomesvirionsGenomicsproteomic databasesgene predictionbaculoviruseslarvaeinvertebrate genomicsWithin family Baculoviridae, members of the <i>Betabaculovirus</i> genus are employed as biocontrol agents against lepidopteran pests, either alone or in combination with selected members of the <i>Alphabaculovirus</i> genus. <i>Epinotia aporema</i> granulovirus (EpapGV) is a fast killing betabaculovirus that infects the bean shoot borer (<i>E. aporema</i>) 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 ac<i>110</i>-like core gene and a putative translation fusion product of ORFs <i>epap48</i> and <i>epap49</i>. Comparative studies of the proteomes available for the family <i>Baculoviridae</i> 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.Facultad de Ciencias ExactasInstituto de Biotecnologia y Biologia Molecular2019info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/107807enginfo:eu-repo/semantics/altIdentifier/url/http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC6372164&blobtype=pdfinfo:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0207735info:eu-repo/semantics/altIdentifier/issn/1932-6203info:eu-repo/semantics/altIdentifier/pmid/30753194info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0207735info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:23:51Zoai:sedici.unlp.edu.ar:10915/107807Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:23:52.083SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Protein composition of the occlusion bodies of <i>Epinotia aporema</i> granulovirus
title Protein composition of the occlusion bodies of <i>Epinotia aporema</i> granulovirus
spellingShingle Protein composition of the occlusion bodies of <i>Epinotia aporema</i> granulovirus
Masson, Tomás
Ciencias Exactas
Biología
proteomes
virions
Genomics
proteomic databases
gene prediction
baculoviruses
larvae
invertebrate genomics
title_short Protein composition of the occlusion bodies of <i>Epinotia aporema</i> granulovirus
title_full Protein composition of the occlusion bodies of <i>Epinotia aporema</i> granulovirus
title_fullStr Protein composition of the occlusion bodies of <i>Epinotia aporema</i> granulovirus
title_full_unstemmed Protein composition of the occlusion bodies of <i>Epinotia aporema</i> granulovirus
title_sort Protein composition of the occlusion bodies of <i>Epinotia aporema</i> granulovirus
dc.creator.none.fl_str_mv Masson, Tomás
Fabre, María Laura
Ferrelli, María Leticia
Pidre, Matías Luis
Romanowski, Víctor
author Masson, Tomás
author_facet Masson, Tomás
Fabre, María Laura
Ferrelli, María Leticia
Pidre, Matías Luis
Romanowski, Víctor
author_role author
author2 Fabre, María Laura
Ferrelli, María Leticia
Pidre, Matías Luis
Romanowski, Víctor
author2_role author
author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Biología
proteomes
virions
Genomics
proteomic databases
gene prediction
baculoviruses
larvae
invertebrate genomics
topic Ciencias Exactas
Biología
proteomes
virions
Genomics
proteomic databases
gene prediction
baculoviruses
larvae
invertebrate genomics
dc.description.none.fl_txt_mv Within family Baculoviridae, members of the <i>Betabaculovirus</i> genus are employed as biocontrol agents against lepidopteran pests, either alone or in combination with selected members of the <i>Alphabaculovirus</i> genus. <i>Epinotia aporema</i> granulovirus (EpapGV) is a fast killing betabaculovirus that infects the bean shoot borer (<i>E. aporema</i>) 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 ac<i>110</i>-like core gene and a putative translation fusion product of ORFs <i>epap48</i> and <i>epap49</i>. Comparative studies of the proteomes available for the family <i>Baculoviridae</i> 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.
Facultad de Ciencias Exactas
Instituto de Biotecnologia y Biologia Molecular
description Within family Baculoviridae, members of the <i>Betabaculovirus</i> genus are employed as biocontrol agents against lepidopteran pests, either alone or in combination with selected members of the <i>Alphabaculovirus</i> genus. <i>Epinotia aporema</i> granulovirus (EpapGV) is a fast killing betabaculovirus that infects the bean shoot borer (<i>E. aporema</i>) 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 ac<i>110</i>-like core gene and a putative translation fusion product of ORFs <i>epap48</i> and <i>epap49</i>. Comparative studies of the proteomes available for the family <i>Baculoviridae</i> 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.
publishDate 2019
dc.date.none.fl_str_mv 2019
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/107807
url http://sedici.unlp.edu.ar/handle/10915/107807
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC6372164&blobtype=pdf
info:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0207735
info:eu-repo/semantics/altIdentifier/issn/1932-6203
info:eu-repo/semantics/altIdentifier/pmid/30753194
info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0207735
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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