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 | Acesso ao texto completo restrito à biblioteca da Embrapa Arroz e Feijão. Para informações adicionais entre em contato com cnpaf.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Arroz e Feijão. |
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Data corrente: |
28/06/2021 |
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Data da última atualização: |
28/06/2021 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 1 |
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Autoria: |
DeBLASIO, S. L.; WILSON, J. R.; TAMBORINDEGUY, C.; JOHNSON, R. S.; PINHEIRO, P. V.; MacCOSS, M. J.; GRAY, S. M.; HECK, M. |
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Afiliação: |
STACY L. DEBLASIO; JENNIFER R. WILSON; CECILIA TAMBORINDEGUY; RICHARD S. JOHNSON; PATRICIA VALLE PINHEIRO, CNPAF; MICHAEL J. MACCOSS; STEWART M. GRAY; MICHELLE HECK. |
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Título: |
Affinity purification - mass spectrometry identifies a novel interaction between a polerovirus and a conserved innate immunity aphid protein that regulates transmission efficiency. |
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Ano de publicação: |
2021 |
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Fonte/Imprenta: |
Journal of Proteome Research, v. 20, n. 6, p. 3365-3387, June 2021. |
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Série: |
1535-3907 |
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DOI: |
https://doi.org/10.1021/acs.jproteome.1c00313 |
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Idioma: |
Inglês |
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Conteúdo: |
The vast majority of plant viruses are transmitted by insect vectors, with many crucial aspects of the transmission process being mediated by key protein?protein interactions. Still, very few vector proteins interacting with viruses have been identified and functionally characterized. Potato leafroll virus (PLRV) is transmitted most efficiently by Myzus persicae, the green peach aphid, in a circulative, non-propagative manner. Using affinity purification coupled to high-resolution mass spectrometry (AP-MS), we identified 11 proteins from M. persicaedisplaying a high probability of interaction with PLRV and an additional 23 vector proteins with medium confidence interaction scores. Three of these aphid proteins were confirmed to directly interact with the structural proteins of PLRV and other luteovirid species via yeast two-hybrid. Immunolocalization of one of these direct PLRV-interacting proteins, an orthologue of the human innate immunity protein complement component 1 Q subcomponent-binding protein (C1QBP), shows that MpC1QBP partially co-localizes with PLRV in cytoplasmic puncta and along the periphery of aphid gut epithelial cells. Artificial diet delivery to aphids of a chemical inhibitor of C1QBP leads to increased PLRV acquisition by aphids and subsequently increased titer in inoculated plants, supporting a role for C1QBP in the acquisition and transmission efficiency of PLRV by M. persicae. This study presents the first use of AP-MS for the in vivo isolation of a functionally relevant insect vector-virus protein complex. MS data are available from ProteomeXchange.org using the project identifier PXD022167. MenosThe vast majority of plant viruses are transmitted by insect vectors, with many crucial aspects of the transmission process being mediated by key protein?protein interactions. Still, very few vector proteins interacting with viruses have been identified and functionally characterized. Potato leafroll virus (PLRV) is transmitted most efficiently by Myzus persicae, the green peach aphid, in a circulative, non-propagative manner. Using affinity purification coupled to high-resolution mass spectrometry (AP-MS), we identified 11 proteins from M. persicaedisplaying a high probability of interaction with PLRV and an additional 23 vector proteins with medium confidence interaction scores. Three of these aphid proteins were confirmed to directly interact with the structural proteins of PLRV and other luteovirid species via yeast two-hybrid. Immunolocalization of one of these direct PLRV-interacting proteins, an orthologue of the human innate immunity protein complement component 1 Q subcomponent-binding protein (C1QBP), shows that MpC1QBP partially co-localizes with PLRV in cytoplasmic puncta and along the periphery of aphid gut epithelial cells. Artificial diet delivery to aphids of a chemical inhibitor of C1QBP leads to increased PLRV acquisition by aphids and subsequently increased titer in inoculated plants, supporting a role for C1QBP in the acquisition and transmission efficiency of PLRV by M. persicae. This study presents the first use of AP-MS for the in vivo isolation of a f... Mostrar Tudo |
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Palavras-Chave: |
Affinity purification; Aphids; Non-model system; Vector-pathogen interactions. |
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Thesaurus NAL: |
Luteoviridae; Mass spectrometry; Myzus; Phloem; Polerovirus; Potato leafroll virus; Purification methods. |
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Categoria do assunto: |
O Insetos e Entomologia |
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Marc: |
LEADER 02793naa a2200361 a 4500
001 2132597
005 2021-06-28
008 2021 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1021/acs.jproteome.1c00313$2DOI
100 1 $aDeBLASIO, S. L.
245 $aAffinity purification - mass spectrometry identifies a novel interaction between a polerovirus and a conserved innate immunity aphid protein that regulates transmission efficiency.$h[electronic resource]
260 $c2021
490 $a1535-3907
520 $aThe vast majority of plant viruses are transmitted by insect vectors, with many crucial aspects of the transmission process being mediated by key protein?protein interactions. Still, very few vector proteins interacting with viruses have been identified and functionally characterized. Potato leafroll virus (PLRV) is transmitted most efficiently by Myzus persicae, the green peach aphid, in a circulative, non-propagative manner. Using affinity purification coupled to high-resolution mass spectrometry (AP-MS), we identified 11 proteins from M. persicaedisplaying a high probability of interaction with PLRV and an additional 23 vector proteins with medium confidence interaction scores. Three of these aphid proteins were confirmed to directly interact with the structural proteins of PLRV and other luteovirid species via yeast two-hybrid. Immunolocalization of one of these direct PLRV-interacting proteins, an orthologue of the human innate immunity protein complement component 1 Q subcomponent-binding protein (C1QBP), shows that MpC1QBP partially co-localizes with PLRV in cytoplasmic puncta and along the periphery of aphid gut epithelial cells. Artificial diet delivery to aphids of a chemical inhibitor of C1QBP leads to increased PLRV acquisition by aphids and subsequently increased titer in inoculated plants, supporting a role for C1QBP in the acquisition and transmission efficiency of PLRV by M. persicae. This study presents the first use of AP-MS for the in vivo isolation of a functionally relevant insect vector-virus protein complex. MS data are available from ProteomeXchange.org using the project identifier PXD022167.
650 $aLuteoviridae
650 $aMass spectrometry
650 $aMyzus
650 $aPhloem
650 $aPolerovirus
650 $aPotato leafroll virus
650 $aPurification methods
653 $aAffinity purification
653 $aAphids
653 $aNon-model system
653 $aVector-pathogen interactions
700 1 $aWILSON, J. R.
700 1 $aTAMBORINDEGUY, C.
700 1 $aJOHNSON, R. S.
700 1 $aPINHEIRO, P. V.
700 1 $aMacCOSS, M. J.
700 1 $aGRAY, S. M.
700 1 $aHECK, M.
773 $tJournal of Proteome Research$gv. 20, n. 6, p. 3365-3387, June 2021.
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