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 | Acesso ao texto completo restrito à biblioteca da Embrapa Recursos Genéticos e Biotecnologia. Para informações adicionais entre em contato com cenargen.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
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Data corrente: |
26/02/2013 |
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Data da última atualização: |
07/03/2023 |
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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: |
NOGUEIRA, F. C.; SILVA, C. P.; ALEXANDRE, D.; SAMUELS, R. I; SOARES, E. L.; ARAGAO, F. J. L.; PALMISANO, G.; DOMONT, G. B.; ROEPSTORFF, P.; CAMPOS, F. A. |
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Afiliação: |
Universidade Federal do Rio de Janeiro; Universidade Federal de Santa Catarina; Universidade Federal de Santa Catarina; Universidade Estadual do Norte Fluminense; Universidade Federal do Ceará; FRANCISCO JOSE LIMA ARAGAO, CENARGEN; University of Southern Denmark; Universidade Federal do Rio de Janeiro; University of Southern Denmark; Universidade Federal do Ceará. |
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Título: |
Global proteome changes in larvae of Callosobruchus maculatus Coleoptera:Chrysomelidae:Bruchinae) following ingestion of a cysteine proteinase inhibitor. |
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Ano de publicação: |
2012 |
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Fonte/Imprenta: |
Proteomics, v. 12, n. 17, p. 2704-2715, 2012. |
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Idioma: |
Inglês |
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Conteúdo: |
The seed-feeding beetle Callosobruchus maculatus is an important cowpea pest (Vigna unguiculata) as well as an interesting model to study insect digestive physiology. The larvae of C. maculatus rely on cysteine and aspartic peptidases to digest proteins in their diet. In this work, the global proteomic changes induced in the intestinal tract of larval C. maculatus challenged by the ingestion of cystatin, a cysteine peptidase inhibitor, was investigated by a nanoLC-MS/MS approach. The ingestion of cystatin caused a delay in the development of the larvae, but the mortality was not high, indicating that C. maculatus is able to adapt to this inhibitor. This proteomic strategy resulted in the identification of 752 and 550 protein groups in the midgut epithelia and midgut contents, respectively, and quantitative analyses allowed us to establish relative differences of the identified proteins. Ingestion of cystatin led to significant changes in the proteome of both the midgut epithelia and midgut contents. We have observed that proteins related to plant cell wall degradation, particularly the key glycoside hydrolases of the families GH5 (endo-?-1,4-mannanase) and GH 28 (polygalacturonase) were overexpressed. Conversely, ?-amylases were downexpressed, indicating that an increase in hemicelluloses digestion helps the larvae to cope with the challenge of cystatin ingestion. Furthermore, a number of proteins associated with transcription/translation and antistress reactions were among the cystatin-responsive proteins, implying that a substantial rearrangement in the proteome occurred in C. maculatus exposed to the inhibitor. MenosThe seed-feeding beetle Callosobruchus maculatus is an important cowpea pest (Vigna unguiculata) as well as an interesting model to study insect digestive physiology. The larvae of C. maculatus rely on cysteine and aspartic peptidases to digest proteins in their diet. In this work, the global proteomic changes induced in the intestinal tract of larval C. maculatus challenged by the ingestion of cystatin, a cysteine peptidase inhibitor, was investigated by a nanoLC-MS/MS approach. The ingestion of cystatin caused a delay in the development of the larvae, but the mortality was not high, indicating that C. maculatus is able to adapt to this inhibitor. This proteomic strategy resulted in the identification of 752 and 550 protein groups in the midgut epithelia and midgut contents, respectively, and quantitative analyses allowed us to establish relative differences of the identified proteins. Ingestion of cystatin led to significant changes in the proteome of both the midgut epithelia and midgut contents. We have observed that proteins related to plant cell wall degradation, particularly the key glycoside hydrolases of the families GH5 (endo-?-1,4-mannanase) and GH 28 (polygalacturonase) were overexpressed. Conversely, ?-amylases were downexpressed, indicating that an increase in hemicelluloses digestion helps the larvae to cope with the challenge of cystatin ingestion. Furthermore, a number of proteins associated with transcription/translation and antistress reactions were among ... Mostrar Tudo |
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Palavras-Chave: |
Peptidase inhibitors; Plant proteomics. |
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Thesagro: |
Callosobruchus Maculatus; Vigna Unguiculata. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02507naa a2200277 a 4500
001 1951245
005 2023-03-07
008 2012 bl uuuu u00u1 u #d
100 1 $aNOGUEIRA, F. C.
245 $aGlobal proteome changes in larvae of Callosobruchus maculatus Coleoptera$bChrysomelidae:Bruchinae) following ingestion of a cysteine proteinase inhibitor.$h[electronic resource]
260 $c2012
520 $aThe seed-feeding beetle Callosobruchus maculatus is an important cowpea pest (Vigna unguiculata) as well as an interesting model to study insect digestive physiology. The larvae of C. maculatus rely on cysteine and aspartic peptidases to digest proteins in their diet. In this work, the global proteomic changes induced in the intestinal tract of larval C. maculatus challenged by the ingestion of cystatin, a cysteine peptidase inhibitor, was investigated by a nanoLC-MS/MS approach. The ingestion of cystatin caused a delay in the development of the larvae, but the mortality was not high, indicating that C. maculatus is able to adapt to this inhibitor. This proteomic strategy resulted in the identification of 752 and 550 protein groups in the midgut epithelia and midgut contents, respectively, and quantitative analyses allowed us to establish relative differences of the identified proteins. Ingestion of cystatin led to significant changes in the proteome of both the midgut epithelia and midgut contents. We have observed that proteins related to plant cell wall degradation, particularly the key glycoside hydrolases of the families GH5 (endo-?-1,4-mannanase) and GH 28 (polygalacturonase) were overexpressed. Conversely, ?-amylases were downexpressed, indicating that an increase in hemicelluloses digestion helps the larvae to cope with the challenge of cystatin ingestion. Furthermore, a number of proteins associated with transcription/translation and antistress reactions were among the cystatin-responsive proteins, implying that a substantial rearrangement in the proteome occurred in C. maculatus exposed to the inhibitor.
650 $aCallosobruchus Maculatus
650 $aVigna Unguiculata
653 $aPeptidase inhibitors
653 $aPlant proteomics
700 1 $aSILVA, C. P.
700 1 $aALEXANDRE, D.
700 1 $aSAMUELS, R. I
700 1 $aSOARES, E. L.
700 1 $aARAGAO, F. J. L.
700 1 $aPALMISANO, G.
700 1 $aDOMONT, G. B.
700 1 $aROEPSTORFF, P.
700 1 $aCAMPOS, F. A.
773 $tProteomics$gv. 12, n. 17, p. 2704-2715, 2012.
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