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Registro Completo |
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Biblioteca(s): |
Embrapa Florestas. |
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Data corrente: |
12/03/2008 |
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Data da última atualização: |
06/12/2023 |
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Tipo da produção científica: |
Comunicado Técnico/Recomendações Técnicas |
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Autoria: |
IEDE, E. T.; PENTEADO, S. D. R. C.; CALDATO, N.; REIS FILHO, W. |
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Afiliação: |
EDSON TADEU IEDE, CNPF; SUSETE DO ROCIO CHIARELLO PENTEADO, CNPF; NÁDIA CALDATO, FUNCEMA; WILSON REIS FILHO, EPAGRI. |
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Título: |
Pineus boerneri (Hemiptera: Adelgidae) - pulgão-lanígero-do-pínus - praga introduzida em plantios de Pinus spp. no Brasil. |
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Ano de publicação: |
2007 |
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Fonte/Imprenta: |
Colombo: Embrapa Florestas, 2007. |
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Páginas: |
6 p. |
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Série: |
(Embrapa Florestas. Comunicado técnico, 190). |
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ISSN: |
1517-5030 |
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Idioma: |
Português |
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Palavras-Chave: |
Espécie exótica; Pineus boerneri; Pulgão-lanígero-do-pínus. |
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Thesagro: |
Praga de planta; Pulgão. |
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Thesaurus Nal: |
Pinus. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/215473/1/com-tec190.pdf
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Marc: |
LEADER 00736nam a2200241 a 4500
001 1313986
005 2023-12-06
008 2007 bl uuuu u0uu1 u #d
022 $a1517-5030
100 1 $aIEDE, E. T.
245 $aPineus boerneri (Hemiptera$bAdelgidae) - pulgão-lanígero-do-pínus - praga introduzida em plantios de Pinus spp. no Brasil.
260 $aColombo: Embrapa Florestas$c2007
300 $a6 p.
490 $a(Embrapa Florestas. Comunicado técnico, 190).
650 $aPinus
650 $aPraga de planta
650 $aPulgão
653 $aEspécie exótica
653 $aPineus boerneri
653 $aPulgão-lanígero-do-pínus
700 1 $aPENTEADO, S. D. R. C.
700 1 $aCALDATO, N.
700 1 $aREIS FILHO, W.
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Registro original: |
Embrapa Florestas (CNPF) |
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Registro Completo
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Biblioteca(s): |
Embrapa Café. |
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Data corrente: |
04/01/2023 |
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Data da última atualização: |
04/01/2023 |
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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: |
BARBOSA, E. A.; ALVES, G. S. C.; COURA, M. de M. A.; SILVA, H. de L. e; ROCHA, F. S. da; NUNES, J. B.; WATANABE, M. de S.; ANDRADE, A. C.; BRANDA, G. D. |
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Afiliação: |
EDER ALVES BARBOSA, UNIVERSIDADE DE BRASÍLIA; GABRIEL SÉRGIO COSTA ALVES, UNIVERSIDADE DE BRASÍLIA; MARCELO DE MELO ANDRADE COURA, UNIVERSIDADE DE BRASÍLIA; HIGOR DE LIMA E SILVA, UNIVERSIDADE DE BRASÍLIA; FILIPE SOUZA DA ROCHA, UNIVERSIDADE DE BRASÍLIA; JOÃO BUENO NUNES, UNIVERSIDADE DE BRASÍLIA; MATHEUS DE SOUZA WATANABE, UNIVERSIDADE DE BRASÍLIA; ALAN CARVALHO ANDRADE, CNPCa; GUILHERME DOTTO BRANDA, UNIVERSIDADE DE BRASÍLIA. |
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Título: |
A first look at the N- and O-glycosylation landscape in anuran skin secretions. |
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Ano de publicação: |
2022 |
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Fonte/Imprenta: |
Biochimie, v. 197, Jun., p.19-37, 2022. |
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DOI: |
https://doi.org/10.1016/j.biochi.2022.01.008 |
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Idioma: |
Inglês |
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Conteúdo: |
Amphibians secrete a complex array of molecules that shape their interactions with coinhabiting microorganisms and macroscopic predators. Glycans are a rapidly evolving and complex class of biomolecules implicated in intrinsic and extrinsic recognition events. Despite the numerous studies aiming at the biochemical characterization of anuran skin secretions, little is known about protein-linked oligosaccharides, their synthesis pathways, and their homing secreted glycoproteins. In the present report, LC-MS/MS was used to investigate the diversity of N- and O-linked oligosaccharides in the skin secretion of two South American frogs, Pithecopus azureus and Boana raniceps. Additionally, the enzymes responsible for glycan synthesis pathways were evaluated based on their skin tissue transcriptome. Our analyses allowed the annotation of various N- and O-glycan structures commonly found in vertebrate proteins. Paucimannosidic glycans were abundant in the skin secretion of both amphibians; however, hybrid and complex N-glycan structures were detected only in B. raniceps. A good correlation between the structures discovered in glycomic analyses and transcripts encoding enzymes necessary for their synthesis was obtained. Some transcripts such as those of MAN1A2, FUT8, and ST6GALNAC were found solely in B. raniceps. Finally, secreted N- and O- linked glycoproteins were predicted from the transcriptomic data, indicating that proteases and protease inhibitors are putative sources of the glycans described herein. Overall, our results show the presence of oligosaccharides in amphibians skin secretions and suggest that their diversity is species-specific, paving the way for novel perspectives involving amphibian evolution and ecology. MenosAmphibians secrete a complex array of molecules that shape their interactions with coinhabiting microorganisms and macroscopic predators. Glycans are a rapidly evolving and complex class of biomolecules implicated in intrinsic and extrinsic recognition events. Despite the numerous studies aiming at the biochemical characterization of anuran skin secretions, little is known about protein-linked oligosaccharides, their synthesis pathways, and their homing secreted glycoproteins. In the present report, LC-MS/MS was used to investigate the diversity of N- and O-linked oligosaccharides in the skin secretion of two South American frogs, Pithecopus azureus and Boana raniceps. Additionally, the enzymes responsible for glycan synthesis pathways were evaluated based on their skin tissue transcriptome. Our analyses allowed the annotation of various N- and O-glycan structures commonly found in vertebrate proteins. Paucimannosidic glycans were abundant in the skin secretion of both amphibians; however, hybrid and complex N-glycan structures were detected only in B. raniceps. A good correlation between the structures discovered in glycomic analyses and transcripts encoding enzymes necessary for their synthesis was obtained. Some transcripts such as those of MAN1A2, FUT8, and ST6GALNAC were found solely in B. raniceps. Finally, secreted N- and O- linked glycoproteins were predicted from the transcriptomic data, indicating that proteases and protease inhibitors are putative sources of the g... Mostrar Tudo |
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Thesaurus NAL: |
Mass spectrometry; Oligosaccharides; Transcriptomics. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/doc/1150624/1/A-first-look-at-the-N.pdf
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Marc: |
LEADER 02536naa a2200265 a 4500
001 2150624
005 2023-01-04
008 2022 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1016/j.biochi.2022.01.008$2DOI
100 1 $aBARBOSA, E. A.
245 $aA first look at the N- and O-glycosylation landscape in anuran skin secretions.$h[electronic resource]
260 $c2022
520 $aAmphibians secrete a complex array of molecules that shape their interactions with coinhabiting microorganisms and macroscopic predators. Glycans are a rapidly evolving and complex class of biomolecules implicated in intrinsic and extrinsic recognition events. Despite the numerous studies aiming at the biochemical characterization of anuran skin secretions, little is known about protein-linked oligosaccharides, their synthesis pathways, and their homing secreted glycoproteins. In the present report, LC-MS/MS was used to investigate the diversity of N- and O-linked oligosaccharides in the skin secretion of two South American frogs, Pithecopus azureus and Boana raniceps. Additionally, the enzymes responsible for glycan synthesis pathways were evaluated based on their skin tissue transcriptome. Our analyses allowed the annotation of various N- and O-glycan structures commonly found in vertebrate proteins. Paucimannosidic glycans were abundant in the skin secretion of both amphibians; however, hybrid and complex N-glycan structures were detected only in B. raniceps. A good correlation between the structures discovered in glycomic analyses and transcripts encoding enzymes necessary for their synthesis was obtained. Some transcripts such as those of MAN1A2, FUT8, and ST6GALNAC were found solely in B. raniceps. Finally, secreted N- and O- linked glycoproteins were predicted from the transcriptomic data, indicating that proteases and protease inhibitors are putative sources of the glycans described herein. Overall, our results show the presence of oligosaccharides in amphibians skin secretions and suggest that their diversity is species-specific, paving the way for novel perspectives involving amphibian evolution and ecology.
650 $aMass spectrometry
650 $aOligosaccharides
650 $aTranscriptomics
700 1 $aALVES, G. S. C.
700 1 $aCOURA, M. de M. A.
700 1 $aSILVA, H. de L. e
700 1 $aROCHA, F. S. da
700 1 $aNUNES, J. B.
700 1 $aWATANABE, M. de S.
700 1 $aANDRADE, A. C.
700 1 $aBRANDA, G. D.
773 $tBiochimie$gv. 197, Jun., p.19-37, 2022.
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