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 | Acesso ao texto completo restrito à biblioteca da Embrapa Agricultura Digital. Para informações adicionais entre em contato com cnptia.biblioteca@embrapa.br. |
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Registro Completo |
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Biblioteca(s): |
Embrapa Agricultura Digital. |
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Data corrente: |
26/11/2009 |
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Data da última atualização: |
15/01/2020 |
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Tipo da produção científica: |
Resumo em Anais de Congresso |
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Autoria: |
NESHICH, I. A. P.; MORAES, F. R. de; MARANGONI, S.; MARTINS, D.; SALIM, J. A.; MAZONI, I.; MANCINI, A.; NESHICH, G.; JARDINE, J. G. |
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Afiliação: |
IZABELLA AGOSTINHO PENA NESHICH, Estagiária/CNPTIA; FABIO ROGERIO DE MORAES, Bolsista/CNPTIA; S. MARANGONI, Unicamp; D. MARTINS, Unicamp; JOSÉ AUGUSTO SALIM, Estagiário/CNPTIA; IVAN MAZONI, CNPTIA; ADAUTO LUIZ MANCINI, CNPTIA; GORAN NESHICH, CNPTIA; JOSE GILBERTO JARDINE, CNPTIA. |
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Título: |
Xylella fastidiosa hexameric pilus retraction motor PILT interfaces are maintained by non-hydrophobic contacts. |
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Ano de publicação: |
2009 |
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Fonte/Imprenta: |
In: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB, 2009. |
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Páginas: |
Não paginado. |
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Idioma: |
Inglês |
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Notas: |
X-Meeting 2009. |
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Conteúdo: |
Xylella fastidiosa (Xf) causes CVC and Pierce?s Disease (affecting citrus and grape). Xf colonizes the xylem vessels in plants. Pathogenicity of the Xf are related to ability to move within the xylem. Avirulent strains rarely move from the inoculation point. Xf has proteins involved in type IV pili, which cause the twitching motility - a form of surface-associated movement. Satyshur and coworkers had solved four structures from PilT proteins (PDB codes: 2GSZ, 2EWV, 2EWW and 2EYU) from a hyperthermophilic organism, Aquifex aeolicus (Aa). PilT is a hexameric ATPase from a subgroup of the bacterial type II/type IV secretion systems, with two major domains: the Nterminal Domain (NTD) and the C-Terminal Domain (CTD) which contains the ATPase core. The importance of polar and charged CTDn: NTDn+1 interface interactions to retraction motion was discussed. Through site-directed mutagenesis on Pseudomonas aeruginosa PilT, they demonstrated that some residues are crucial to protein function, half of them (D29, R95 and R207) located on interface region. The Xf PilT has 68% of similarity and 49% of identical aminoacids to Aa). We modelled each Xf PilT chain. We analyzed the hexameric structure of Aa Pilt (PDB code: 2GSZ) and Xf PilT hexamer model (named here as 2HXF) using Blue Star STING platform. By analysis of Interface Forming Residues (IFR), we found that there was a significant difference among the interfaces: Xf PilT interfaces area occupied mainly by charged amino acids. This does not hold for the free surfaces (molecular surface without interfaces). In 2GSZ the interface area is occupied by hydrophobic and polar AA; In addition, the interfaces have less charged AA than free surface. The Aa PilT interfaces are more hydrophobic when compared to Xf PilT. The number and energies of contacts established between IFRs in 2HXF are higher than 2GSZ, suggesting that Xf PilT interfaces are more stable. Apparently, the most important IFRs (which establish most energetic contacts at the surface) are conserved within Proteobacteria and Aquificae PilTs (Clustalw alignment data). Thus, we suggest that the difference among amino acid composition of interfaces between Xf PilT and Aa PilT reflect their crucial importance on successful host infections across the Proteobacteria. We hypothesize here that similarities found in primary sequence alignment could be maintained at 3D level, indicating a possible higher selective pressure on these locations in Proteobacteria (as compared to the Aa PilT). We also suggest that these residues, crucially important to protein functionality, might serve as potential targets to eliminate bacteria pathogenicity. MenosXylella fastidiosa (Xf) causes CVC and Pierce?s Disease (affecting citrus and grape). Xf colonizes the xylem vessels in plants. Pathogenicity of the Xf are related to ability to move within the xylem. Avirulent strains rarely move from the inoculation point. Xf has proteins involved in type IV pili, which cause the twitching motility - a form of surface-associated movement. Satyshur and coworkers had solved four structures from PilT proteins (PDB codes: 2GSZ, 2EWV, 2EWW and 2EYU) from a hyperthermophilic organism, Aquifex aeolicus (Aa). PilT is a hexameric ATPase from a subgroup of the bacterial type II/type IV secretion systems, with two major domains: the Nterminal Domain (NTD) and the C-Terminal Domain (CTD) which contains the ATPase core. The importance of polar and charged CTDn: NTDn+1 interface interactions to retraction motion was discussed. Through site-directed mutagenesis on Pseudomonas aeruginosa PilT, they demonstrated that some residues are crucial to protein function, half of them (D29, R95 and R207) located on interface region. The Xf PilT has 68% of similarity and 49% of identical aminoacids to Aa). We modelled each Xf PilT chain. We analyzed the hexameric structure of Aa Pilt (PDB code: 2GSZ) and Xf PilT hexamer model (named here as 2HXF) using Blue Star STING platform. By analysis of Interface Forming Residues (IFR), we found that there was a significant difference among the interfaces: Xf PilT interfaces area occupied mainly by charged amino acids. This do... Mostrar Tudo |
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Palavras-Chave: |
Aminoácidos; Bioinformática; Contatos não hidrofóbicos; Proteínas. |
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Thesagro: |
Xylella Fastidiosa. |
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Thesaurus Nal: |
Bioinformatics; Proteins. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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Marc: |
LEADER 03706nam a2200313 a 4500
001 1576270
005 2020-01-15
008 2009 bl uuuu u00u1 u #d
100 1 $aNESHICH, I. A. P.
245 $aXylella fastidiosa hexameric pilus retraction motor PILT interfaces are maintained by non-hydrophobic contacts.$h[electronic resource]
260 $aIn: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB$c2009
300 $aNão paginado.
500 $aX-Meeting 2009.
520 $aXylella fastidiosa (Xf) causes CVC and Pierce?s Disease (affecting citrus and grape). Xf colonizes the xylem vessels in plants. Pathogenicity of the Xf are related to ability to move within the xylem. Avirulent strains rarely move from the inoculation point. Xf has proteins involved in type IV pili, which cause the twitching motility - a form of surface-associated movement. Satyshur and coworkers had solved four structures from PilT proteins (PDB codes: 2GSZ, 2EWV, 2EWW and 2EYU) from a hyperthermophilic organism, Aquifex aeolicus (Aa). PilT is a hexameric ATPase from a subgroup of the bacterial type II/type IV secretion systems, with two major domains: the Nterminal Domain (NTD) and the C-Terminal Domain (CTD) which contains the ATPase core. The importance of polar and charged CTDn: NTDn+1 interface interactions to retraction motion was discussed. Through site-directed mutagenesis on Pseudomonas aeruginosa PilT, they demonstrated that some residues are crucial to protein function, half of them (D29, R95 and R207) located on interface region. The Xf PilT has 68% of similarity and 49% of identical aminoacids to Aa). We modelled each Xf PilT chain. We analyzed the hexameric structure of Aa Pilt (PDB code: 2GSZ) and Xf PilT hexamer model (named here as 2HXF) using Blue Star STING platform. By analysis of Interface Forming Residues (IFR), we found that there was a significant difference among the interfaces: Xf PilT interfaces area occupied mainly by charged amino acids. This does not hold for the free surfaces (molecular surface without interfaces). In 2GSZ the interface area is occupied by hydrophobic and polar AA; In addition, the interfaces have less charged AA than free surface. The Aa PilT interfaces are more hydrophobic when compared to Xf PilT. The number and energies of contacts established between IFRs in 2HXF are higher than 2GSZ, suggesting that Xf PilT interfaces are more stable. Apparently, the most important IFRs (which establish most energetic contacts at the surface) are conserved within Proteobacteria and Aquificae PilTs (Clustalw alignment data). Thus, we suggest that the difference among amino acid composition of interfaces between Xf PilT and Aa PilT reflect their crucial importance on successful host infections across the Proteobacteria. We hypothesize here that similarities found in primary sequence alignment could be maintained at 3D level, indicating a possible higher selective pressure on these locations in Proteobacteria (as compared to the Aa PilT). We also suggest that these residues, crucially important to protein functionality, might serve as potential targets to eliminate bacteria pathogenicity.
650 $aBioinformatics
650 $aProteins
650 $aXylella Fastidiosa
653 $aAminoácidos
653 $aBioinformática
653 $aContatos não hidrofóbicos
653 $aProteínas
700 1 $aMORAES, F. R. de
700 1 $aMARANGONI, S.
700 1 $aMARTINS, D.
700 1 $aSALIM, J. A.
700 1 $aMAZONI, I.
700 1 $aMANCINI, A.
700 1 $aNESHICH, G.
700 1 $aJARDINE, J. G.
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Embrapa Agricultura Digital (CNPTIA) |
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Registro Completo
|
Biblioteca(s): |
Embrapa Pesca e Aquicultura. |
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Data corrente: |
09/11/2020 |
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Data da última atualização: |
25/11/2020 |
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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: |
FRISSO, R. M.; MATOS, F. T. de; MORO, G. V.; MATTOS, B. O. de. |
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Afiliação: |
ROSIMERY MENEZES FRISSO, UNIVERSIDADE NILTON LINS, Manaus-AM; FLAVIA TAVARES DE MATOS, CNPASA; GIOVANNI VITTI MORO, CNPASA; BRUNO OLIVETTI DE MATTOS, INSTITUTO FEDERAL DE EDUCAÇÃO, CIÊNCIA E TECNOLOGIA DO AMAZONAS. |
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Título: |
Stocking density of Amazon fish (Colossoma macropomum) farmed in a continental neotropical reservoir with a net cages system. |
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Ano de publicação: |
2020 |
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Fonte/Imprenta: |
Aquaculture, v. 529, 735702, Dec. 2020. |
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ISSN: |
0044-8486 |
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DOI: |
https://doi.org/10.1016/j.aquaculture.2020.735702 |
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Idioma: |
Inglês |
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Conteúdo: |
A 60-day experiment was conducted to evaluate the best stocking density (SD) and net cage (NC) size for rearing tambaqui juveniles (Colossoma macropomu) in a continental neotropical reservoir. 57,688 tambaqui juveniles (50.10 ± 1.39 g, mean ± S.E.M.) had been randomly stocked in 16 NC. The experiment was run with a 2 × 2 factorial scheme at two SD (15 kg/m3; 24 kg/m3) and two NC sizes (22.5 m3; 40 m3), with four replications: T1: 15 kg/m3 x 22.5 m3; T2: 24 kg/m3 x 22.5 m3; T3: 15 kg/m3 x 40m3; T4: 24 kg/m3 x 40m3. After 60 days, growth performance, biochemical parameters and body composition of fish were evaluated. Individual weight gain, feed conversion ratio, feed efficiency rate, specific growth rate and protein efficiency ratio were better at SD 24 kg/m3. For body composition, the crude protein and lower crude fat values in NC 24 kg/m3 and NC 40 m3 were higher. The biochemical parameters showed no significant difference for total proteins and plasma cholesterol. Triglycerides had higher rates for the fish stored in NC 40 m3. An SD-NC interaction appeared for glucose and cortisol, with higher values for SD 15 kg/m3 in NC 40 m3; the highest values were observed in SD 24 kg/m3 for NC 22.5m3. Therefore, the production of the fish stocked in SD 24 kg/m3 was more efficient as the biochemical parameters had better indices for the fish raised in 40m3. The findings in this study suggest using SD 24 kg/m3 in NC 40 m3 to maximise fish productivity and welfare. |
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Palavras-Chave: |
Cage farming; Intensive system; Welfare. |
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Thesagro: |
Colossoma Macropomum; Gaiola para Pesca; Peixe; Tambaqui. |
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Thesaurus NAL: |
Cages; Fish. |
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Categoria do assunto: |
L Ciência Animal e Produtos de Origem Animal |
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Marc: |
LEADER 02328naa a2200289 a 4500
001 2126408
005 2020-11-25
008 2020 bl uuuu u00u1 u #d
022 $a0044-8486
024 7 $ahttps://doi.org/10.1016/j.aquaculture.2020.735702$2DOI
100 1 $aFRISSO, R. M.
245 $aStocking density of Amazon fish (Colossoma macropomum) farmed in a continental neotropical reservoir with a net cages system.$h[electronic resource]
260 $c2020
520 $aA 60-day experiment was conducted to evaluate the best stocking density (SD) and net cage (NC) size for rearing tambaqui juveniles (Colossoma macropomu) in a continental neotropical reservoir. 57,688 tambaqui juveniles (50.10 ± 1.39 g, mean ± S.E.M.) had been randomly stocked in 16 NC. The experiment was run with a 2 × 2 factorial scheme at two SD (15 kg/m3; 24 kg/m3) and two NC sizes (22.5 m3; 40 m3), with four replications: T1: 15 kg/m3 x 22.5 m3; T2: 24 kg/m3 x 22.5 m3; T3: 15 kg/m3 x 40m3; T4: 24 kg/m3 x 40m3. After 60 days, growth performance, biochemical parameters and body composition of fish were evaluated. Individual weight gain, feed conversion ratio, feed efficiency rate, specific growth rate and protein efficiency ratio were better at SD 24 kg/m3. For body composition, the crude protein and lower crude fat values in NC 24 kg/m3 and NC 40 m3 were higher. The biochemical parameters showed no significant difference for total proteins and plasma cholesterol. Triglycerides had higher rates for the fish stored in NC 40 m3. An SD-NC interaction appeared for glucose and cortisol, with higher values for SD 15 kg/m3 in NC 40 m3; the highest values were observed in SD 24 kg/m3 for NC 22.5m3. Therefore, the production of the fish stocked in SD 24 kg/m3 was more efficient as the biochemical parameters had better indices for the fish raised in 40m3. The findings in this study suggest using SD 24 kg/m3 in NC 40 m3 to maximise fish productivity and welfare.
650 $aCages
650 $aFish
650 $aColossoma Macropomum
650 $aGaiola para Pesca
650 $aPeixe
650 $aTambaqui
653 $aCage farming
653 $aIntensive system
653 $aWelfare
700 1 $aMATOS, F. T. de
700 1 $aMORO, G. V.
700 1 $aMATTOS, B. O. de
773 $tAquaculture$gv. 529, 735702, Dec. 2020.
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Embrapa Pesca e Aquicultura (CNPASA) |
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