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Registro Completo |
Biblioteca(s): |
Embrapa Gado de Corte. |
Data corrente: |
04/02/2009 |
Data da última atualização: |
22/07/2011 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Autoria: |
ARAÚJO, F. R.; COSTA, C. M.; RAMOS, C. A. N.; FARIAS, T. A.; SOUZA, I. I.; F. de; MELO, E. S. P.; ELISEI, C.; ROSINHA, G. M. S.; SOARES, C. O.; FRAGOSO, S. P.; FONSECA, A. H. |
Afiliação: |
Flábio Ribeiro Araújo, CNPGC; Cátia Marques da Costa, UFRRJ; Carlos Alberto do Nascimento Ramos, UFMS; Thaís Andrade Farias, bolsista CNPGC; Ingrid Ieda Fernando de Souza, , bolsista CNPGC; Elaine Silva Pádua de Melo, UFMS; Carina Elisei, bolsista CNPGC. |
Título: |
IgG and IgG2 antibodies from cattle naturally infected with Anaplasma marginale recognize the recombinant vaccine candidate antigens VirB9, VirB10, and elongation factor-Tu. |
Ano de publicação: |
2008 |
Fonte/Imprenta: |
Memórias do Instituto Oswaldo Cruz, Rio de Janeiro, v. 103, n. 2, p. 186-190, Mar., 2008. |
Idioma: |
Inglês |
Conteúdo: |
Anaplasma marginale is an important vector-borne rickettsia of ruminants in tropical and subtropical regions of the world. Immunization with purified outer membranes of this organism induces protection against acute anaplasmosis. Previous studies, with proteomic and genomic approach identified 21 proteins within the outer membrane immunogen in addition to previously characterized major surface protein1a-5 (MSP1a-5). Among the newly described proteins were VirB9, VirB10, and elongation factor-Tu (EF-Tu). VirB9, VirB10 are considered part of the type IV secretion system (TFSS), which mediates secretion or cell-to-cell transfer of macromolecules, proteins, or DNA-protein complexes in Gram-negative bacteria. EF-Tu can be located in the bacterial surface, mediating bacterial attachment to host cells, or in the bacterial cytoplasm for protein synthesis. However, the roles of VirB9, VirB10, and TFSS in A. marginale have not been defined. VirB9, VirB10, and EF-Tu have not been explored as vaccine antigens. In this study, we demonstrate that sera of cattle infected with A. marginale, with homologous or heterologous isolates recognize recombinant VirB9, VirB10, and EF-Tu. IgG2 from naturally infected cattle also reacts with these proteins. Recognition of epitopes by total IgG and by IgG2 from infected cattle with A. marginale support the inclusion of these proteins in recombinant vaccines against this rickettsia. |
Palavras-Chave: |
Brasil; Proteína recombinante; Rio Grande do Norte; VirB10; VirB9. |
Thesagro: |
Anaplasma Marginale; Anaplasmose; Anticorpo; Imunidade; Imunologia; Ruminante; Sanidade Animal; Vacina. |
Categoria do assunto: |
-- |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/38369/1/115.pdf
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Marc: |
LEADER 02630naa a2200409 a 4500 001 1326865 005 2011-07-22 008 2008 bl uuuu u00u1 u #d 100 1 $aARAÚJO, F. R. 245 $aIgG and IgG2 antibodies from cattle naturally infected with Anaplasma marginale recognize the recombinant vaccine candidate antigens VirB9, VirB10, and elongation factor-Tu.$h[electronic resource] 260 $c2008 520 $aAnaplasma marginale is an important vector-borne rickettsia of ruminants in tropical and subtropical regions of the world. Immunization with purified outer membranes of this organism induces protection against acute anaplasmosis. Previous studies, with proteomic and genomic approach identified 21 proteins within the outer membrane immunogen in addition to previously characterized major surface protein1a-5 (MSP1a-5). Among the newly described proteins were VirB9, VirB10, and elongation factor-Tu (EF-Tu). VirB9, VirB10 are considered part of the type IV secretion system (TFSS), which mediates secretion or cell-to-cell transfer of macromolecules, proteins, or DNA-protein complexes in Gram-negative bacteria. EF-Tu can be located in the bacterial surface, mediating bacterial attachment to host cells, or in the bacterial cytoplasm for protein synthesis. However, the roles of VirB9, VirB10, and TFSS in A. marginale have not been defined. VirB9, VirB10, and EF-Tu have not been explored as vaccine antigens. In this study, we demonstrate that sera of cattle infected with A. marginale, with homologous or heterologous isolates recognize recombinant VirB9, VirB10, and EF-Tu. IgG2 from naturally infected cattle also reacts with these proteins. Recognition of epitopes by total IgG and by IgG2 from infected cattle with A. marginale support the inclusion of these proteins in recombinant vaccines against this rickettsia. 650 $aAnaplasma Marginale 650 $aAnaplasmose 650 $aAnticorpo 650 $aImunidade 650 $aImunologia 650 $aRuminante 650 $aSanidade Animal 650 $aVacina 653 $aBrasil 653 $aProteína recombinante 653 $aRio Grande do Norte 653 $aVirB10 653 $aVirB9 700 1 $aCOSTA, C. M. 700 1 $aRAMOS, C. A. N. 700 1 $aFARIAS, T. A. 700 1 $aSOUZA, I. I. 700 1 $aF. de 700 1 $aMELO, E. S. P. 700 1 $aELISEI, C. 700 1 $aROSINHA, G. M. S. 700 1 $aSOARES, C. O. 700 1 $aFRAGOSO, S. P. 700 1 $aFONSECA, A. H. 773 $tMemórias do Instituto Oswaldo Cruz, Rio de Janeiro$gv. 103, n. 2, p. 186-190, Mar., 2008.
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Embrapa Gado de Corte (CNPGC) |
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Registro Completo
Biblioteca(s): |
Embrapa Agroenergia. |
Data corrente: |
17/10/2012 |
Data da última atualização: |
21/09/2017 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Circulação/Nível: |
A - 1 |
Autoria: |
SILVA, J. A.; MACEDO, G. P.; RODRIGUES, D. de S.; GIORDANO, R. L. C.; GONÇALVES, L. R. B. |
Afiliação: |
J. A. Silva, UFC; G. P. Macedo, UFC; DASCIANA DE SOUSA RODRIGUES, CNPAE; R. L. C. Giordano, Universidade Federal de São Carlos; L. R. B. Gonçalves, UFC. |
Título: |
Immobilization of Candida antarctica lipase B by covalent attachment on chitosan-based hydrogels using different support activation strategies. |
Ano de publicação: |
2012 |
Fonte/Imprenta: |
Biochemical Engineering Journal, V. 60, P. 16-24, 2012. |
DOI: |
10.1016/j.bej.2011.09.011 |
Idioma: |
Inglês |
Palavras-Chave: |
Catálise; Chitosan-alginate complex; Enzimas imobilizadas. |
Thesagro: |
Lípase. |
Thesaurus NAL: |
biocatalysis; chitosan; immobilized enzymes. |
Categoria do assunto: |
-- |
Marc: |
LEADER 00831naa a2200253 a 4500 001 1936989 005 2017-09-21 008 2012 bl uuuu u00u1 u #d 024 7 $a10.1016/j.bej.2011.09.011$2DOI 100 1 $aSILVA, J. A. 245 $aImmobilization of Candida antarctica lipase B by covalent attachment on chitosan-based hydrogels using different support activation strategies.$h[electronic resource] 260 $c2012 650 $abiocatalysis 650 $achitosan 650 $aimmobilized enzymes 650 $aLípase 653 $aCatálise 653 $aChitosan-alginate complex 653 $aEnzimas imobilizadas 700 1 $aMACEDO, G. P. 700 1 $aRODRIGUES, D. de S. 700 1 $aGIORDANO, R. L. C. 700 1 $aGONÇALVES, L. R. B. 773 $tBiochemical Engineering Journal, V. 60, P. 16-24, 2012.
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