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Registro Completo |
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Biblioteca(s): |
Embrapa Semiárido. |
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Data corrente: |
02/12/2010 |
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Data da última atualização: |
03/10/2014 |
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Autoria: |
CAMPELLO, F. C. B.; SENA, C. M. de; PAREYN, F. G. |
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Título: |
Proposta de integração da atividade florestal ao sistema agrário da Região do Seridó-RN. |
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Ano de publicação: |
1989 |
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Fonte/Imprenta: |
Natal: IBAMA, 1989. |
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Páginas: |
12 p. |
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Série: |
(IBAMA. Circular Técnica, 3). |
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Idioma: |
Português |
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Conteúdo: |
Visando demonstrar a possibilidade da integração da atividade florestal à produção agropecuária, bem como sua contribuição para o equilíbrio do balanço demanda/oferta de produtos florestais, apresenta-se este trabalho para a região do Seridó do Rio Grande do Norte, localizada no semi-árido do Nordeste brasileiro. |
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Palavras-Chave: |
Forest; Projeto PNUD/FAO/BRA/87/007; Projeto político florestal. |
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Thesagro: |
Floresta. |
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Categoria do assunto: |
K Ciência Florestal e Produtos de Origem Vegetal |
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Marc: |
LEADER 00912nam a2200205 a 4500
001 1868562
005 2014-10-03
008 1989 bl uuuu u0uu1 u #d
100 1 $aCAMPELLO, F. C. B.
245 $aProposta de integração da atividade florestal ao sistema agrário da Região do Seridó-RN.
260 $aNatal: IBAMA$c1989
300 $a12 p.
490 $a(IBAMA. Circular Técnica, 3).
520 $aVisando demonstrar a possibilidade da integração da atividade florestal à produção agropecuária, bem como sua contribuição para o equilíbrio do balanço demanda/oferta de produtos florestais, apresenta-se este trabalho para a região do Seridó do Rio Grande do Norte, localizada no semi-árido do Nordeste brasileiro.
650 $aFloresta
653 $aForest
653 $aProjeto PNUD/FAO/BRA/87/007
653 $aProjeto político florestal
700 1 $aSENA, C. M. de
700 1 $aPAREYN, F. G.
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Embrapa Semiárido (CPATSA) |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Rondônia. Para informações adicionais entre em contato com cpafro.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Rondônia. |
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Data corrente: |
22/08/2016 |
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Data da última atualização: |
22/08/2016 |
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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: |
PRADO, N. D. R.; SILVA, M. P. da; MORAIS, M. S. S.; KAYANO, A. M.; MOREIRA-DILL, L. S.; LUIZ, M. B.; FULY, A. L.; HUACCA, M. E. F.; FERNANDES, C. de F.; CALDERON, L. A.; ZULIANI, J. P.; SILVA, L. H. P. da; SOARES, A. M.; STABELI, R. G.; FERNANDES, C. F. C. |
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Afiliação: |
Nidiane D. R. Prado, Fundação Oswaldo Cruz, Fiocruz Rondônia; Michele P. da Silva, UFF; Michelle S. S. Morais, Fundação Oswaldo Cruz, Fiocruz Rondônia; Anderson M. Kayano, Fundação Oswaldo Cruz, Fiocruz Rondônia; Leandro S. Moreira-Dill, Fundação Oswaldo Cruz, Fiocruz Rondônia; Marcos B. Luiz, Fundação Oswaldo Cruz, Fiocruz Rondônia; André L. Fuly, Universidade Federal Fluminense; Maribel E. F. Huacca, UNIR; CLEBERSON DE FREITAS FERNANDES, CPAF-Rondonia; Leonardo A. Calderon, UNIR; Juliana P. Zuliani, UNIR; Luiz H. Pereira da Silva, Fundação Oswaldo Cruz, Fiocruz Rondônia; Andreimar M. Soares, Fundação Oswaldo Cruz, Fiocruz Rondônia; Rodrigo G. Stabeli, UNIR; Carla F. C. Fernandes, Fundaç ã o Oswaldo Cruz, Fiocruz Rondônia. |
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Título: |
Inhibition of the Myotoxicity Induced byBothropsjararacussuVenom and IsolatedPhospholipases A2 by Specific Camelid Single-Domain Antibody Fragments. |
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Ano de publicação: |
2016 |
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Fonte/Imprenta: |
PLOS ONE, v. 11, n. 3, March 30, 2016. |
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DOI: |
DOI:10.1371/journal.pone.0151363 |
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Idioma: |
Inglês |
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Conteúdo: |
Antivenoms, produced using animal hyperimmune plasma, remains the standard therapy for snakebites. Although effective against systemic damages, conventional antivenoms have limited efficacy against local tissue damage. Additionally, the hypersensitivity reactions, often elicited by antivenoms, the high costs for animal maintenance, the difficulty of producing homogeneous lots, and the instability of biological products instigate the search for innovative products for antivenom therapy. In this study, camelid antibody fragments (VHH) with specificity to Bothropstoxin I and II (BthTX-I and BthTX-II), two myotoxic phospholipases from Bothrops jararacussu venom, were selected from an immune VHH phage display library. After biopanning, 28 and 6 clones recognized BthTX-I and BthTX-II by ELISA, respectively. Complementarity determining regions (CDRs) and immunoglobulin frameworks (FRs) of 13 VHH-deduced amino acid sequences were identified, as well as the camelid hallmark amino acid substitutions in FR2. Three VHH clones (KF498607, KF498608, and KC329718) were capable of recognizing BthTX-I by Western blot and showed affinity constants in the nanomolar range against both toxins. VHHs inhibited the BthTX-II phospholipase A2 activity, and when tested for cross-reactivity, presented specificity to the Bothrops genus in ELISA. Furthermore, two clones (KC329718 and KF498607) neutralized the myotoxic effects induced by B. jararacussu venom, BthTX-I, BthTX-II, and by a myotoxin from Bothrops brazili venom (MTX-I) in mice. Molecular docking revealed that VHH CDRs are expected to bind the C-terminal of both toxins, essential for myotoxic activity, and to epitopes in the BthTX-II enzymatic cleft. Identified VHHs could be a biotechnological tool to improve the treatment for snake envenomation, an important and neglected world public health problem. MenosAntivenoms, produced using animal hyperimmune plasma, remains the standard therapy for snakebites. Although effective against systemic damages, conventional antivenoms have limited efficacy against local tissue damage. Additionally, the hypersensitivity reactions, often elicited by antivenoms, the high costs for animal maintenance, the difficulty of producing homogeneous lots, and the instability of biological products instigate the search for innovative products for antivenom therapy. In this study, camelid antibody fragments (VHH) with specificity to Bothropstoxin I and II (BthTX-I and BthTX-II), two myotoxic phospholipases from Bothrops jararacussu venom, were selected from an immune VHH phage display library. After biopanning, 28 and 6 clones recognized BthTX-I and BthTX-II by ELISA, respectively. Complementarity determining regions (CDRs) and immunoglobulin frameworks (FRs) of 13 VHH-deduced amino acid sequences were identified, as well as the camelid hallmark amino acid substitutions in FR2. Three VHH clones (KF498607, KF498608, and KC329718) were capable of recognizing BthTX-I by Western blot and showed affinity constants in the nanomolar range against both toxins. VHHs inhibited the BthTX-II phospholipase A2 activity, and when tested for cross-reactivity, presented specificity to the Bothrops genus in ELISA. Furthermore, two clones (KC329718 and KF498607) neutralized the myotoxic effects induced by B. jararacussu venom, BthTX-I, BthTX-II, and by a myotoxin from Bothr... Mostrar Tudo |
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Palavras-Chave: |
Animal hyperimmune plasma; Anticorpos de camelídeos; Antiveneno; Camelid antibody; Plasma de animal hiperimune; Veneno de cobra. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 03022naa a2200373 a 4500
001 2051429
005 2016-08-22
008 2016 bl uuuu u00u1 u #d
024 7 $aDOI:10.1371/journal.pone.0151363$2DOI
100 1 $aPRADO, N. D. R.
245 $aInhibition of the Myotoxicity Induced byBothropsjararacussuVenom and IsolatedPhospholipases A2 by Specific Camelid Single-Domain Antibody Fragments.$h[electronic resource]
260 $c2016
520 $aAntivenoms, produced using animal hyperimmune plasma, remains the standard therapy for snakebites. Although effective against systemic damages, conventional antivenoms have limited efficacy against local tissue damage. Additionally, the hypersensitivity reactions, often elicited by antivenoms, the high costs for animal maintenance, the difficulty of producing homogeneous lots, and the instability of biological products instigate the search for innovative products for antivenom therapy. In this study, camelid antibody fragments (VHH) with specificity to Bothropstoxin I and II (BthTX-I and BthTX-II), two myotoxic phospholipases from Bothrops jararacussu venom, were selected from an immune VHH phage display library. After biopanning, 28 and 6 clones recognized BthTX-I and BthTX-II by ELISA, respectively. Complementarity determining regions (CDRs) and immunoglobulin frameworks (FRs) of 13 VHH-deduced amino acid sequences were identified, as well as the camelid hallmark amino acid substitutions in FR2. Three VHH clones (KF498607, KF498608, and KC329718) were capable of recognizing BthTX-I by Western blot and showed affinity constants in the nanomolar range against both toxins. VHHs inhibited the BthTX-II phospholipase A2 activity, and when tested for cross-reactivity, presented specificity to the Bothrops genus in ELISA. Furthermore, two clones (KC329718 and KF498607) neutralized the myotoxic effects induced by B. jararacussu venom, BthTX-I, BthTX-II, and by a myotoxin from Bothrops brazili venom (MTX-I) in mice. Molecular docking revealed that VHH CDRs are expected to bind the C-terminal of both toxins, essential for myotoxic activity, and to epitopes in the BthTX-II enzymatic cleft. Identified VHHs could be a biotechnological tool to improve the treatment for snake envenomation, an important and neglected world public health problem.
653 $aAnimal hyperimmune plasma
653 $aAnticorpos de camelídeos
653 $aAntiveneno
653 $aCamelid antibody
653 $aPlasma de animal hiperimune
653 $aVeneno de cobra
700 1 $aSILVA, M. P. da
700 1 $aMORAIS, M. S. S.
700 1 $aKAYANO, A. M.
700 1 $aMOREIRA-DILL, L. S.
700 1 $aLUIZ, M. B.
700 1 $aFULY, A. L.
700 1 $aHUACCA, M. E. F.
700 1 $aFERNANDES, C. de F.
700 1 $aCALDERON, L. A.
700 1 $aZULIANI, J. P.
700 1 $aSILVA, L. H. P. da
700 1 $aSOARES, A. M.
700 1 $aSTABELI, R. G.
700 1 $aFERNANDES, C. F. C.
773 $tPLOS ONE$gv. 11, n. 3, March 30, 2016.
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