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| 1. |  | DUCATI, C.; NERES, M. A.; CASTAGNARA, D. D.; OLIVEIRA, P. S. R.; WEIRICH, D.; SILVA, G. M. da; SUNAHARA, S. M. M. Forage potential of black oat Iapar 61 alone or in association with birdsfoot trefoil. Ciencia e Investigación Agraria, Santiago, v. 42, n. 3, p. 341-351, dic. 2016.| Biblioteca(s): Embrapa Pecuária Sul. |
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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: |
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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.
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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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