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Alkylation of Histidine Residues of Bothrops jararacussu Venom Proteins and Isolated Phospholipases A(2): A Biotechnological Tool to Improve the Production of Antibodies
  • Fundacao Oswaldo Cruz
  • Universidade Federal de Rondônia (UNIR)
  • Brazilian Inst Environm & Renewable Nat Resources
  • Universidade de São Paulo (USP)
  • Universidade Federal de Sergipe (UFS)
  • Universidade Federal da Paraíba (UFPB)
  • Universidade Estadual Paulista (UNESP)
  • Inst Res Biomed IRB Barcelona
  • Univ Barcelona
  • Univ KwaZulu Natal
  • Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
  • Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
  • Instituto Nacional de Ciencia e Tecnologia em Toxinas (INCT-Tox)
  • Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
  • Instituto Brasileiro do Meio ambiente e dos Recursos Naturais renovaveis (IBAMA)
  • Institute for Research in Biomedicine (IRB) (Barcelona, Spain)
  • Parc Cientific de Barcelona (Universidade de Barcelona, Spain)
Crude venom of Bothrops jararacussu and isolated phospholipases A(2) (PLA(2)) of this toxin (BthTX-I and BthTX-II) were chemically modified (alkylation) by p-bromophenacyl bromide (BPB) in order to study antibody production capacity in function of the structure-function relationship of these substances (crude venom and PLA(2) native and alkylated). BthTX-II showed enzymatic activity, while BthTX-I did not. Alkylation reduced BthTX-II activity by 50% while this process abolished the catalytic and myotoxic activities of BthTX-I, while reducing its edema-inducing activity by about 50%. Antibody production against the native and alkylated forms of BthTX-I and -II and the cross-reactivity of antibodies to native and alkylated toxins did not show any apparent differences and these observations were reinforced by surface plasmon resonance (SPR) data. Histopathological analysis of mouse gastrocnemius muscle sections after injection of PBS, BthTX-I, BthTX-II, or both myotoxins previously incubated with neutralizing antibody showed inhibition of the toxin-inducedmyotoxicity. These results reveal that the chemical modification of the phospholipases A(2) (PLA(2)) diminished their toxicity but did not alter their antigenicity. This observation indicates that the modified PLA(2) may provide a biotechnological tool to attenuate the toxicity of the crude venom, by improving the production of antibodies and decreasing the local toxic effects of this poisonous substance in animals used to produce antivenom.
Issue Date: 
Biomed Research International. New York: Hindawi Publishing Corporation, 12 p., 2014.
Time Duration: 
Hindawi Publishing Corporation
Access Rights: 
Acesso aberto
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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