You are in the accessibility menu

Please use this identifier to cite or link to this item:
Full metadata record
DC FieldValueLanguage
dc.contributor.authorGuimaraes, C. L. S.-
dc.contributor.authorAndriao-Escarso, S. H.-
dc.contributor.authorMoreira-Dill, L. S.-
dc.contributor.authorCarvalho, B. M. A.-
dc.contributor.authorMarchi-Salvador, D. P.-
dc.contributor.authorSantos-Filho, N. A.-
dc.contributor.authorFernandes, C. A. H.-
dc.contributor.authorFontes, M. R. M.-
dc.contributor.authorGiglio, J. R.-
dc.contributor.authorBarraviera, B.-
dc.contributor.authorZuliani, J. P.-
dc.contributor.authorFernandes, C. F. C.-
dc.contributor.authorCalderon, L. A.-
dc.contributor.authorStabeli, R. G.-
dc.contributor.authorAlbericio, F.-
dc.contributor.authorSilva, S. L. da-
dc.contributor.authorSoares, A. M.-
dc.identifier.citationBiomed Research International. New York: Hindawi Publishing Corporation, 12 p., 2014.-
dc.description.abstractCrude 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.en
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
dc.description.sponsorshipInstituto Nacional de Ciencia e Tecnologia em Toxinas (INCT-Tox)-
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)-
dc.description.sponsorshipInstituto Brasileiro do Meio ambiente e dos Recursos Naturais renovaveis (IBAMA)-
dc.description.sponsorshipInstitute for Research in Biomedicine (IRB) (Barcelona, Spain)-
dc.description.sponsorshipParc Cientific de Barcelona (Universidade de Barcelona, Spain)-
dc.publisherHindawi Publishing Corporation-
dc.sourceWeb of Science-
dc.titleAlkylation of Histidine Residues of Bothrops jararacussu Venom Proteins and Isolated Phospholipases A(2): A Biotechnological Tool to Improve the Production of Antibodiesen
dc.contributor.institutionFundacao Oswaldo Cruz-
dc.contributor.institutionUniversidade Federal de Rondônia (UNIR)-
dc.contributor.institutionBrazilian Inst Environm & Renewable Nat Resources-
dc.contributor.institutionUniversidade de São Paulo (USP)-
dc.contributor.institutionUniversidade Federal de Sergipe (UFS)-
dc.contributor.institutionUniversidade Federal da Paraíba (UFPB)-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionInst Res Biomed IRB Barcelona-
dc.contributor.institutionCIBER BBN-
dc.contributor.institutionUniv Barcelona-
dc.contributor.institutionUniv KwaZulu Natal-
dc.description.affiliationFundacao Oswaldo Cruz, Ctr Appl Biomol Studies Hlth CEBio, Fiocruz Rondonia, Porto Velho, RO, Brazil-
dc.description.affiliationFed Univ Rondonia UNIR, Dept Med, Porto Velho, RO, Brazil-
dc.description.affiliationBrazilian Inst Environm & Renewable Nat Resources, Porto Velho, RO, Brazil-
dc.description.affiliationUniv Sao Paulo, Fac Med Ribeirao Preto, Dept Biochem & Immunol, BR-14049 Ribeirao Preto, SP, Brazil-
dc.description.affiliationFed Univ Sao Joao Del Rei UFSJ, Dept Chem Biotechnol & Bioproc Engn, Ouro Branco, MG, Brazil-
dc.description.affiliationFed Univ Paraiba UFPB, Ctr Sci & Nat, Dept Mol Biol, Joao Pessoa, Paraiba, Brazil-
dc.description.affiliationUniv Sao Paulo, Fac Pharmaceut Sci Ribeirao Preto, Dept Clin Anal, BR-14049 Ribeirao Preto, SP, Brazil-
dc.description.affiliationState Univ Paulista UNESP, Dept Phys & Biophys, Botucatu, SP, Brazil-
dc.description.affiliationState Univ Paulista UNESP, Ctr Study Venoms & Venomous Anim CEVAP, Botucatu, SP, Brazil-
dc.description.affiliationInst Res Biomed IRB Barcelona, Barcelona, Spain-
dc.description.affiliationCIBER BBN, Barcelona, Spain-
dc.description.affiliationUniv Barcelona, Dept Organ Chem, Barcelona, Spain-
dc.description.affiliationUniv KwaZulu Natal, Sch Chem & Phys, ZA-4001 Durban, South Africa-
dc.description.affiliationUnespState Univ Paulista UNESP, Dept Phys & Biophys, Botucatu, SP, Brazil-
dc.description.affiliationUnespState Univ Paulista UNESP, Ctr Study Venoms & Venomous Anim CEVAP, Botucatu, SP, Brazil-
dc.rights.accessRightsAcesso aberto-
dc.relation.ispartofBioMed Research International-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.