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A comparison between the recombinant expression and chemical synthesis of a short cysteine-rich insecticidal spider peptide J. Venom. Anim. Toxins incl. Trop. Dis.
Clement,Herlinda; Flores,Vianey; Diego-Garcia,Elia; Corrales-Garcia,Ligia; Villegas,Elba; Corzo,Gerardo.
Tipo: Info:eu-repo/semantics/article Palavras-chave: Insecticidal peptides; Protein expression; Bacteria; Theraphosid spider; Chemical synthesis; Cysteine-rich peptides.
Ano: 2015 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992015000100324
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Heterologous expression, protein folding and antibody recognition of a neurotoxin from the Mexican coral snake Micrurus laticorallis J. Venom. Anim. Toxins incl. Trop. Dis.
Clement,Herlinda; Flores,Vianey; la Rosa,Guillermo De; Zamudio,Fernando; Alagon,Alejandro; Corzo,Gerardo.
Abstract Background The cysteine-rich neurotoxins from elapid venoms are primarily responsible for human and animal envenomation; however, their low concentration in the venom may hamper the production of efficient elapid antivenoms. Therefore, the aim of the present study was to produce fully active elapid neurotoxic immunogens for elapid antivenom production. Method Cysteine-rich neurotoxins showed recombinant expression in two strains of E. coli, and were purified using affinity chromatography and reverse-phase HPLC (rpHPLC). Results The cDNA of the four disulfide-bridged peptide neurotoxin Mlat1 was cloned into a modified expression vector, pQE30, which was transfected into two different E. coli strains. The recombinant toxin (HisrMlat1) was...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Micrurus laticorallis; Protein folding; Recombinant; Elapid; Toxin; Protein recognition.
Ano: 2016 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992016000100318
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