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Structure–functionstudies on jaburetox,a recombinantinsecticidal peptidederived from jackbean (Canavaliaensiformis) urease Anne H.S. MartinelliKarine KappaunRodrigo Ligabue‐Braun2013 год

Structure–function studies on jaburetox, a recombinant insecticidal peptide derived from jack bean (Canavalia ensiformis) urease
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Аннотация: Ureases are metalloenzymes involved in defense mechanisms in plants. The insecticidal activity of Canavalia ensiformis (jack bean) ureases relies partially on an internal 10kDa peptide generated by enzymatic hydrolysis of the protein within susceptible insects. A recombinant version of this peptide, jaburetox, exhibits insecticidal, antifungal and membrane-disruptive properties. Molecular modeling of jaburetox revealed a prominent β-hairpin motif consistent with either neurotoxicity or pore formation.Aiming to identify structural motifs involved in its effects, mutated versions of jaburetox were built: 1) a peptide lacking the β-hairpin motif (residues 61-74), JbtxΔ-β; 2) a peptide corresponding the N-terminal half (residues 1-44), Jbtx N-ter, and 3) a peptide corresponding the C-terminal half (residues 45-93), Jbtx C-ter.1) JbtxΔ-β disrupts liposomes, and exhibited entomotoxic effects similar to the whole peptide, suggesting that the β-hairpin motif is not a determinant of these biological activities; 2) both Jbtx C-ter and Jbtx N-ter disrupted liposomes, the C-terminal peptide being the most active; and 3) while Jbtx N-ter persisted to be biologically active, Jbtx C-ter was less active when tested on different insect preparations. Molecular modeling and dynamics were applied to the urease-derived peptides to complement the structure-function analysis.The N-terminal portion of the Jbtx carries the most important entomotoxic domain which is fully active in the absence of the β-hairpin motif. Although the β-hairpin contributes to some extent, probably by interaction with insect membranes, it is not essential for the entomotoxic properties of Jbtx.Jbtx represents a new type of insecticidal and membrane-active peptide.
Год издания: 2013
Авторы: Anne H.S. Martinelli, Karine Kappaun, Rodrigo Ligabue‐Braun, Marina S. Defferrari, Angela Regina Piovesan, Fernanda Stanisçuaski, Diogo Ribeiro Demartini, Cháriston André Dal Belo, Carlos Gabriel Moreira de Almeida, Cristian Follmer, Hugo Verli, Célia R. Carlini, Giancarlo Pasquali
Издательство: Elsevier BV
Источник: Biochimica et Biophysica Acta (BBA) - General Subjects
Ключевые слова: Antimicrobial Peptides and Activities, Biochemical and Structural Characterization, Microbial Applications in Construction Materials
Другие ссылки: Biochimica et Biophysica Acta (BBA) - General Subjects (HTML)
PUCRS Repository (Pontifical Catholic University of Rio Grande do Sul) (PDF)
PUCRS Repository (Pontifical Catholic University of Rio Grande do Sul) (HTML)
PubMed (HTML)