A Rhipicephalus (Boophilus) microplus cathepsin with dual peptidase and antimicrobial activity

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• 作者：Daiane P. Oldiges^a ; Luí ; s F. Parizi^a ; Karine R. Zimmer^a ; Daniel M. Lorenzini^a ; Adriana Seixas^a ; ^d ; Aoi Masuda^a ; Itabajara da Silva Vaz Jr.^a ; ^c ; ^{itacbt@gmail.com} ; ^{itabajara.vaz@ufrgs.br} ; Carlos Termignoni^a ; ^b
• 关键词：Tick ; Antimicrobial peptide ; Cysteine endopeptidase
• 刊名：International Journal for Parasitology
• 出版年：2012
• 出版时间：June, 2012
• 年：2012
• 卷：42
• 期：7
• 页码：635-645
• 全文大小：1365 K

文摘

The cattle tick, Rhipicephalus (Boophilus) microplus, is a haematophagous arthropod responsible for considerable losses in the livestock industry. Immunological control with vaccines is a promising alternative to replace chemical acaricides. Due to their importance in parasite physiology, cysteine endopeptidases are potential targets. In a previous study, native Vitellin Degrading Cysteine Endopeptidase (VTDCE) was successfully tested as a vaccine antigen for bovines against R. microplus. In this work, nucleotide and amino acid VTDCE sequences were obtained from cDNA databanks, based on data from Edman sequencing and mass spectrometry. Subsequently, cloning and expression, purification, immunological and biochemical characterisation of the recombinant protein were performed to determine the biological importance of VTDCE. By Western blot, polyclonal antibodies produced against recombinant VTDCE recognised native VTDCE. Interestingly, molecular analysis showed that the VTDCE sequence has similarity to antimicrobial peptides. Indeed, experimental results revealed that VTDCE has an antimicrobial activity which is independent of endopeptidase activity. We believe that this is the first known study to show that an arthropod enzyme has antimicrobial activity.