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Identification and characterization of a cathepsin-f-like protease in Trichinella spiralis

Identification and characterization of a cathepsin-F-like pr...

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中国畜牧兽医学会兽医寄生虫学分会第十三次学术研讨会

作者： Zi-gang Qu Xue-ting Ma Wen-hui Li Nian-zhang Zhang Long Yue Jian-min Cui Jian-ping Cai Wan-zhong Jia Bao-quan fu State Key Laboratory of Veterinary Etiological Biology Key Laboratory of Veterinary Public Health of the Ministry of AgricultureKey Laboratory of Veterinary Parasitology of Gansu ProvinceLanzhou Veterinary Research InstituteChinese Academy of Agricultural Sciences Jiangsu Co-innovation Center for Prevention and Control of Important Animal Infectious Disease

Trichinellosis is a an emerging and reemerging infectious disease,caused by Trichinella *** f belongs to cysteine protease that is a major virulence factor for parasitic helminths,and it may be a potential anti-helminth drug target and vaccine *** this study,the cDNA encoding a putative cathepsin f-like peptidase in Trichinella spiralis,TsCf1,was obtained and its biochemical characterization and expression profile were *** demonstrated that the TsCf1 gene encodes a protein of 366 aa with the theoretical molecular weight of 41.9 ku and isoelectric point of *** signal peptide sequence of TsCf1 located between amino acids 1 and 19 and 3 putative N-glycosylation sites were *** cysteine protease conserved active site of Cys173,His309 and Asn333 were identified and cathepsin f specific motif ERfNAQ like KLfNAQ sequence was revealed in the propeptide of *** analysis revealed a higher than 40%identity with other cathepsin f from parasitic helminth and phylogenetic analysis indicated TsCf1 located in the different clans with trematode cathepsin ***-PCR revealed the gene was expressed in muscle larvae,newborn larvae and adult *** SDS-PAGE revealed the recombinant protein was expressed with the molecular weight of 45 *** analysis showed that TsCf1 located on the inner layer of the cuticle and stichosome of the parasite,which probably play a vital role in nutrition *** purified recombinant TsCf1 was used to immunize rabbit and the immune serum could recognize a band of soluble protein of muscle larvae at about 46 *** renaturation the TsCf1 recombinat protein demonstrated substantial enzyme activity to Z-Phe-Arg-AMC substrate with the optimal pH 5.5 and this activity could be inhibited by cysteine protease inhibitor *** analysis revealed the kinetic parameters of the recombinant peptidase to be Km=0.5091 μM and Vmax= 6.12 RfU/sμM at pH 5.5,and the IC50 value of E64 was 1

关键词： Trichinella spiralis cysteine protease cathepsin f enzyme activity

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