a preliminary study: expression of rhoptry protein 1 (rop1) toxoplasma gondii in prokaryote system

نویسندگان

zahra eslamirad department of parasitology, arak university of medical sciences, arak, ir iran; molecular and medicine research center, arak university of medical sciences, arak, ir iran; department of parasitology, arak university of medical sciences, arak, ir iran. tel: +98-8614173505, fax: +98-8614173521

fatemeh ghaffarifar depepartment of parasitology, faculty of medical sciences, tarbiat modares university, tehran, ir iran

mana shojapour molecular and medicine research center, arak university of medical sciences, arak, ir iran

behzad khansarinejad department of microbiology, arak university of medical sciences, arak, ir iran

چکیده

background toxoplasma gondii is an obligatory intracellular protozoan parasite, which infects human beings. since the current antigens used for diagnosis or vaccination are contaminated with non parasitic material in which the parasite is grown, it is tried to produce recombinant antigens to design vaccines against toxoplasmosis, or make diagnostic kits. choosing the type of antigen to produce recombinant vaccine or diagnostic kits is considerably important. the rhoptry protein 1 is one of the excretory-secretary antigens of toxoplasma which seems to be an appropriate candidate in production of recombinant vaccines and diagnostic kits. conclusions the result of this study showed that recombinant rop1 toxoplasma was produced successfully. in the present study, unlike other studies, the goal was to express full length of rop1. also this protein was produced alone not fused with other proteins. objectives the current study aimed to produce rhoptry protein 1 from iranian strains of toxoplasma for further investigations. materials and methods genomic dna was isolated from tachyzoite of parasite by phenol chloroform method and gene fragment was amplified by polymerase chain reaction. the polymerase chain reaction products were ligated into restriction enzymes sites of ptz57r/t cloning vector. the product was sub-cloned into a prokaryotic expression plasmid (pet32a). the recombinant expression vector containing rhoptry protein 1 sequence was transformed into escherichia coli bl21 plyss and was induced by isopropyl β-d-1-thiogalactopyranoside. the sodium dodecyl sulfate polyacrylamide gel electrophoresis and western blotting methods were used to confirm the production of protein. results the result showed that the desired molecular weight protein is produced. recombinant protein was confirmed by western blot using ni-nta- conjugate.

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عنوان ژورنال:
jundishapur journal of microbiology

جلد ۶، شماره ۶، صفحات ۰-۰

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