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Karimi, Farrokh,Mousavi, Amir,Salmanian, Ali Hatef,Alizadeh, Houshang,Rafati, Sima 한국식물생명공학회 2013 Plant biotechnology reports Vol.7 No.4
Chloroplast genetic engineering offers an opportunity for high level expression and cost-effective recombinant protein production. Escherichia coli O157:H7 is one of the most important zoonotic pathogens causing hemorrhagic colitis (HC) and the life-threatening hemolytic-uremic syndrome in humans worldwide. The occurrence of zoonotic E. coli O157:H7 outbreaks in recent years has led to increased efforts in the development of safe and cost-effective immunogenic antigens against E. coli O157:H7. EspA and Tir/Intimin proteins are the important virulence factors which are encoded by the LEE locus of enterohemorrhagic E. coli. In this study, we hypothesized that the high level expression of the chimeric form of these effectors in chloroplasts and using tobacco transplastomic plants as an oral delivery system for the development of an edible-base vaccine would induce an immune response for the prevention of E. coli 0157:H7 attachment and colonization in animal model mice. The prokaryotic codonoptimized EIT protein was expressed in plastid genome via chloroplast transformation. Putative transplastomic plants were analyzed by PCR, and Southern blot analysis confirming chloroplast integration and homoplasmy in the T1 progeny. Immunoblotting and ELISA assays demonstrated that the EIT protein was expressed in chloroplasts and accumulated up to 1.4 % of total soluble protein in leaf tissue. In mice orally immunized with transplastomic tobacco plant leaves, high immunological responses (IgG and IgA specific antibodies) were detected in serum and feces. Finally, the challenging assay with E. coli O157:H7 in immunized mice showed reduced bacterial shedding.
Farrokh Karimi,Amir Mousavi,Houshang Alizadeh,Ali Hatef Salmanian,Sima Rafati 한국식물생명공학회 2013 Plant biotechnology reports Vol.7 No.4
Chloroplast genetic engineering offers an opportunity for high level expression and cost-effective recombinant protein production. Escherichia coli O157:H7 is one of the most important zoonotic pathogens causing hemorrhagic colitis (HC) and the life-threatening hemolytic- uremic syndrome in humans worldwide. The occurrence of zoonotic E. coli O157:H7 outbreaks in recent years has led to increased efforts in the development of safe and cost-effective immunogenic antigens against E. coli O157:H7. EspA and Tir/Intimin proteins are the important virulence factors which are encoded by the LEE locus of enterohemorrhagic E. coli. In this study, we hypothesized that the high level expression of the chimeric form of these effectors in chloroplasts and using tobacco transplastomic plants as an oral delivery system for the development of an edible-base vaccine would induce an immune response for the prevention of E. coli 0157:H7 attachment and colonization in animal model mice. The prokaryotic codonoptimizedEIT protein was expressed in plastid genome via chloroplast transformation. Putative transplastomic plants were analyzed by PCR, and Southern blot analysis confirmingchloroplast integration and homoplasmy in the T1 progeny. Immunoblotting and ELISA assays demonstrated that the EIT protein was expressed in chloroplasts and accumulated up to 1.4 % of total soluble protein in leaf tissue. In mice orally immunized with transplastomic tobacco plant leaves, high immunological responses (IgG and IgA specific antibodies) were detected in serum and feces. Finally, the challenging assay with E. coli O157:H7 in immunized mice showed reduced bacterial shedding.
Expression of Escherichia coli Heat-labile Enterotoxin B Subunit (LTB) in Saccharomyces cerevisiae
Mohammad Ahangarzadeh Rezaee,Abbas Rezaee,Seyed Mohammad Moazzeni,Ali Hatef Salmanian,Yoko Yasuda,Kunio Tochikubo,Shahin Najar Pirayeh,Mohsen Arzanlou 한국미생물학회 2005 The journal of microbiology Vol.43 No.4
Heat-labile enterotoxin B subunit (LTB) of enterotoxigenic Escherichia coli (ETEC) is both a strong mucosal adjuvant and immunogen. It is a subunit vaccine candidate to be used against ETEC-induced diarrhea. It has already been expressed in several bacterial and plant systems. In order to construct yeast expressing vector for the LTB protein, the eltB gene encoding LTB was amplified from a human origin enterotoxigenic E. coli DNA by PCR. The expression plasmid pLTB83 was constructed by inserting the eltB gene into the pYES2 shuttle vector immediately downstream of the GAL1 promoter. The recombinant vector was transformed into S. cerevisiae and was then induced by galactose. The LTB protein was detected in the total soluble protein of the yeast by SDS-PAGE analysis. Quantitative ELISA showed that the maximum amount of LTB protein expressed in the yeast was approximately 1.9% of the total soluble protein. Immunoblotting analysis showed the yeast-derived LTB protein was antigenically indistinguishable from bacterial LTB protein. Since the whole-recombinant yeast has been introduced as a new vaccine formulation the expression of LTB in S. cerevisiae can offer an inexpensive yet effective strategy to protect against ETEC, especially in developing countries where it is needed most.
Expression of Escherichia coli Heat-labile Enterotoxin B Subunit (LTB) in Saccharomyces cerevisiae
Rezaee Mohammad Ahangarzadeh,Rezaee Abbas,Moazzeni Seyed Mohammad,Salmanian Ali Hatef,Yasuda Yoko,Tochikubo Kunio,Pirayeh Shahin Najar,Arzanlou Mohsen The Microbiological Society of Korea 2005 The journal of microbiology Vol.43 No.4
Heat-labile enterotoxin B subunit (LTB) of enterotoxigenic Escherichia coli (ETEC) is both a strong mucosal adjuvant and immunogen. It is a subunit vaccine candidate to be used against ETEC-induced diarrhea. It has already been expressed in several bacterial and plant systems. In order to construct yeast expressing vector for the LTB protein, the eltB gene encoding LTB was amplified from a human origin enterotoxigenic E. coli DNA by PCR. The expression plasmid pLTB83 was constructed by inserting the eltB gene into the pYES2 shuttle vector immediately downstream of the GAL1 promoter. The recombinant vector was transformed into S. cerevisiae and was then induced by galactose. The LTB protein was detected in the total soluble protein of the yeast by SDS-PAGE analysis. Quantitative ELISA showed that the maximum amount of LTB protein expressed in the yeast was approximately $1.9\%$ of the total soluble protein. Immunoblotting analysis showed the yeast-derived LTB protein was antigenically indistinguishable from bacterial LTB protein. Since the whole-recombinant yeast has been introduced as a new vaccine formulation the expression of LTB in S. cerevisiae can offer an inexpensive yet effective strategy to protect against ETEC, especially in developing countries where it is needed most.
Elnaz Khadivinia,Hakimeh Sharafi,Faranak Hadi,Hossein Shahbani Zahiri,Sima Modiri,Azadeh Tohidi,Amir Mousavi,Ali Hatef Salmanian,Kambiz Akbari Noghabi 한국공업화학회 2014 Journal of Industrial and Engineering Chemistry Vol.20 No.6
In this study, biosorption of cadmium (II) ions from aqueous solutions by a glyphosate degradingbacterium, Ochrobactrum sp. GDOS, was investigated in batch conditions. The isolate was able to utilize3 mM GP as the sole phosphorous source, favorable to bacterium growth and survival. The effect ofdifferent basic parameters such as initial pH, contact time, initial concentrations of cadmium ion andtemperature on cadmium uptake was evaluated. The adsorption process for Cd (II) is well fitted withLangmuir adsorption isotherm. Experimental data were also tested in terms of biosorption kinetics usingpseudo-first-order and pseudo-second-order kineticmodels. Maximummetal uptake qmax was obtainedas 83.33 mg g1. The sorption process of cadmium onto the Ochrobactrum sp. GDOS biomass followedsecond-order rate kinetic (R2 = 0.9986). A high desorption efficiency was obtained in pH 2. Reusability ofthe biomass was examined under successive biosorption–desorption cycle repeated thrice. Thecharacteristics of the possible interactions between biosorbent and metal ions were also evaluated byscanning electron microscope (SEM), Fourier transform infrared (FT-IR) and X-ray diffraction analysis.