An LTB-entrapped protein in PLGA nanoparticles preserves against enterotoxin of enterotoxigenic Escherichia coli
Objective(s): Enterotoxigenic Escherichia coli (ETEC) is known as the most common bacterial causes of diarrheal diseases related to morbidity and mortality. Heat-labile enterotoxin (LT) is a part of major virulence factors in ETEC pathogenesis. Antigen entrapment into nanoparticles (NPs) can protect...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Emad Kordbacheh [verfasserIn] Shahram Nazarian [verfasserIn] Davood Sadeghi [verfasserIn] Abbas Hajizade [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2018 |
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| Schlagwörter: |
Enterotoxigenic Escherichia coli |
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| Übergeordnetes Werk: |
In: Iranian Journal of Basic Medical Sciences - Mashhad University of Medical Sciences, 2009, 21(2018), 5, Seite 517-524 |
|---|---|
| Übergeordnetes Werk: |
volume:21 ; year:2018 ; number:5 ; pages:517-524 |
| Links: |
Link aufrufen |
|---|
| DOI / URN: |
10.22038/ijbms.2018.27017.6609 |
|---|
| Katalog-ID: |
DOAJ037316540 |
|---|
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| 245 | 1 | 3 | |a An LTB-entrapped protein in PLGA nanoparticles preserves against enterotoxin of enterotoxigenic Escherichia coli |
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| 520 | |a Objective(s): Enterotoxigenic Escherichia coli (ETEC) is known as the most common bacterial causes of diarrheal diseases related to morbidity and mortality. Heat-labile enterotoxin (LT) is a part of major virulence factors in ETEC pathogenesis. Antigen entrapment into nanoparticles (NPs) can protect them and enhance their immunogenicity.Materials and Methods: In the present study, recombinant LTB protein was expressed in E. coli BL21 (DE3) and purified by an Ni-NTA agarose column. The protein was entrapped in PLGA polymer by the double emulsion method. NPs were characterized physicochemically and the protein release from the NPs was evaluated. ELISA assay was performed for investigation of raised antibody against the recombinant protein in mice. The anti-toxicity and anti-adherence attributes of the immune sera against ETEC were also evaluated.Results: It showed the successful cloning of a 313 bp DNA fragment encoding LTB protein in the pET28a vector. Over-expression in BL21 (DE3) led to the formation of corresponding 15.5 kDa protein bands in the SDS-PAGE gel. Western blotting by using anti-CTX confirmed the purified LTB. Protein-entrapped NPs had a spherical shape with the size of 238 nm mean diameter and 85% entrapment efficiency. Immunological analyses showed the production of a high titer of specific IgG antibody in immunized animals. The neutralizing antibody in the sera of immunized animals was approved by GM1 binding and Ileal loop assays.Conclusion: The results indicate the efficacy of the entrapped LTB protein as an effective immunogen which induces the humoral responses. | ||
| 650 | 4 | |a Enterotoxigenic Escherichia coli | |
| 650 | 4 | |a Heat-labile enterotoxin Immunization | |
| 650 | 4 | |a Nanoparticle | |
| 650 | 4 | |a PLGA | |
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| 700 | 0 | |a Shahram Nazarian |e verfasserin |4 aut | |
| 700 | 0 | |a Davood Sadeghi |e verfasserin |4 aut | |
| 700 | 0 | |a Abbas Hajizade |e verfasserin |4 aut | |
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10.22038/ijbms.2018.27017.6609 doi (DE-627)DOAJ037316540 (DE-599)DOAJ302aff78ae644a5bbd014ad2bd6b21ca DE-627 ger DE-627 rakwb eng Emad Kordbacheh verfasserin aut An LTB-entrapped protein in PLGA nanoparticles preserves against enterotoxin of enterotoxigenic Escherichia coli 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Objective(s): Enterotoxigenic Escherichia coli (ETEC) is known as the most common bacterial causes of diarrheal diseases related to morbidity and mortality. Heat-labile enterotoxin (LT) is a part of major virulence factors in ETEC pathogenesis. Antigen entrapment into nanoparticles (NPs) can protect them and enhance their immunogenicity.Materials and Methods: In the present study, recombinant LTB protein was expressed in E. coli BL21 (DE3) and purified by an Ni-NTA agarose column. The protein was entrapped in PLGA polymer by the double emulsion method. NPs were characterized physicochemically and the protein release from the NPs was evaluated. ELISA assay was performed for investigation of raised antibody against the recombinant protein in mice. The anti-toxicity and anti-adherence attributes of the immune sera against ETEC were also evaluated.Results: It showed the successful cloning of a 313 bp DNA fragment encoding LTB protein in the pET28a vector. Over-expression in BL21 (DE3) led to the formation of corresponding 15.5 kDa protein bands in the SDS-PAGE gel. Western blotting by using anti-CTX confirmed the purified LTB. Protein-entrapped NPs had a spherical shape with the size of 238 nm mean diameter and 85% entrapment efficiency. Immunological analyses showed the production of a high titer of specific IgG antibody in immunized animals. The neutralizing antibody in the sera of immunized animals was approved by GM1 binding and Ileal loop assays.Conclusion: The results indicate the efficacy of the entrapped LTB protein as an effective immunogen which induces the humoral responses. Enterotoxigenic Escherichia coli Heat-labile enterotoxin Immunization Nanoparticle PLGA Medicine R Shahram Nazarian verfasserin aut Davood Sadeghi verfasserin aut Abbas Hajizade verfasserin aut In Iranian Journal of Basic Medical Sciences Mashhad University of Medical Sciences, 2009 21(2018), 5, Seite 517-524 (DE-627)602537185 (DE-600)2500485-2 20083874 nnns volume:21 year:2018 number:5 pages:517-524 https://doi.org/10.22038/ijbms.2018.27017.6609 kostenfrei https://doaj.org/article/302aff78ae644a5bbd014ad2bd6b21ca kostenfrei http://ijbms.mums.ac.ir/article_10545_abc4c98e982432fb8391d05f1a9faaf5.pdf kostenfrei https://doaj.org/toc/2008-3866 Journal toc kostenfrei https://doaj.org/toc/2008-3874 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2018 5 517-524 |
| spelling |
10.22038/ijbms.2018.27017.6609 doi (DE-627)DOAJ037316540 (DE-599)DOAJ302aff78ae644a5bbd014ad2bd6b21ca DE-627 ger DE-627 rakwb eng Emad Kordbacheh verfasserin aut An LTB-entrapped protein in PLGA nanoparticles preserves against enterotoxin of enterotoxigenic Escherichia coli 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Objective(s): Enterotoxigenic Escherichia coli (ETEC) is known as the most common bacterial causes of diarrheal diseases related to morbidity and mortality. Heat-labile enterotoxin (LT) is a part of major virulence factors in ETEC pathogenesis. Antigen entrapment into nanoparticles (NPs) can protect them and enhance their immunogenicity.Materials and Methods: In the present study, recombinant LTB protein was expressed in E. coli BL21 (DE3) and purified by an Ni-NTA agarose column. The protein was entrapped in PLGA polymer by the double emulsion method. NPs were characterized physicochemically and the protein release from the NPs was evaluated. ELISA assay was performed for investigation of raised antibody against the recombinant protein in mice. The anti-toxicity and anti-adherence attributes of the immune sera against ETEC were also evaluated.Results: It showed the successful cloning of a 313 bp DNA fragment encoding LTB protein in the pET28a vector. Over-expression in BL21 (DE3) led to the formation of corresponding 15.5 kDa protein bands in the SDS-PAGE gel. Western blotting by using anti-CTX confirmed the purified LTB. Protein-entrapped NPs had a spherical shape with the size of 238 nm mean diameter and 85% entrapment efficiency. Immunological analyses showed the production of a high titer of specific IgG antibody in immunized animals. The neutralizing antibody in the sera of immunized animals was approved by GM1 binding and Ileal loop assays.Conclusion: The results indicate the efficacy of the entrapped LTB protein as an effective immunogen which induces the humoral responses. Enterotoxigenic Escherichia coli Heat-labile enterotoxin Immunization Nanoparticle PLGA Medicine R Shahram Nazarian verfasserin aut Davood Sadeghi verfasserin aut Abbas Hajizade verfasserin aut In Iranian Journal of Basic Medical Sciences Mashhad University of Medical Sciences, 2009 21(2018), 5, Seite 517-524 (DE-627)602537185 (DE-600)2500485-2 20083874 nnns volume:21 year:2018 number:5 pages:517-524 https://doi.org/10.22038/ijbms.2018.27017.6609 kostenfrei https://doaj.org/article/302aff78ae644a5bbd014ad2bd6b21ca kostenfrei http://ijbms.mums.ac.ir/article_10545_abc4c98e982432fb8391d05f1a9faaf5.pdf kostenfrei https://doaj.org/toc/2008-3866 Journal toc kostenfrei https://doaj.org/toc/2008-3874 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2018 5 517-524 |
| allfields_unstemmed |
10.22038/ijbms.2018.27017.6609 doi (DE-627)DOAJ037316540 (DE-599)DOAJ302aff78ae644a5bbd014ad2bd6b21ca DE-627 ger DE-627 rakwb eng Emad Kordbacheh verfasserin aut An LTB-entrapped protein in PLGA nanoparticles preserves against enterotoxin of enterotoxigenic Escherichia coli 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Objective(s): Enterotoxigenic Escherichia coli (ETEC) is known as the most common bacterial causes of diarrheal diseases related to morbidity and mortality. Heat-labile enterotoxin (LT) is a part of major virulence factors in ETEC pathogenesis. Antigen entrapment into nanoparticles (NPs) can protect them and enhance their immunogenicity.Materials and Methods: In the present study, recombinant LTB protein was expressed in E. coli BL21 (DE3) and purified by an Ni-NTA agarose column. The protein was entrapped in PLGA polymer by the double emulsion method. NPs were characterized physicochemically and the protein release from the NPs was evaluated. ELISA assay was performed for investigation of raised antibody against the recombinant protein in mice. The anti-toxicity and anti-adherence attributes of the immune sera against ETEC were also evaluated.Results: It showed the successful cloning of a 313 bp DNA fragment encoding LTB protein in the pET28a vector. Over-expression in BL21 (DE3) led to the formation of corresponding 15.5 kDa protein bands in the SDS-PAGE gel. Western blotting by using anti-CTX confirmed the purified LTB. Protein-entrapped NPs had a spherical shape with the size of 238 nm mean diameter and 85% entrapment efficiency. Immunological analyses showed the production of a high titer of specific IgG antibody in immunized animals. The neutralizing antibody in the sera of immunized animals was approved by GM1 binding and Ileal loop assays.Conclusion: The results indicate the efficacy of the entrapped LTB protein as an effective immunogen which induces the humoral responses. Enterotoxigenic Escherichia coli Heat-labile enterotoxin Immunization Nanoparticle PLGA Medicine R Shahram Nazarian verfasserin aut Davood Sadeghi verfasserin aut Abbas Hajizade verfasserin aut In Iranian Journal of Basic Medical Sciences Mashhad University of Medical Sciences, 2009 21(2018), 5, Seite 517-524 (DE-627)602537185 (DE-600)2500485-2 20083874 nnns volume:21 year:2018 number:5 pages:517-524 https://doi.org/10.22038/ijbms.2018.27017.6609 kostenfrei https://doaj.org/article/302aff78ae644a5bbd014ad2bd6b21ca kostenfrei http://ijbms.mums.ac.ir/article_10545_abc4c98e982432fb8391d05f1a9faaf5.pdf kostenfrei https://doaj.org/toc/2008-3866 Journal toc kostenfrei https://doaj.org/toc/2008-3874 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2018 5 517-524 |
| allfieldsGer |
10.22038/ijbms.2018.27017.6609 doi (DE-627)DOAJ037316540 (DE-599)DOAJ302aff78ae644a5bbd014ad2bd6b21ca DE-627 ger DE-627 rakwb eng Emad Kordbacheh verfasserin aut An LTB-entrapped protein in PLGA nanoparticles preserves against enterotoxin of enterotoxigenic Escherichia coli 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Objective(s): Enterotoxigenic Escherichia coli (ETEC) is known as the most common bacterial causes of diarrheal diseases related to morbidity and mortality. Heat-labile enterotoxin (LT) is a part of major virulence factors in ETEC pathogenesis. Antigen entrapment into nanoparticles (NPs) can protect them and enhance their immunogenicity.Materials and Methods: In the present study, recombinant LTB protein was expressed in E. coli BL21 (DE3) and purified by an Ni-NTA agarose column. The protein was entrapped in PLGA polymer by the double emulsion method. NPs were characterized physicochemically and the protein release from the NPs was evaluated. ELISA assay was performed for investigation of raised antibody against the recombinant protein in mice. The anti-toxicity and anti-adherence attributes of the immune sera against ETEC were also evaluated.Results: It showed the successful cloning of a 313 bp DNA fragment encoding LTB protein in the pET28a vector. Over-expression in BL21 (DE3) led to the formation of corresponding 15.5 kDa protein bands in the SDS-PAGE gel. Western blotting by using anti-CTX confirmed the purified LTB. Protein-entrapped NPs had a spherical shape with the size of 238 nm mean diameter and 85% entrapment efficiency. Immunological analyses showed the production of a high titer of specific IgG antibody in immunized animals. The neutralizing antibody in the sera of immunized animals was approved by GM1 binding and Ileal loop assays.Conclusion: The results indicate the efficacy of the entrapped LTB protein as an effective immunogen which induces the humoral responses. Enterotoxigenic Escherichia coli Heat-labile enterotoxin Immunization Nanoparticle PLGA Medicine R Shahram Nazarian verfasserin aut Davood Sadeghi verfasserin aut Abbas Hajizade verfasserin aut In Iranian Journal of Basic Medical Sciences Mashhad University of Medical Sciences, 2009 21(2018), 5, Seite 517-524 (DE-627)602537185 (DE-600)2500485-2 20083874 nnns volume:21 year:2018 number:5 pages:517-524 https://doi.org/10.22038/ijbms.2018.27017.6609 kostenfrei https://doaj.org/article/302aff78ae644a5bbd014ad2bd6b21ca kostenfrei http://ijbms.mums.ac.ir/article_10545_abc4c98e982432fb8391d05f1a9faaf5.pdf kostenfrei https://doaj.org/toc/2008-3866 Journal toc kostenfrei https://doaj.org/toc/2008-3874 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2018 5 517-524 |
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10.22038/ijbms.2018.27017.6609 doi (DE-627)DOAJ037316540 (DE-599)DOAJ302aff78ae644a5bbd014ad2bd6b21ca DE-627 ger DE-627 rakwb eng Emad Kordbacheh verfasserin aut An LTB-entrapped protein in PLGA nanoparticles preserves against enterotoxin of enterotoxigenic Escherichia coli 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Objective(s): Enterotoxigenic Escherichia coli (ETEC) is known as the most common bacterial causes of diarrheal diseases related to morbidity and mortality. Heat-labile enterotoxin (LT) is a part of major virulence factors in ETEC pathogenesis. Antigen entrapment into nanoparticles (NPs) can protect them and enhance their immunogenicity.Materials and Methods: In the present study, recombinant LTB protein was expressed in E. coli BL21 (DE3) and purified by an Ni-NTA agarose column. The protein was entrapped in PLGA polymer by the double emulsion method. NPs were characterized physicochemically and the protein release from the NPs was evaluated. ELISA assay was performed for investigation of raised antibody against the recombinant protein in mice. The anti-toxicity and anti-adherence attributes of the immune sera against ETEC were also evaluated.Results: It showed the successful cloning of a 313 bp DNA fragment encoding LTB protein in the pET28a vector. Over-expression in BL21 (DE3) led to the formation of corresponding 15.5 kDa protein bands in the SDS-PAGE gel. Western blotting by using anti-CTX confirmed the purified LTB. Protein-entrapped NPs had a spherical shape with the size of 238 nm mean diameter and 85% entrapment efficiency. Immunological analyses showed the production of a high titer of specific IgG antibody in immunized animals. The neutralizing antibody in the sera of immunized animals was approved by GM1 binding and Ileal loop assays.Conclusion: The results indicate the efficacy of the entrapped LTB protein as an effective immunogen which induces the humoral responses. Enterotoxigenic Escherichia coli Heat-labile enterotoxin Immunization Nanoparticle PLGA Medicine R Shahram Nazarian verfasserin aut Davood Sadeghi verfasserin aut Abbas Hajizade verfasserin aut In Iranian Journal of Basic Medical Sciences Mashhad University of Medical Sciences, 2009 21(2018), 5, Seite 517-524 (DE-627)602537185 (DE-600)2500485-2 20083874 nnns volume:21 year:2018 number:5 pages:517-524 https://doi.org/10.22038/ijbms.2018.27017.6609 kostenfrei https://doaj.org/article/302aff78ae644a5bbd014ad2bd6b21ca kostenfrei http://ijbms.mums.ac.ir/article_10545_abc4c98e982432fb8391d05f1a9faaf5.pdf kostenfrei https://doaj.org/toc/2008-3866 Journal toc kostenfrei https://doaj.org/toc/2008-3874 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2018 5 517-524 |
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ltb-entrapped protein in plga nanoparticles preserves against enterotoxin of enterotoxigenic escherichia coli |
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An LTB-entrapped protein in PLGA nanoparticles preserves against enterotoxin of enterotoxigenic Escherichia coli |
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Objective(s): Enterotoxigenic Escherichia coli (ETEC) is known as the most common bacterial causes of diarrheal diseases related to morbidity and mortality. Heat-labile enterotoxin (LT) is a part of major virulence factors in ETEC pathogenesis. Antigen entrapment into nanoparticles (NPs) can protect them and enhance their immunogenicity.Materials and Methods: In the present study, recombinant LTB protein was expressed in E. coli BL21 (DE3) and purified by an Ni-NTA agarose column. The protein was entrapped in PLGA polymer by the double emulsion method. NPs were characterized physicochemically and the protein release from the NPs was evaluated. ELISA assay was performed for investigation of raised antibody against the recombinant protein in mice. The anti-toxicity and anti-adherence attributes of the immune sera against ETEC were also evaluated.Results: It showed the successful cloning of a 313 bp DNA fragment encoding LTB protein in the pET28a vector. Over-expression in BL21 (DE3) led to the formation of corresponding 15.5 kDa protein bands in the SDS-PAGE gel. Western blotting by using anti-CTX confirmed the purified LTB. Protein-entrapped NPs had a spherical shape with the size of 238 nm mean diameter and 85% entrapment efficiency. Immunological analyses showed the production of a high titer of specific IgG antibody in immunized animals. The neutralizing antibody in the sera of immunized animals was approved by GM1 binding and Ileal loop assays.Conclusion: The results indicate the efficacy of the entrapped LTB protein as an effective immunogen which induces the humoral responses. |
| abstractGer |
Objective(s): Enterotoxigenic Escherichia coli (ETEC) is known as the most common bacterial causes of diarrheal diseases related to morbidity and mortality. Heat-labile enterotoxin (LT) is a part of major virulence factors in ETEC pathogenesis. Antigen entrapment into nanoparticles (NPs) can protect them and enhance their immunogenicity.Materials and Methods: In the present study, recombinant LTB protein was expressed in E. coli BL21 (DE3) and purified by an Ni-NTA agarose column. The protein was entrapped in PLGA polymer by the double emulsion method. NPs were characterized physicochemically and the protein release from the NPs was evaluated. ELISA assay was performed for investigation of raised antibody against the recombinant protein in mice. The anti-toxicity and anti-adherence attributes of the immune sera against ETEC were also evaluated.Results: It showed the successful cloning of a 313 bp DNA fragment encoding LTB protein in the pET28a vector. Over-expression in BL21 (DE3) led to the formation of corresponding 15.5 kDa protein bands in the SDS-PAGE gel. Western blotting by using anti-CTX confirmed the purified LTB. Protein-entrapped NPs had a spherical shape with the size of 238 nm mean diameter and 85% entrapment efficiency. Immunological analyses showed the production of a high titer of specific IgG antibody in immunized animals. The neutralizing antibody in the sera of immunized animals was approved by GM1 binding and Ileal loop assays.Conclusion: The results indicate the efficacy of the entrapped LTB protein as an effective immunogen which induces the humoral responses. |
| abstract_unstemmed |
Objective(s): Enterotoxigenic Escherichia coli (ETEC) is known as the most common bacterial causes of diarrheal diseases related to morbidity and mortality. Heat-labile enterotoxin (LT) is a part of major virulence factors in ETEC pathogenesis. Antigen entrapment into nanoparticles (NPs) can protect them and enhance their immunogenicity.Materials and Methods: In the present study, recombinant LTB protein was expressed in E. coli BL21 (DE3) and purified by an Ni-NTA agarose column. The protein was entrapped in PLGA polymer by the double emulsion method. NPs were characterized physicochemically and the protein release from the NPs was evaluated. ELISA assay was performed for investigation of raised antibody against the recombinant protein in mice. The anti-toxicity and anti-adherence attributes of the immune sera against ETEC were also evaluated.Results: It showed the successful cloning of a 313 bp DNA fragment encoding LTB protein in the pET28a vector. Over-expression in BL21 (DE3) led to the formation of corresponding 15.5 kDa protein bands in the SDS-PAGE gel. Western blotting by using anti-CTX confirmed the purified LTB. Protein-entrapped NPs had a spherical shape with the size of 238 nm mean diameter and 85% entrapment efficiency. Immunological analyses showed the production of a high titer of specific IgG antibody in immunized animals. The neutralizing antibody in the sera of immunized animals was approved by GM1 binding and Ileal loop assays.Conclusion: The results indicate the efficacy of the entrapped LTB protein as an effective immunogen which induces the humoral responses. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">DOAJ037316540</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230308002852.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">230227s2018 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.22038/ijbms.2018.27017.6609</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)DOAJ037316540</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)DOAJ302aff78ae644a5bbd014ad2bd6b21ca</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="0" ind2=" "><subfield code="a">Emad Kordbacheh</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="3"><subfield code="a">An LTB-entrapped protein in PLGA nanoparticles preserves against enterotoxin of enterotoxigenic Escherichia coli</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2018</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Objective(s): Enterotoxigenic Escherichia coli (ETEC) is known as the most common bacterial causes of diarrheal diseases related to morbidity and mortality. Heat-labile enterotoxin (LT) is a part of major virulence factors in ETEC pathogenesis. Antigen entrapment into nanoparticles (NPs) can protect them and enhance their immunogenicity.Materials and Methods: In the present study, recombinant LTB protein was expressed in E. coli BL21 (DE3) and purified by an Ni-NTA agarose column. The protein was entrapped in PLGA polymer by the double emulsion method. NPs were characterized physicochemically and the protein release from the NPs was evaluated. ELISA assay was performed for investigation of raised antibody against the recombinant protein in mice. The anti-toxicity and anti-adherence attributes of the immune sera against ETEC were also evaluated.Results: It showed the successful cloning of a 313 bp DNA fragment encoding LTB protein in the pET28a vector. Over-expression in BL21 (DE3) led to the formation of corresponding 15.5 kDa protein bands in the SDS-PAGE gel. Western blotting by using anti-CTX confirmed the purified LTB. Protein-entrapped NPs had a spherical shape with the size of 238 nm mean diameter and 85% entrapment efficiency. Immunological analyses showed the production of a high titer of specific IgG antibody in immunized animals. The neutralizing antibody in the sera of immunized animals was approved by GM1 binding and Ileal loop assays.Conclusion: The results indicate the efficacy of the entrapped LTB protein as an effective immunogen which induces the humoral responses.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Enterotoxigenic Escherichia coli</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Heat-labile enterotoxin Immunization</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Nanoparticle</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">PLGA</subfield></datafield><datafield tag="653" ind1=" " ind2="0"><subfield code="a">Medicine</subfield></datafield><datafield tag="653" ind1=" " ind2="0"><subfield code="a">R</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Shahram Nazarian</subfield><subfield code="e">verfasserin</subfield><subfield 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