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Heterologous expression, immunochemical and computational analysis of recombinant human interferon alpha 2b
Interferon alpha 2b (IFNα-2b) is an important cytokine and used for antiviral and anticancer treatment. The low cost production of IFNα-2b with high biological activity is necessary to provide the interferon therapy to the hepatitis patients in Pakistan. In the present study, human interferon alpha...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer International Publishing AG
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3695685/ https://www.ncbi.nlm.nih.gov/pubmed/23875128 http://dx.doi.org/10.1186/2193-1801-2-264 |
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author | Gull, Iram Samra, Zahoor Qadir Aslam, Muhammad Shahbaz Athar, Muhammad Amin |
author_facet | Gull, Iram Samra, Zahoor Qadir Aslam, Muhammad Shahbaz Athar, Muhammad Amin |
author_sort | Gull, Iram |
collection | PubMed |
description | Interferon alpha 2b (IFNα-2b) is an important cytokine and used for antiviral and anticancer treatment. The low cost production of IFNα-2b with high biological activity is necessary to provide the interferon therapy to the hepatitis patients in Pakistan. In the present study, human interferon alpha 2b (hIFNα-2b) gene from a healthy person was cloned and overexpressed in E. coli BL21(DE3). The molecular weight of the expressed hIFNα-2b is 19 kDa. The over expressed recombinant hIFNα-2b was checked by ELISA using antibodies raised against commercially available hIFNα-2b. The biocomputational analysis of recombinant hIFNα-2b gene showed the 99.9% nucleotide sequence and 100% deduced amino acid sequence homology with reported sequences of IFNα-2b. The predicted 3D-structure showed mainly five α-helices, one 3(10) helix and two disulfide bonds at Cys1-Cys98 and Cys129-Cys138. The amino acid sequence alignment indicated that the disulfide linkage position is conserved in all IFNα family members. On the basis of sequence homology among interferon alpha family, new potent variants of hIFNα-2b with enhance efficacy can be produced. Indigenous production of IFNα-2b from gene of local population will reduce the cost and increase tolerability of interferon therapy. |
format | Online Article Text |
id | pubmed-3695685 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Springer International Publishing AG |
record_format | MEDLINE/PubMed |
spelling | pubmed-36956852013-07-18 Heterologous expression, immunochemical and computational analysis of recombinant human interferon alpha 2b Gull, Iram Samra, Zahoor Qadir Aslam, Muhammad Shahbaz Athar, Muhammad Amin Springerplus Research Interferon alpha 2b (IFNα-2b) is an important cytokine and used for antiviral and anticancer treatment. The low cost production of IFNα-2b with high biological activity is necessary to provide the interferon therapy to the hepatitis patients in Pakistan. In the present study, human interferon alpha 2b (hIFNα-2b) gene from a healthy person was cloned and overexpressed in E. coli BL21(DE3). The molecular weight of the expressed hIFNα-2b is 19 kDa. The over expressed recombinant hIFNα-2b was checked by ELISA using antibodies raised against commercially available hIFNα-2b. The biocomputational analysis of recombinant hIFNα-2b gene showed the 99.9% nucleotide sequence and 100% deduced amino acid sequence homology with reported sequences of IFNα-2b. The predicted 3D-structure showed mainly five α-helices, one 3(10) helix and two disulfide bonds at Cys1-Cys98 and Cys129-Cys138. The amino acid sequence alignment indicated that the disulfide linkage position is conserved in all IFNα family members. On the basis of sequence homology among interferon alpha family, new potent variants of hIFNα-2b with enhance efficacy can be produced. Indigenous production of IFNα-2b from gene of local population will reduce the cost and increase tolerability of interferon therapy. Springer International Publishing AG 2013-06-15 /pmc/articles/PMC3695685/ /pubmed/23875128 http://dx.doi.org/10.1186/2193-1801-2-264 Text en © Gull et al.; licensee Springer. 2013 This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Gull, Iram Samra, Zahoor Qadir Aslam, Muhammad Shahbaz Athar, Muhammad Amin Heterologous expression, immunochemical and computational analysis of recombinant human interferon alpha 2b |
title | Heterologous expression, immunochemical and computational analysis of recombinant human interferon alpha 2b |
title_full | Heterologous expression, immunochemical and computational analysis of recombinant human interferon alpha 2b |
title_fullStr | Heterologous expression, immunochemical and computational analysis of recombinant human interferon alpha 2b |
title_full_unstemmed | Heterologous expression, immunochemical and computational analysis of recombinant human interferon alpha 2b |
title_short | Heterologous expression, immunochemical and computational analysis of recombinant human interferon alpha 2b |
title_sort | heterologous expression, immunochemical and computational analysis of recombinant human interferon alpha 2b |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3695685/ https://www.ncbi.nlm.nih.gov/pubmed/23875128 http://dx.doi.org/10.1186/2193-1801-2-264 |
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