Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography
Visceral leishmaniasis, a disease caused by Leishmania infantum chagasi, represents a major public health problem in many areas of the world. However, there is currently no vaccine for human use. The aim of this work was to purify the 503 antigen of Leishmania i. chagasi directly from unclarified...
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ri-123456789-324822021-05-10T19:50:35Z Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography Santos, Everaldo Silvino dos Sousa Junior, Francisco Caninde de Vaz, Michelle Rossana Ferreira Padilha, Carlos Eduardo de Araújo Chibério, Abimaelle Silva Martins, Daniella Regina Arantes Macedo, Gorete Ribeiro de Expanded bed adsorption Leishmania infantum chagasi Recombinant protein purification Unclarified bacterial homogenate Visceral leishmaniasis Visceral leishmaniasis, a disease caused by Leishmania infantum chagasi, represents a major public health problem in many areas of the world. However, there is currently no vaccine for human use. The aim of this work was to purify the 503 antigen of Leishmania i. chagasi directly from unclarified Escherichia coli feedstock through expanded bed adsorption (EBA) chromatography. Batch experiments were performed to optimize the adsorption and elution conditions of the antigen onto a STREAMLINETM Chelating resin using two central composite rotatable designs (CCRD). The results showed that the optimal binding con- ditions of the 503 antigen were pH 8.0 in the presence of 2.4 M NaCl. For the elution of the target protein, the optimized conditions included the presence of 600.0 mM imidazole. The adsorption isothermal data of the 503 antigen were fitted to the Langmuir adsorption isotherm. The EBA experiment successfully recovered 59.2% of the 503 antigen from the unclarified E. coli homogenate with a purification factor of 6.0 2021-05-10T19:50:34Z 2021-05-10T19:50:34Z 2015-04-01 article SOUSA JUNIOR, F. C.; VAZ, M. R. F.; PADILHA, C. E.; CHIBERIO, A. S.; MARTINS, D. R. A.; MACEDO, G. R.; SANTOS, E. S.. Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography. Journal of Chromatography. B (Print), p. 1, 2015. Disponivel em https://www.sciencedirect.com/science/article/abs/pii/S1570023215000719?via%3Dihub. Acesso em: 01 abr. 2021. https://doi.org/10.1016/j.jchromb.2015.01.031 1570-0232 https://repositorio.ufrn.br/handle/123456789/32482 10.1016/j.jchromb.2015.01.031 en Attribution 3.0 Brazil http://creativecommons.org/licenses/by/3.0/br/ application/pdf Elsevier |
institution |
Repositório Institucional |
collection |
RI - UFRN |
language |
English |
topic |
Expanded bed adsorption Leishmania infantum chagasi Recombinant protein purification Unclarified bacterial homogenate Visceral leishmaniasis |
spellingShingle |
Expanded bed adsorption Leishmania infantum chagasi Recombinant protein purification Unclarified bacterial homogenate Visceral leishmaniasis Santos, Everaldo Silvino dos Sousa Junior, Francisco Caninde de Vaz, Michelle Rossana Ferreira Padilha, Carlos Eduardo de Araújo Chibério, Abimaelle Silva Martins, Daniella Regina Arantes Macedo, Gorete Ribeiro de Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography |
description |
Visceral leishmaniasis, a disease caused by Leishmania infantum chagasi, represents a major public health
problem in many areas of the world. However, there is currently no vaccine for human use. The aim of
this work was to purify the 503 antigen of Leishmania i. chagasi directly from unclarified Escherichia coli
feedstock through expanded bed adsorption (EBA) chromatography. Batch experiments were performed
to optimize the adsorption and elution conditions of the antigen onto a STREAMLINETM Chelating resin
using two central composite rotatable designs (CCRD). The results showed that the optimal binding con-
ditions of the 503 antigen were pH 8.0 in the presence of 2.4 M NaCl. For the elution of the target protein,
the optimized conditions included the presence of 600.0 mM imidazole. The adsorption isothermal data
of the 503 antigen were fitted to the Langmuir adsorption isotherm. The EBA experiment successfully
recovered 59.2% of the 503 antigen from the unclarified E. coli homogenate with a purification factor of
6.0 |
format |
article |
author |
Santos, Everaldo Silvino dos Sousa Junior, Francisco Caninde de Vaz, Michelle Rossana Ferreira Padilha, Carlos Eduardo de Araújo Chibério, Abimaelle Silva Martins, Daniella Regina Arantes Macedo, Gorete Ribeiro de |
author_facet |
Santos, Everaldo Silvino dos Sousa Junior, Francisco Caninde de Vaz, Michelle Rossana Ferreira Padilha, Carlos Eduardo de Araújo Chibério, Abimaelle Silva Martins, Daniella Regina Arantes Macedo, Gorete Ribeiro de |
author_sort |
Santos, Everaldo Silvino dos |
title |
Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography |
title_short |
Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography |
title_full |
Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography |
title_fullStr |
Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography |
title_full_unstemmed |
Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography |
title_sort |
recovery and purification of recombinant 503 antigen of leishmania infantum chagasi using expanded bed adsorption chromatography |
publisher |
Elsevier |
publishDate |
2021 |
url |
https://repositorio.ufrn.br/handle/123456789/32482 |
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