Protein refolding based on high hydrostatic pressure and alkaline pH: Application on a recombinant dengue virus NS1 protein
In this study we evaluated the association of high hydrostatic pressure (HHP) and alkaline pH as a minimally denaturing condition for the solubilization of inclusion bodies (IBs) generated by recombinant proteins expressed by Escherichia coli strains. The method was successfully applied to a recombi...
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| creator | Chura-Chambi, Rosa Maria da Silva, Cleide Mara Rosa Pereira, Lennon Ramos Bartolini, Paolo Ferreira, Luis Carlos de Souza Morganti, Ligia |
| description | In this study we evaluated the association of high hydrostatic pressure (HHP) and alkaline pH as a minimally denaturing condition for the solubilization of inclusion bodies (IBs) generated by recombinant proteins expressed by Escherichia coli strains. The method was successfully applied to a recombinant form of the dengue virus (DENV) non-structural protein 1 (NS1). The minimal pH for IBs solubilization at 1 bar was 12 while a pH of 10 was sufficient for solubilization at HHP: 2.4 kbar for 90 min and 0.4 kbar for 14 h 30 min. An optimal refolding condition was achieved by compression of IBs at HHP and pH 10.5 in the presence of arginine, oxidized and reduced glutathiones, providing much higher yields (up to 8-fold) than association of HHP and GdnHCl via an established protocol. The refolded NS1, 109 ± 9.5 mg/L bacterial culture was recovered mainly as monomer and dimer, corresponding up to 90% of the total protein and remaining immunologically active. The proposed conditions represent an alternative for the refolding of immunologically active recombinant proteins expressed as IBs. |
| doi_str_mv | 10.1371/journal.pone.0211162 |
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The method was successfully applied to a recombinant form of the dengue virus (DENV) non-structural protein 1 (NS1). The minimal pH for IBs solubilization at 1 bar was 12 while a pH of 10 was sufficient for solubilization at HHP: 2.4 kbar for 90 min and 0.4 kbar for 14 h 30 min. An optimal refolding condition was achieved by compression of IBs at HHP and pH 10.5 in the presence of arginine, oxidized and reduced glutathiones, providing much higher yields (up to 8-fold) than association of HHP and GdnHCl via an established protocol. The refolded NS1, 109 ± 9.5 mg/L bacterial culture was recovered mainly as monomer and dimer, corresponding up to 90% of the total protein and remaining immunologically active. The proposed conditions represent an alternative for the refolding of immunologically active recombinant proteins expressed as IBs.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0211162</identifier><identifier>PMID: 30682103</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Alkalies ; Antigens ; Arginine ; Biology and Life Sciences ; Compression ; Dengue ; Dengue fever ; Dengue Virus - chemistry ; Dengue Virus - genetics ; Dimers ; E coli ; Escherichia coli ; Gene expression ; Growth hormones ; Hydrogen-Ion Concentration ; Hydrostatic Pressure ; Inclusion bodies ; Medicine and Health Sciences ; NS1 protein ; pH effects ; Physical Sciences ; Pressure ; Protein folding ; Protein Refolding ; Proteins ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Research and Analysis Methods ; Solubilization ; Vaccines ; Vector-borne diseases ; Viral diseases ; Viral Nonstructural Proteins - chemistry ; Viral Nonstructural Proteins - genetics ; Viruses</subject><ispartof>PloS one, 2019-01, Vol.14 (1), p.e0211162-e0211162</ispartof><rights>COPYRIGHT 2019 Public Library of Science</rights><rights>2019 Chura-Chambi et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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The method was successfully applied to a recombinant form of the dengue virus (DENV) non-structural protein 1 (NS1). The minimal pH for IBs solubilization at 1 bar was 12 while a pH of 10 was sufficient for solubilization at HHP: 2.4 kbar for 90 min and 0.4 kbar for 14 h 30 min. An optimal refolding condition was achieved by compression of IBs at HHP and pH 10.5 in the presence of arginine, oxidized and reduced glutathiones, providing much higher yields (up to 8-fold) than association of HHP and GdnHCl via an established protocol. The refolded NS1, 109 ± 9.5 mg/L bacterial culture was recovered mainly as monomer and dimer, corresponding up to 90% of the total protein and remaining immunologically active. The proposed conditions represent an alternative for the refolding of immunologically active recombinant proteins expressed as IBs.</description><subject>Alkalies</subject><subject>Antigens</subject><subject>Arginine</subject><subject>Biology and Life Sciences</subject><subject>Compression</subject><subject>Dengue</subject><subject>Dengue fever</subject><subject>Dengue Virus - chemistry</subject><subject>Dengue Virus - genetics</subject><subject>Dimers</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Gene expression</subject><subject>Growth hormones</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrostatic Pressure</subject><subject>Inclusion bodies</subject><subject>Medicine and Health Sciences</subject><subject>NS1 protein</subject><subject>pH effects</subject><subject>Physical Sciences</subject><subject>Pressure</subject><subject>Protein folding</subject><subject>Protein Refolding</subject><subject>Proteins</subject><subject>Recombinant Proteins - 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The method was successfully applied to a recombinant form of the dengue virus (DENV) non-structural protein 1 (NS1). The minimal pH for IBs solubilization at 1 bar was 12 while a pH of 10 was sufficient for solubilization at HHP: 2.4 kbar for 90 min and 0.4 kbar for 14 h 30 min. An optimal refolding condition was achieved by compression of IBs at HHP and pH 10.5 in the presence of arginine, oxidized and reduced glutathiones, providing much higher yields (up to 8-fold) than association of HHP and GdnHCl via an established protocol. The refolded NS1, 109 ± 9.5 mg/L bacterial culture was recovered mainly as monomer and dimer, corresponding up to 90% of the total protein and remaining immunologically active. The proposed conditions represent an alternative for the refolding of immunologically active recombinant proteins expressed as IBs.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>30682103</pmid><doi>10.1371/journal.pone.0211162</doi><tpages>e0211162</tpages><orcidid>https://orcid.org/0000-0002-7870-1793</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Alkalies Antigens Arginine Biology and Life Sciences Compression Dengue Dengue fever Dengue Virus - chemistry Dengue Virus - genetics Dimers E coli Escherichia coli Gene expression Growth hormones Hydrogen-Ion Concentration Hydrostatic Pressure Inclusion bodies Medicine and Health Sciences NS1 protein pH effects Physical Sciences Pressure Protein folding Protein Refolding Proteins Recombinant Proteins - chemistry Recombinant Proteins - genetics Research and Analysis Methods Solubilization Vaccines Vector-borne diseases Viral diseases Viral Nonstructural Proteins - chemistry Viral Nonstructural Proteins - genetics Viruses |
| title | Protein refolding based on high hydrostatic pressure and alkaline pH: Application on a recombinant dengue virus NS1 protein |
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