Enzyme replacement therapy for Morquio A: an active recombinant N-acetylgalactosamine-6-sulfate sulfatase produced in Escherichia coli BL21
Mucopolysaccharidosis IVA (MPS IVA) is an autosomal recessive disorder caused by N -acetylgalactosamine-6-sulfate sulfatase (GALNS) deficiency. Currently no effective therapies exist for MPS IVA. In this work, production of a recombinant GALNS enzyme (rGALNS) in Escherichia coli BL21 strain was stud...
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| Veröffentlicht in: | Journal of industrial microbiology & biotechnology 2010-11, Vol.37 (11), p.1193-1201 |
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| creator | Rodríguez, Alexander Espejo, Ángela J. Hernández, Alejandra Velásquez, Olga L. Lizaraso, Lina M. Cordoba, Henry A. Sánchez, Oscar F. Alméciga-Díaz, Carlos J. Barrera, Luis A. |
| description | Mucopolysaccharidosis IVA (MPS IVA) is an autosomal recessive disorder caused by
N
-acetylgalactosamine-6-sulfate sulfatase (GALNS) deficiency. Currently no effective therapies exist for MPS IVA. In this work, production of a recombinant GALNS enzyme (rGALNS) in
Escherichia coli
BL21 strain was studied. At shake scale, the effect of glucose concentration on microorganism growth, and microorganism culture and induction times on rGALNS production were evaluated. At bench scale, the effect of aeration and agitation on microorganism growth, and culture and induction times were evaluated. The highest enzyme activity levels at shake scale were observed in 12 h culture after 2–4 h induction. At bench scale the highest enzyme activity levels were observed after 2 h induction. rGALNS amounts in inclusion bodies fraction were up to 17-fold higher than those observed in the soluble fraction. However, the highest levels of active enzyme were found in the soluble fraction. Western blot analysis showed the presence of a 50-kDa band, in both soluble and inclusion bodies fractions. These results show for the first time the feasibility and potential of production of active rGALNS in a prokaryotic system for development of enzyme replacement therapy for MPS IVA disease. |
| doi_str_mv | 10.1007/s10295-010-0766-x |
| format | Article |
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N
-acetylgalactosamine-6-sulfate sulfatase (GALNS) deficiency. Currently no effective therapies exist for MPS IVA. In this work, production of a recombinant GALNS enzyme (rGALNS) in
Escherichia coli
BL21 strain was studied. At shake scale, the effect of glucose concentration on microorganism growth, and microorganism culture and induction times on rGALNS production were evaluated. At bench scale, the effect of aeration and agitation on microorganism growth, and culture and induction times were evaluated. The highest enzyme activity levels at shake scale were observed in 12 h culture after 2–4 h induction. At bench scale the highest enzyme activity levels were observed after 2 h induction. rGALNS amounts in inclusion bodies fraction were up to 17-fold higher than those observed in the soluble fraction. However, the highest levels of active enzyme were found in the soluble fraction. Western blot analysis showed the presence of a 50-kDa band, in both soluble and inclusion bodies fractions. These results show for the first time the feasibility and potential of production of active rGALNS in a prokaryotic system for development of enzyme replacement therapy for MPS IVA disease.</description><identifier>ISSN: 1367-5435</identifier><identifier>EISSN: 1476-5535</identifier><identifier>DOI: 10.1007/s10295-010-0766-x</identifier><identifier>PMID: 20582614</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer-Verlag</publisher><subject>Biochemistry ; Bioengineering ; Bioinformatics ; Biological and medical sciences ; Biomedical and Life Sciences ; Biotechnology ; Blotting, Western ; Chondroitinsulfatases - biosynthesis ; Chondroitinsulfatases - genetics ; Cloning, Molecular ; Culture Media ; Disease ; E coli ; Enzymatic activity ; Enzyme Replacement Therapy - methods ; Enzyme-Linked Immunosorbent Assay ; Enzymes ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Fermentation ; Fundamental and applied biological sciences. Psychology ; Genetic Engineering ; Glucose ; Inclusion Bodies - microbiology ; Inorganic Chemistry ; Life Sciences ; Mammals ; Medical research ; Microbiology ; Mucopolysaccharidosis IV - therapy ; Original Paper ; Peptides ; Plasmids - genetics ; Plasmids - metabolism ; Proteins ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - genetics ; Studies ; Sulfates ; Tumor necrosis factor-TNF ; Yeast</subject><ispartof>Journal of industrial microbiology & biotechnology, 2010-11, Vol.37 (11), p.1193-1201</ispartof><rights>Society for Industrial Microbiology 2010</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c443t-99c0d9447f396cc3ab21c48558788a880e2b039928d7b9e412634e1c7b9303d53</citedby><cites>FETCH-LOGICAL-c443t-99c0d9447f396cc3ab21c48558788a880e2b039928d7b9e412634e1c7b9303d53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10295-010-0766-x$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10295-010-0766-x$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23360520$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20582614$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rodríguez, Alexander</creatorcontrib><creatorcontrib>Espejo, Ángela J.</creatorcontrib><creatorcontrib>Hernández, Alejandra</creatorcontrib><creatorcontrib>Velásquez, Olga L.</creatorcontrib><creatorcontrib>Lizaraso, Lina M.</creatorcontrib><creatorcontrib>Cordoba, Henry A.</creatorcontrib><creatorcontrib>Sánchez, Oscar F.</creatorcontrib><creatorcontrib>Alméciga-Díaz, Carlos J.</creatorcontrib><creatorcontrib>Barrera, Luis A.</creatorcontrib><title>Enzyme replacement therapy for Morquio A: an active recombinant N-acetylgalactosamine-6-sulfate sulfatase produced in Escherichia coli BL21</title><title>Journal of industrial microbiology & biotechnology</title><addtitle>J Ind Microbiol Biotechnol</addtitle><addtitle>J Ind Microbiol Biotechnol</addtitle><description>Mucopolysaccharidosis IVA (MPS IVA) is an autosomal recessive disorder caused by
N
-acetylgalactosamine-6-sulfate sulfatase (GALNS) deficiency. Currently no effective therapies exist for MPS IVA. In this work, production of a recombinant GALNS enzyme (rGALNS) in
Escherichia coli
BL21 strain was studied. At shake scale, the effect of glucose concentration on microorganism growth, and microorganism culture and induction times on rGALNS production were evaluated. At bench scale, the effect of aeration and agitation on microorganism growth, and culture and induction times were evaluated. The highest enzyme activity levels at shake scale were observed in 12 h culture after 2–4 h induction. At bench scale the highest enzyme activity levels were observed after 2 h induction. rGALNS amounts in inclusion bodies fraction were up to 17-fold higher than those observed in the soluble fraction. However, the highest levels of active enzyme were found in the soluble fraction. Western blot analysis showed the presence of a 50-kDa band, in both soluble and inclusion bodies fractions. These results show for the first time the feasibility and potential of production of active rGALNS in a prokaryotic system for development of enzyme replacement therapy for MPS IVA disease.</description><subject>Biochemistry</subject><subject>Bioengineering</subject><subject>Bioinformatics</subject><subject>Biological and medical sciences</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Blotting, Western</subject><subject>Chondroitinsulfatases - biosynthesis</subject><subject>Chondroitinsulfatases - genetics</subject><subject>Cloning, Molecular</subject><subject>Culture Media</subject><subject>Disease</subject><subject>E coli</subject><subject>Enzymatic activity</subject><subject>Enzyme Replacement Therapy - methods</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Enzymes</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Fermentation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic Engineering</subject><subject>Glucose</subject><subject>Inclusion Bodies - microbiology</subject><subject>Inorganic Chemistry</subject><subject>Life Sciences</subject><subject>Mammals</subject><subject>Medical research</subject><subject>Microbiology</subject><subject>Mucopolysaccharidosis IV - therapy</subject><subject>Original Paper</subject><subject>Peptides</subject><subject>Plasmids - genetics</subject><subject>Plasmids - metabolism</subject><subject>Proteins</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - genetics</subject><subject>Studies</subject><subject>Sulfates</subject><subject>Tumor necrosis factor-TNF</subject><subject>Yeast</subject><issn>1367-5435</issn><issn>1476-5535</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp1kd9qFDEUxgdRbK0-gDcSBPEqevI_410tWxVWvdHrkM1k2pSZZJvMlK7P4EP0WXwys8xqQfDqJJzf950PvqZ5TuANAVBvCwHaCgwEMCgp8e2D5phwJbEQTDysbyYVFpyJo-ZJKVcAIJSij5sjCkJTSfhx83MVf-xGj7LfDtb50ccJTZc-2-0O9SmjzylfzyH9ujt9h2xE1k3hZk-7NG5CtJX-gqtu2g0XthpMqdgxRI8lLvPQ28mjZdri0Tanbna-QyGiVXH1SnCXwSKXhoDeryl52jzq7VD8s8M8ab6fr76dfcTrrx8-nZ2useOcTbhtHXQt56pnrXSO2Q0ljmshtNLaag2eboC1LdWd2rSeEyoZ98TVDwPWCXbSvF58a6Lr2ZfJjKE4Pww2-jQXo0RLGBEAlXz5D3mV5hxrOKOJ4KCVVBUiC-RyKiX73mxzGG3eGQJmX5RZijK1KLMvytxWzYuD8bwZffdX8aeZCrw6ALY4O_TZRhfKPceYBEH3CenClbqKFz7fJ_z_9d8r_6xD</recordid><startdate>20101101</startdate><enddate>20101101</enddate><creator>Rodríguez, Alexander</creator><creator>Espejo, Ángela J.</creator><creator>Hernández, Alejandra</creator><creator>Velásquez, Olga L.</creator><creator>Lizaraso, Lina M.</creator><creator>Cordoba, Henry A.</creator><creator>Sánchez, Oscar F.</creator><creator>Alméciga-Díaz, Carlos J.</creator><creator>Barrera, Luis A.</creator><general>Springer-Verlag</general><general>Springer</general><general>Oxford University Press</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X7</scope><scope>7XB</scope><scope>87Z</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8FL</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>FYUFA</scope><scope>F~G</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>LK8</scope><scope>M0C</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20101101</creationdate><title>Enzyme replacement therapy for Morquio A: an active recombinant N-acetylgalactosamine-6-sulfate sulfatase produced in Escherichia coli BL21</title><author>Rodríguez, Alexander ; Espejo, Ángela J. ; Hernández, Alejandra ; Velásquez, Olga L. ; Lizaraso, Lina M. ; Cordoba, Henry A. ; Sánchez, Oscar F. ; Alméciga-Díaz, Carlos J. ; Barrera, Luis A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-99c0d9447f396cc3ab21c48558788a880e2b039928d7b9e412634e1c7b9303d53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Biochemistry</topic><topic>Bioengineering</topic><topic>Bioinformatics</topic><topic>Biological and medical sciences</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Blotting, Western</topic><topic>Chondroitinsulfatases - biosynthesis</topic><topic>Chondroitinsulfatases - genetics</topic><topic>Cloning, Molecular</topic><topic>Culture Media</topic><topic>Disease</topic><topic>E coli</topic><topic>Enzymatic activity</topic><topic>Enzyme Replacement Therapy - methods</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Enzymes</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Fermentation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetic Engineering</topic><topic>Glucose</topic><topic>Inclusion Bodies - microbiology</topic><topic>Inorganic Chemistry</topic><topic>Life Sciences</topic><topic>Mammals</topic><topic>Medical research</topic><topic>Microbiology</topic><topic>Mucopolysaccharidosis IV - therapy</topic><topic>Original Paper</topic><topic>Peptides</topic><topic>Plasmids - genetics</topic><topic>Plasmids - metabolism</topic><topic>Proteins</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - genetics</topic><topic>Studies</topic><topic>Sulfates</topic><topic>Tumor necrosis factor-TNF</topic><topic>Yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rodríguez, Alexander</creatorcontrib><creatorcontrib>Espejo, Ángela J.</creatorcontrib><creatorcontrib>Hernández, Alejandra</creatorcontrib><creatorcontrib>Velásquez, Olga L.</creatorcontrib><creatorcontrib>Lizaraso, Lina M.</creatorcontrib><creatorcontrib>Cordoba, Henry A.</creatorcontrib><creatorcontrib>Sánchez, Oscar F.</creatorcontrib><creatorcontrib>Alméciga-Díaz, Carlos J.</creatorcontrib><creatorcontrib>Barrera, Luis A.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Access via ABI/INFORM (ProQuest)</collection><collection>ABI/INFORM Global (PDF only)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ABI/INFORM Global (Alumni Edition)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ABI/INFORM Collection (Alumni Edition)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Business Premium Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Business Premium Collection (Alumni)</collection><collection>Health Research Premium Collection</collection><collection>ABI/INFORM Global (Corporate)</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Business Collection (Alumni Edition)</collection><collection>ProQuest Business Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ABI/INFORM Professional Advanced</collection><collection>ProQuest Biological Science Collection</collection><collection>ABI/INFORM Global</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Business</collection><collection>ProQuest One Business (Alumni)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of industrial microbiology & biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rodríguez, Alexander</au><au>Espejo, Ángela J.</au><au>Hernández, Alejandra</au><au>Velásquez, Olga L.</au><au>Lizaraso, Lina M.</au><au>Cordoba, Henry A.</au><au>Sánchez, Oscar F.</au><au>Alméciga-Díaz, Carlos J.</au><au>Barrera, Luis A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzyme replacement therapy for Morquio A: an active recombinant N-acetylgalactosamine-6-sulfate sulfatase produced in Escherichia coli BL21</atitle><jtitle>Journal of industrial microbiology & biotechnology</jtitle><stitle>J Ind Microbiol Biotechnol</stitle><addtitle>J Ind Microbiol Biotechnol</addtitle><date>2010-11-01</date><risdate>2010</risdate><volume>37</volume><issue>11</issue><spage>1193</spage><epage>1201</epage><pages>1193-1201</pages><issn>1367-5435</issn><eissn>1476-5535</eissn><abstract>Mucopolysaccharidosis IVA (MPS IVA) is an autosomal recessive disorder caused by
N
-acetylgalactosamine-6-sulfate sulfatase (GALNS) deficiency. Currently no effective therapies exist for MPS IVA. In this work, production of a recombinant GALNS enzyme (rGALNS) in
Escherichia coli
BL21 strain was studied. At shake scale, the effect of glucose concentration on microorganism growth, and microorganism culture and induction times on rGALNS production were evaluated. At bench scale, the effect of aeration and agitation on microorganism growth, and culture and induction times were evaluated. The highest enzyme activity levels at shake scale were observed in 12 h culture after 2–4 h induction. At bench scale the highest enzyme activity levels were observed after 2 h induction. rGALNS amounts in inclusion bodies fraction were up to 17-fold higher than those observed in the soluble fraction. However, the highest levels of active enzyme were found in the soluble fraction. Western blot analysis showed the presence of a 50-kDa band, in both soluble and inclusion bodies fractions. These results show for the first time the feasibility and potential of production of active rGALNS in a prokaryotic system for development of enzyme replacement therapy for MPS IVA disease.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer-Verlag</pub><pmid>20582614</pmid><doi>10.1007/s10295-010-0766-x</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Biochemistry Bioengineering Bioinformatics Biological and medical sciences Biomedical and Life Sciences Biotechnology Blotting, Western Chondroitinsulfatases - biosynthesis Chondroitinsulfatases - genetics Cloning, Molecular Culture Media Disease E coli Enzymatic activity Enzyme Replacement Therapy - methods Enzyme-Linked Immunosorbent Assay Enzymes Escherichia coli - genetics Escherichia coli - metabolism Fermentation Fundamental and applied biological sciences. Psychology Genetic Engineering Glucose Inclusion Bodies - microbiology Inorganic Chemistry Life Sciences Mammals Medical research Microbiology Mucopolysaccharidosis IV - therapy Original Paper Peptides Plasmids - genetics Plasmids - metabolism Proteins Recombinant Proteins - biosynthesis Recombinant Proteins - genetics Studies Sulfates Tumor necrosis factor-TNF Yeast |
| title | Enzyme replacement therapy for Morquio A: an active recombinant N-acetylgalactosamine-6-sulfate sulfatase produced in Escherichia coli BL21 |
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