A System for Production of Commercial Quantities of Human Lactoferrin: A Broad Spectrum Natural Antibiotic
We previously reported the production of limited quantities of biologically active recombinant human lactoferrin in the filamentous fungus, Aspergillus oryzae . In the present study, we report a modification of this production system combined with a classical strain improvement program that has enab...
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| Veröffentlicht in: | Bio/Technology 1995-05, Vol.13 (5), p.498-503 |
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| creator | Ward, Pauline P. Piddington, Christopher S. Cunningham, Grainne A. Zhou, Xiaodong Wyatt, Roger D. Conneely, Orla M. |
| description | We previously reported the production of limited quantities of biologically active recombinant human lactoferrin in the filamentous fungus,
Aspergillus oryzae
. In the present study, we report a modification of this production system combined with a classical strain improvement program that has enabled production of levels of recombinant human lactoferrin in excess of 2 g/l. The protein was expressed in
Aspergillus awamori
as a glucoamylase fusion polypeptide which was secreted into the growth medium and processed to mature human lactoferrin by an endogenous KEX-2 peptidase. The recombinant protein retains full biological activity in terms of its ability to bind iron and human enterocyte receptors. Furthermore, the recombinant protein functions as a potent broad spectrum antimicrobial protein. |
| doi_str_mv | 10.1038/nbt0595-498 |
| format | Article |
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Aspergillus oryzae
. In the present study, we report a modification of this production system combined with a classical strain improvement program that has enabled production of levels of recombinant human lactoferrin in excess of 2 g/l. The protein was expressed in
Aspergillus awamori
as a glucoamylase fusion polypeptide which was secreted into the growth medium and processed to mature human lactoferrin by an endogenous KEX-2 peptidase. The recombinant protein retains full biological activity in terms of its ability to bind iron and human enterocyte receptors. Furthermore, the recombinant protein functions as a potent broad spectrum antimicrobial protein.</description><identifier>ISSN: 0733-222X</identifier><identifier>ISSN: 1087-0156</identifier><identifier>EISSN: 1546-1696</identifier><identifier>EISSN: 2331-3684</identifier><identifier>DOI: 10.1038/nbt0595-498</identifier><identifier>PMID: 9634791</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Agriculture ; Animals ; Anti-Bacterial Agents - biosynthesis ; Anti-Bacterial Agents - pharmacology ; Antibiotics ; Aspergillus ; Aspergillus awamori ; Aspergillus oryzae ; Bioinformatics ; Biological and medical sciences ; Biomedical and Life Sciences ; Biomedical Engineering/Biotechnology ; Biomedicine ; Biotechnology ; Caco-2 Cells ; Escherichia coli - drug effects ; Female ; Fundamental and applied biological sciences. Psychology ; Glucan 1,4-alpha-Glucosidase - genetics ; Glycosylation ; Health. Pharmaceutical industry ; Humans ; Hydrogen-Ion Concentration ; Industrial applications and implications. Economical aspects ; Lactoferrin - biosynthesis ; Lactoferrin - pharmacology ; Life Sciences ; Mice ; Mice, Inbred ICR ; Microbial Sensitivity Tests ; Production of active biomolecules ; Promoter Regions, Genetic ; Protein Binding ; Recombinant Fusion Proteins - biosynthesis ; Recombinant Fusion Proteins - pharmacology</subject><ispartof>Bio/Technology, 1995-05, Vol.13 (5), p.498-503</ispartof><rights>Nature Publishing Company 1995</rights><rights>1995 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c483t-52d21892877e71b7be2830fa2de9ed640006c909e1f547704ba8b21cb6a1593d3</citedby><cites>FETCH-LOGICAL-c483t-52d21892877e71b7be2830fa2de9ed640006c909e1f547704ba8b21cb6a1593d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nbt0595-498$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nbt0595-498$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3512851$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9634791$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ward, Pauline P.</creatorcontrib><creatorcontrib>Piddington, Christopher S.</creatorcontrib><creatorcontrib>Cunningham, Grainne A.</creatorcontrib><creatorcontrib>Zhou, Xiaodong</creatorcontrib><creatorcontrib>Wyatt, Roger D.</creatorcontrib><creatorcontrib>Conneely, Orla M.</creatorcontrib><title>A System for Production of Commercial Quantities of Human Lactoferrin: A Broad Spectrum Natural Antibiotic</title><title>Bio/Technology</title><addtitle>Nat Biotechnol</addtitle><addtitle>Biotechnology (N Y)</addtitle><description>We previously reported the production of limited quantities of biologically active recombinant human lactoferrin in the filamentous fungus,
Aspergillus oryzae
. In the present study, we report a modification of this production system combined with a classical strain improvement program that has enabled production of levels of recombinant human lactoferrin in excess of 2 g/l. The protein was expressed in
Aspergillus awamori
as a glucoamylase fusion polypeptide which was secreted into the growth medium and processed to mature human lactoferrin by an endogenous KEX-2 peptidase. The recombinant protein retains full biological activity in terms of its ability to bind iron and human enterocyte receptors. Furthermore, the recombinant protein functions as a potent broad spectrum antimicrobial protein.</description><subject>Agriculture</subject><subject>Animals</subject><subject>Anti-Bacterial Agents - biosynthesis</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Antibiotics</subject><subject>Aspergillus</subject><subject>Aspergillus awamori</subject><subject>Aspergillus oryzae</subject><subject>Bioinformatics</subject><subject>Biological and medical sciences</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedical Engineering/Biotechnology</subject><subject>Biomedicine</subject><subject>Biotechnology</subject><subject>Caco-2 Cells</subject><subject>Escherichia coli - drug effects</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glucan 1,4-alpha-Glucosidase - genetics</subject><subject>Glycosylation</subject><subject>Health. Pharmaceutical industry</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Industrial applications and implications. Economical aspects</subject><subject>Lactoferrin - biosynthesis</subject><subject>Lactoferrin - pharmacology</subject><subject>Life Sciences</subject><subject>Mice</subject><subject>Mice, Inbred ICR</subject><subject>Microbial Sensitivity Tests</subject><subject>Production of active biomolecules</subject><subject>Promoter Regions, Genetic</subject><subject>Protein Binding</subject><subject>Recombinant Fusion Proteins - biosynthesis</subject><subject>Recombinant Fusion Proteins - pharmacology</subject><issn>0733-222X</issn><issn>1087-0156</issn><issn>1546-1696</issn><issn>2331-3684</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkbtrHDEYxIVJsM-OK9cGFcFNsoneWrk7H0kcOPLACaRbtFqt0bErnfUo_N9Hxy2uAqm-Yn4zH8wAcIXRB4xo-9H3GXHFG6baE7DCnIkGCyVegRWSlDaEkD9n4DylHUJMCsJOwakSlEmFV2C3hg_PKdsZjiHCHzEMxWQXPAwj3IR5ttE4PcGfRfvssrPpINyXWXu41SaH0cbo_C1cw7sY9AAf9tbkWGb4TecSq3Ndfb0L2Zk34PWop2Qvl3sBfn_-9Gtz32y_f_m6WW8bw1qaG04GgltFWimtxL3sLWkpGjUZrLKDYAghYRRSFo-cSYlYr9ueYNMLjbmiA70AN8fcfQxPxabczS4ZO03a21BSJ6XiQjDxXxALWXsSuILvjqCJIaVox24f3azjc4dRd5igWybo6gSVvl5iSz_b4YVdOq_620XXyehpjNobl14wyjFp-QF7f8RSVfyjjd0ulOhrc__8-heg5Jyt</recordid><startdate>19950501</startdate><enddate>19950501</enddate><creator>Ward, Pauline P.</creator><creator>Piddington, Christopher S.</creator><creator>Cunningham, Grainne A.</creator><creator>Zhou, Xiaodong</creator><creator>Wyatt, Roger D.</creator><creator>Conneely, Orla M.</creator><general>Nature Publishing Group US</general><general>Nature Publications</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>7QO</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19950501</creationdate><title>A System for Production of Commercial Quantities of Human Lactoferrin: A Broad Spectrum Natural Antibiotic</title><author>Ward, Pauline P. ; Piddington, Christopher S. ; Cunningham, Grainne A. ; Zhou, Xiaodong ; Wyatt, Roger D. ; Conneely, Orla M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c483t-52d21892877e71b7be2830fa2de9ed640006c909e1f547704ba8b21cb6a1593d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Agriculture</topic><topic>Animals</topic><topic>Anti-Bacterial Agents - biosynthesis</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>Antibiotics</topic><topic>Aspergillus</topic><topic>Aspergillus awamori</topic><topic>Aspergillus oryzae</topic><topic>Bioinformatics</topic><topic>Biological and medical sciences</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedical Engineering/Biotechnology</topic><topic>Biomedicine</topic><topic>Biotechnology</topic><topic>Caco-2 Cells</topic><topic>Escherichia coli - drug effects</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glucan 1,4-alpha-Glucosidase - genetics</topic><topic>Glycosylation</topic><topic>Health. Pharmaceutical industry</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Industrial applications and implications. Economical aspects</topic><topic>Lactoferrin - biosynthesis</topic><topic>Lactoferrin - pharmacology</topic><topic>Life Sciences</topic><topic>Mice</topic><topic>Mice, Inbred ICR</topic><topic>Microbial Sensitivity Tests</topic><topic>Production of active biomolecules</topic><topic>Promoter Regions, Genetic</topic><topic>Protein Binding</topic><topic>Recombinant Fusion Proteins - biosynthesis</topic><topic>Recombinant Fusion Proteins - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ward, Pauline P.</creatorcontrib><creatorcontrib>Piddington, Christopher S.</creatorcontrib><creatorcontrib>Cunningham, Grainne A.</creatorcontrib><creatorcontrib>Zhou, Xiaodong</creatorcontrib><creatorcontrib>Wyatt, Roger D.</creatorcontrib><creatorcontrib>Conneely, Orla M.</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>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Bio/Technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ward, Pauline P.</au><au>Piddington, Christopher S.</au><au>Cunningham, Grainne A.</au><au>Zhou, Xiaodong</au><au>Wyatt, Roger D.</au><au>Conneely, Orla M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A System for Production of Commercial Quantities of Human Lactoferrin: A Broad Spectrum Natural Antibiotic</atitle><jtitle>Bio/Technology</jtitle><stitle>Nat Biotechnol</stitle><addtitle>Biotechnology (N Y)</addtitle><date>1995-05-01</date><risdate>1995</risdate><volume>13</volume><issue>5</issue><spage>498</spage><epage>503</epage><pages>498-503</pages><issn>0733-222X</issn><issn>1087-0156</issn><eissn>1546-1696</eissn><eissn>2331-3684</eissn><abstract>We previously reported the production of limited quantities of biologically active recombinant human lactoferrin in the filamentous fungus,
Aspergillus oryzae
. In the present study, we report a modification of this production system combined with a classical strain improvement program that has enabled production of levels of recombinant human lactoferrin in excess of 2 g/l. The protein was expressed in
Aspergillus awamori
as a glucoamylase fusion polypeptide which was secreted into the growth medium and processed to mature human lactoferrin by an endogenous KEX-2 peptidase. The recombinant protein retains full biological activity in terms of its ability to bind iron and human enterocyte receptors. Furthermore, the recombinant protein functions as a potent broad spectrum antimicrobial protein.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>9634791</pmid><doi>10.1038/nbt0595-498</doi><tpages>6</tpages></addata></record> |
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| ispartof | Bio/Technology, 1995-05, Vol.13 (5), p.498-503 |
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| language | eng |
| recordid | cdi_proquest_miscellaneous_77956646 |
| source | MEDLINE; Springer Nature - Complete Springer Journals; Nature Journals Online |
| subjects | Agriculture Animals Anti-Bacterial Agents - biosynthesis Anti-Bacterial Agents - pharmacology Antibiotics Aspergillus Aspergillus awamori Aspergillus oryzae Bioinformatics Biological and medical sciences Biomedical and Life Sciences Biomedical Engineering/Biotechnology Biomedicine Biotechnology Caco-2 Cells Escherichia coli - drug effects Female Fundamental and applied biological sciences. Psychology Glucan 1,4-alpha-Glucosidase - genetics Glycosylation Health. Pharmaceutical industry Humans Hydrogen-Ion Concentration Industrial applications and implications. Economical aspects Lactoferrin - biosynthesis Lactoferrin - pharmacology Life Sciences Mice Mice, Inbred ICR Microbial Sensitivity Tests Production of active biomolecules Promoter Regions, Genetic Protein Binding Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - pharmacology |
| title | A System for Production of Commercial Quantities of Human Lactoferrin: A Broad Spectrum Natural Antibiotic |
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