Cation exchange chromatography provides effective retrovirus clearance for antibody purification processes
One measure taken to ensure safety of biotherapeutics produced in mammalian cells is to demonstrate the clearance of potential viral contaminants by downstream purification processes. This paper provides evidence that cation exchange chromatography (CEX), a widely used polishing step for monoclonal...
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| Veröffentlicht in: | Biotechnology and bioengineering 2012-01, Vol.109 (1), p.157-165 |
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| creator | Connell-Crowley, Lisa Nguyen, Thao Bach, Julia Chinniah, Shivanthi Bashiri, Houman Gillespie, Ron Moscariello, John Hinckley, Peter Dehghani, Houman Vunnum, Suresh Vedantham, Ganesh |
| description | One measure taken to ensure safety of biotherapeutics produced in mammalian cells is to demonstrate the clearance of potential viral contaminants by downstream purification processes. This paper provides evidence that cation exchange chromatography (CEX), a widely used polishing step for monoclonal antibody (mAb) production, can effectively and reproducibly remove xMuLV, a retrovirus used as a model of non‐infectious retrovirus‐like particles found in Chinese hamster ovary cells. The dominant mechanism for xMuLV clearance by the strong cation exchanger, Fractogel SO 3−, is by retention of the virus via adsorption instead of inactivation. Experimental data defining the design space for effective xMuLV removal by Fractogel SO 3− with respect to operational pH, elution ionic strength, loading, and load/equilibration buffer ionic strength are provided. Additionally, xMuLV is able to bind to other CEX resins, such as Fractogel COO− and SP Sepharose Fast Flow, suggesting that this phenomenon is not restricted to one type of CEX resin. Taken together, the data indicate that CEX chromatography can be a robust and reproducible removal step for the model retrovirus xMuLV. Biotechnol. Bioeng. 2012;109: 157–165. © 2011 Wiley Periodicals, Inc. |
| doi_str_mv | 10.1002/bit.23300 |
| format | Article |
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This paper provides evidence that cation exchange chromatography (CEX), a widely used polishing step for monoclonal antibody (mAb) production, can effectively and reproducibly remove xMuLV, a retrovirus used as a model of non‐infectious retrovirus‐like particles found in Chinese hamster ovary cells. The dominant mechanism for xMuLV clearance by the strong cation exchanger, Fractogel SO 3−, is by retention of the virus via adsorption instead of inactivation. Experimental data defining the design space for effective xMuLV removal by Fractogel SO 3− with respect to operational pH, elution ionic strength, loading, and load/equilibration buffer ionic strength are provided. Additionally, xMuLV is able to bind to other CEX resins, such as Fractogel COO− and SP Sepharose Fast Flow, suggesting that this phenomenon is not restricted to one type of CEX resin. Taken together, the data indicate that CEX chromatography can be a robust and reproducible removal step for the model retrovirus xMuLV. Biotechnol. Bioeng. 2012;109: 157–165. © 2011 Wiley Periodicals, Inc.</description><identifier>ISSN: 0006-3592</identifier><identifier>ISSN: 1097-0290</identifier><identifier>EISSN: 1097-0290</identifier><identifier>DOI: 10.1002/bit.23300</identifier><identifier>PMID: 21837666</identifier><identifier>CODEN: BIBIAU</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Adsorption ; Animals ; Antibodies, Monoclonal - isolation & purification ; Bioengineering ; Biotechnology - methods ; Buffers ; Cation exchanging ; Cells ; CEX ; CHO Cells ; Chromatography ; Chromatography, Ion Exchange - methods ; Clearances ; Cricetinae ; Cricetulus ; Ion exchange ; Leukemia Virus, Murine - isolation & purification ; Monoclonal antibodies ; monoclonal antibody ; Osmolar Concentration ; Polymers ; Purification ; Resins ; Rodents ; Strength ; viral clearance ; Virus Attachment ; Viruses ; xMuLV</subject><ispartof>Biotechnology and bioengineering, 2012-01, Vol.109 (1), p.157-165</ispartof><rights>Copyright © 2011 Wiley Periodicals, Inc.</rights><rights>Copyright John Wiley and Sons, Limited Jan 2012</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4920-b895622247ae26f34afa8059e6b129d9ecc314451dd1dd34c6b5f498de98fec53</citedby><cites>FETCH-LOGICAL-c4920-b895622247ae26f34afa8059e6b129d9ecc314451dd1dd34c6b5f498de98fec53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbit.23300$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbit.23300$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21837666$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Connell-Crowley, Lisa</creatorcontrib><creatorcontrib>Nguyen, Thao</creatorcontrib><creatorcontrib>Bach, Julia</creatorcontrib><creatorcontrib>Chinniah, Shivanthi</creatorcontrib><creatorcontrib>Bashiri, Houman</creatorcontrib><creatorcontrib>Gillespie, Ron</creatorcontrib><creatorcontrib>Moscariello, John</creatorcontrib><creatorcontrib>Hinckley, Peter</creatorcontrib><creatorcontrib>Dehghani, Houman</creatorcontrib><creatorcontrib>Vunnum, Suresh</creatorcontrib><creatorcontrib>Vedantham, Ganesh</creatorcontrib><title>Cation exchange chromatography provides effective retrovirus clearance for antibody purification processes</title><title>Biotechnology and bioengineering</title><addtitle>Biotechnol. Bioeng</addtitle><description>One measure taken to ensure safety of biotherapeutics produced in mammalian cells is to demonstrate the clearance of potential viral contaminants by downstream purification processes. This paper provides evidence that cation exchange chromatography (CEX), a widely used polishing step for monoclonal antibody (mAb) production, can effectively and reproducibly remove xMuLV, a retrovirus used as a model of non‐infectious retrovirus‐like particles found in Chinese hamster ovary cells. The dominant mechanism for xMuLV clearance by the strong cation exchanger, Fractogel SO 3−, is by retention of the virus via adsorption instead of inactivation. Experimental data defining the design space for effective xMuLV removal by Fractogel SO 3− with respect to operational pH, elution ionic strength, loading, and load/equilibration buffer ionic strength are provided. Additionally, xMuLV is able to bind to other CEX resins, such as Fractogel COO− and SP Sepharose Fast Flow, suggesting that this phenomenon is not restricted to one type of CEX resin. Taken together, the data indicate that CEX chromatography can be a robust and reproducible removal step for the model retrovirus xMuLV. Biotechnol. Bioeng. 2012;109: 157–165. © 2011 Wiley Periodicals, Inc.</description><subject>Adsorption</subject><subject>Animals</subject><subject>Antibodies, Monoclonal - isolation & purification</subject><subject>Bioengineering</subject><subject>Biotechnology - methods</subject><subject>Buffers</subject><subject>Cation exchanging</subject><subject>Cells</subject><subject>CEX</subject><subject>CHO Cells</subject><subject>Chromatography</subject><subject>Chromatography, Ion Exchange - methods</subject><subject>Clearances</subject><subject>Cricetinae</subject><subject>Cricetulus</subject><subject>Ion exchange</subject><subject>Leukemia Virus, Murine - isolation & purification</subject><subject>Monoclonal antibodies</subject><subject>monoclonal antibody</subject><subject>Osmolar Concentration</subject><subject>Polymers</subject><subject>Purification</subject><subject>Resins</subject><subject>Rodents</subject><subject>Strength</subject><subject>viral clearance</subject><subject>Virus Attachment</subject><subject>Viruses</subject><subject>xMuLV</subject><issn>0006-3592</issn><issn>1097-0290</issn><issn>1097-0290</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9v0zAYhy3ExMrgwBdAERfgkM3_HR-hgm5aNS5DO1qO83p1SZPOTsb67XGXbQekgWTLsvW8z2v7h9A7go8JxvSkDsMxZQzjF2hGsFYlphq_RDOMsSyZ0PQQvU5pnbeqkvIVOqSkYkpKOUPruR1C3xVw51a2u4bCrWK_sUN_He12tSu2sb8NDaQCvAc3hFsoIgz7wzimwrVgo-0cFL6Phe2GUPdNLhpj8MFN5mxwkBKkN-jA2zbB24f1CP38_u1yfloufyzO5l-WpeOa4rKutJCUUq4sUOkZt95WWGiQNaG60eAcI5wL0jR5MO5kLTzXVQO6ylcU7Ah9nLy5880IaTCbkBy0re2gH5PRWEjFBKsy-emfJJGKcEaoIP9HMVFaVoLzjH74C133Y-zyk_etFcHsHvo8QS72KUXwZhvDxsZdNpl9qCaHau5Dzez7B-FYb6B5Ih9TzMDJBPwOLeyeN5mvZ5ePynKqCGmAu6cKG3-Z_DdKmKuLRZ4XanF-JcyS_QHeort7</recordid><startdate>201201</startdate><enddate>201201</enddate><creator>Connell-Crowley, Lisa</creator><creator>Nguyen, Thao</creator><creator>Bach, Julia</creator><creator>Chinniah, Shivanthi</creator><creator>Bashiri, Houman</creator><creator>Gillespie, Ron</creator><creator>Moscariello, John</creator><creator>Hinckley, Peter</creator><creator>Dehghani, Houman</creator><creator>Vunnum, Suresh</creator><creator>Vedantham, Ganesh</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</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>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>201201</creationdate><title>Cation exchange chromatography provides effective retrovirus clearance for antibody purification processes</title><author>Connell-Crowley, Lisa ; 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Bioeng</addtitle><date>2012-01</date><risdate>2012</risdate><volume>109</volume><issue>1</issue><spage>157</spage><epage>165</epage><pages>157-165</pages><issn>0006-3592</issn><issn>1097-0290</issn><eissn>1097-0290</eissn><coden>BIBIAU</coden><abstract>One measure taken to ensure safety of biotherapeutics produced in mammalian cells is to demonstrate the clearance of potential viral contaminants by downstream purification processes. This paper provides evidence that cation exchange chromatography (CEX), a widely used polishing step for monoclonal antibody (mAb) production, can effectively and reproducibly remove xMuLV, a retrovirus used as a model of non‐infectious retrovirus‐like particles found in Chinese hamster ovary cells. The dominant mechanism for xMuLV clearance by the strong cation exchanger, Fractogel SO 3−, is by retention of the virus via adsorption instead of inactivation. Experimental data defining the design space for effective xMuLV removal by Fractogel SO 3− with respect to operational pH, elution ionic strength, loading, and load/equilibration buffer ionic strength are provided. Additionally, xMuLV is able to bind to other CEX resins, such as Fractogel COO− and SP Sepharose Fast Flow, suggesting that this phenomenon is not restricted to one type of CEX resin. Taken together, the data indicate that CEX chromatography can be a robust and reproducible removal step for the model retrovirus xMuLV. Biotechnol. Bioeng. 2012;109: 157–165. © 2011 Wiley Periodicals, Inc.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>21837666</pmid><doi>10.1002/bit.23300</doi><tpages>9</tpages></addata></record> |
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| subjects | Adsorption Animals Antibodies, Monoclonal - isolation & purification Bioengineering Biotechnology - methods Buffers Cation exchanging Cells CEX CHO Cells Chromatography Chromatography, Ion Exchange - methods Clearances Cricetinae Cricetulus Ion exchange Leukemia Virus, Murine - isolation & purification Monoclonal antibodies monoclonal antibody Osmolar Concentration Polymers Purification Resins Rodents Strength viral clearance Virus Attachment Viruses xMuLV |
| title | Cation exchange chromatography provides effective retrovirus clearance for antibody purification processes |
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