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Purification of cell culture‐derived human influenza A virus by size‐exclusion and anion‐exchange chromatography

Identifieur interne : 000F02 ( Main/Exploration ); précédent : 000F01; suivant : 000F03

Purification of cell culture‐derived human influenza A virus by size‐exclusion and anion‐exchange chromatography

Auteurs : Bernd Kalbfuss [Allemagne] ; Michael Wolff ; Robert Morenweiser [Allemagne] ; Udo Reichl [Allemagne]

Source :

Biotechnology and Bioengineering [ 0006-3592 ] ; 2007-04-01.

RBID : ISTEX:6361D18733E8E1F2625744DEC10599CEF8AE7A99

English descriptors

Teeft :
- Accessible pore volume fraction, Additional steps, Adsorption, Appropriate phosphate buffer, April, Assay, Batch, Batch adsorption experiment, Batch adsorption experiments, Best separation, Bimodal distributions, Bioengineering, Bioprocess engineering, Biotechnology, Cell culture, Cell culture medium, Cell culture supernatants, Chicken eggs, Chromatography, Chromatography media, Column chromatography, Column load, Column volumes, Contact time, Continuous cell lines, Density gradient centrifugation, Desorbed virus, Different concentrations, Different selectivity, Dynamic light, Eluate, Eluate fractions, Elution, Elution peak, Elution volume, Equine virus, European pharmacopeia, Exclusion limit, Feed material, Feed volume, Fractionation limit, Further optimization, Good agreement, Hcdna, Hcdna concentration, Hcdna concentrations, Healthcare, Healthcare sweden, Hemagglutinin, Hemagglutinin protein, Heyward, High load, High resolution, Hitrap screening columns, Host cell, Host cell protein, Human vaccines, Human virus, Hydrochloric acid, Independent batches, Injection volume, Ionic strength, Kalbfuss, Linear gradient, Loading study, Mammalian cells, Mass concentration, Material balances, Mdck cells, Microtiter plates, Nacl, Narrow range, Nayak, Negative charge, Next step, Other impurities, Overall product, Overall reduction, Overall yields, Owthrough, Particle volume distributions, Phosphate buffer, Pore, Pore diffusivity, Pore glass, Pore size, Product fraction, Product fractions, Product yields, Protein, Protein assay, Protein purity, Residual amount, Room temperature, Salt concentration, Same batch, Sample tube, Screening columns, Separation behavior, Sepharose, Sepharose sepharose, Similar amounts, Size distribution, Sizeexclusion chromatography, Small protein, Small solutes, Sodium chloride, Sodium hydroxide, Split peak elution, Standard deviations, Stationary phase, Step gradient, Supernatant, Tandem mass spectrometry, Total protein, Total protein concentration, Total protein mass, Total recoveries, Total recovery, Tricorn columns, Tryptic digestion, Turkey coronavirus, Unit operation, Unit operations, Vaccine, Vesicular stomatitis virus, Viral, Viral preparations, Viral protein, Virion, Virus, Virus biotechnology, Virus eluate fractions, Virus matrix protein, Virus peak, Virus population, Void fraction, Void volume, Waste fraction, Wiley interscience, Wiley periodicals.

Abstract

A process comprising of size‐exclusion chromatography (SEC) and anion‐exchange chromatography (AEC) was investigated for downstream processing of cell culture‐derived influenza A virus. Human influenza virus A/PR/8/34 (H1N1) was propagated in serum‐free medium using MDCK cells as a host. Concentrates of the virus were prepared from clarified and inactivated cell culture supernatants by cross‐flow ultrafiltration as described before. SEC on Sepharose 4 FF resulted in average product yields of 85% based on hemagglutination (HA) activity. Productivity was maximized to 0.15 column volumes (cv) of concentrate per hour yielding a reduction in total protein and host cell DNA (hcDNA) to 35 and 34%, respectively. AEC on Sepharose Q XL was used to separate hcDNA from virus at a salt concentration of 0.65 M sodium chloride. Product yields >80% were achieved for loads >160 kHAU/mL of resin. The reduction in hcDNA was 67‐fold. Split peak elution and bimodal particle volume distributions suggested aggregation of virions. Co‐elution with hcDNA and constant amounts of hcDNA per dose indiciated association of virions to hcDNA. An overall product yield of 52% was achieved. Total protein was reduced more than 19‐fold; hcDNA more than 500‐fold by the process. Estimation of the dose volume from HA activity predicted a protein content at the limit for human vaccines. Reduction of hcDNA was found insufficient (about 500 ng per dose) requiring further optimization of AEC or additional purification steps. All operations were selected to be scalable and independent of the virus strain rendering the process suitable for vaccine production. Biotechnol. Bioeng. 2007;96:932–944. © 2006 Wiley Periodicals, Inc.

Url:

https://api.istex.fr/ark:/67375/WNG-18T4B2K4-5/fulltext.pdf

DOI: 10.1002/bit.21109

Affiliations:

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Le document en format XML

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<term>Additional steps</term>
<term>Adsorption</term>
<term>Appropriate phosphate buffer</term>
<term>April</term>
<term>Assay</term>
<term>Batch</term>
<term>Batch adsorption experiment</term>
<term>Batch adsorption experiments</term>
<term>Best separation</term>
<term>Bimodal distributions</term>
<term>Bioengineering</term>
<term>Bioprocess engineering</term>
<term>Biotechnology</term>
<term>Cell culture</term>
<term>Cell culture medium</term>
<term>Cell culture supernatants</term>
<term>Chicken eggs</term>
<term>Chromatography</term>
<term>Chromatography media</term>
<term>Column chromatography</term>
<term>Column load</term>
<term>Column volumes</term>
<term>Contact time</term>
<term>Continuous cell lines</term>
<term>Density gradient centrifugation</term>
<term>Desorbed virus</term>
<term>Different concentrations</term>
<term>Different selectivity</term>
<term>Dynamic light</term>
<term>Eluate</term>
<term>Eluate fractions</term>
<term>Elution</term>
<term>Elution peak</term>
<term>Elution volume</term>
<term>Equine virus</term>
<term>European pharmacopeia</term>
<term>Exclusion limit</term>
<term>Feed material</term>
<term>Feed volume</term>
<term>Fractionation limit</term>
<term>Further optimization</term>
<term>Good agreement</term>
<term>Hcdna</term>
<term>Hcdna concentration</term>
<term>Hcdna concentrations</term>
<term>Healthcare</term>
<term>Healthcare sweden</term>
<term>Hemagglutinin</term>
<term>Hemagglutinin protein</term>
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<term>High load</term>
<term>High resolution</term>
<term>Hitrap screening columns</term>
<term>Host cell</term>
<term>Host cell protein</term>
<term>Human vaccines</term>
<term>Human virus</term>
<term>Hydrochloric acid</term>
<term>Independent batches</term>
<term>Injection volume</term>
<term>Ionic strength</term>
<term>Kalbfuss</term>
<term>Linear gradient</term>
<term>Loading study</term>
<term>Mammalian cells</term>
<term>Mass concentration</term>
<term>Material balances</term>
<term>Mdck cells</term>
<term>Microtiter plates</term>
<term>Nacl</term>
<term>Narrow range</term>
<term>Nayak</term>
<term>Negative charge</term>
<term>Next step</term>
<term>Other impurities</term>
<term>Overall product</term>
<term>Overall reduction</term>
<term>Overall yields</term>
<term>Owthrough</term>
<term>Particle volume distributions</term>
<term>Phosphate buffer</term>
<term>Pore</term>
<term>Pore diffusivity</term>
<term>Pore glass</term>
<term>Pore size</term>
<term>Product fraction</term>
<term>Product fractions</term>
<term>Product yields</term>
<term>Protein</term>
<term>Protein assay</term>
<term>Protein purity</term>
<term>Residual amount</term>
<term>Room temperature</term>
<term>Salt concentration</term>
<term>Same batch</term>
<term>Sample tube</term>
<term>Screening columns</term>
<term>Separation behavior</term>
<term>Sepharose</term>
<term>Sepharose sepharose</term>
<term>Similar amounts</term>
<term>Size distribution</term>
<term>Sizeexclusion chromatography</term>
<term>Small protein</term>
<term>Small solutes</term>
<term>Sodium chloride</term>
<term>Sodium hydroxide</term>
<term>Split peak elution</term>
<term>Standard deviations</term>
<term>Stationary phase</term>
<term>Step gradient</term>
<term>Supernatant</term>
<term>Tandem mass spectrometry</term>
<term>Total protein</term>
<term>Total protein concentration</term>
<term>Total protein mass</term>
<term>Total recoveries</term>
<term>Total recovery</term>
<term>Tricorn columns</term>
<term>Tryptic digestion</term>
<term>Turkey coronavirus</term>
<term>Unit operation</term>
<term>Unit operations</term>
<term>Vaccine</term>
<term>Vesicular stomatitis virus</term>
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<term>Viral preparations</term>
<term>Viral protein</term>
<term>Virion</term>
<term>Virus</term>
<term>Virus biotechnology</term>
<term>Virus eluate fractions</term>
<term>Virus matrix protein</term>
<term>Virus peak</term>
<term>Virus population</term>
<term>Void fraction</term>
<term>Void volume</term>
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<term>Wiley interscience</term>
<term>Wiley periodicals</term>
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<front><div type="abstract" xml:lang="en">A process comprising of size‐exclusion chromatography (SEC) and anion‐exchange chromatography (AEC) was investigated for downstream processing of cell culture‐derived influenza A virus. Human influenza virus A/PR/8/34 (H1N1) was propagated in serum‐free medium using MDCK cells as a host. Concentrates of the virus were prepared from clarified and inactivated cell culture supernatants by cross‐flow ultrafiltration as described before. SEC on Sepharose 4 FF resulted in average product yields of 85% based on hemagglutination (HA) activity. Productivity was maximized to 0.15 column volumes (cv) of concentrate per hour yielding a reduction in total protein and host cell DNA (hcDNA) to 35 and 34%, respectively. AEC on Sepharose Q XL was used to separate hcDNA from virus at a salt concentration of 0.65 M sodium chloride. Product yields >80% were achieved for loads >160 kHAU/mL of resin. The reduction in hcDNA was 67‐fold. Split peak elution and bimodal particle volume distributions suggested aggregation of virions. Co‐elution with hcDNA and constant amounts of hcDNA per dose indiciated association of virions to hcDNA. An overall product yield of 52% was achieved. Total protein was reduced more than 19‐fold; hcDNA more than 500‐fold by the process. Estimation of the dose volume from HA activity predicted a protein content at the limit for human vaccines. Reduction of hcDNA was found insufficient (about 500 ng per dose) requiring further optimization of AEC or additional purification steps. All operations were selected to be scalable and independent of the virus strain rendering the process suitable for vaccine production. Biotechnol. Bioeng. 2007;96:932–944. © 2006 Wiley Periodicals, Inc.</div>
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Purification of cell culture‐derived human influenza A virus by size‐exclusion and anion‐exchange chromatography

Purification of cell culture‐derived human influenza A virus by size‐exclusion and anion‐exchange chromatography

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English descriptors

Abstract

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