Defining the mechanistic binding of viral particles to a multi‐modal anion exchange resin
Abstract
A multi‐tiered approach to determine the binding mechanism of viral clearance utilizing a multi‐modal anion exchange resin was applied to a panel of four viral species that are typically used in validating viral clearance studies (i.e., X‐MuLV, MVM, REO3, and PrV). First, virus spiked buffer‐only experiments were conducted to evaluate the virus's affinity for single mode and multi‐modal chromatography resins under different buffer conditions in a chromatography column setting. From these results we hypothesize that the mechanisms of binding of the viruses involve binding to both the hydrophobic and anionic functional groups. This mechanistic view agreed with the general surface characteristics of the different virus species in terms of isoelectric point and relative hydrophobicity values. This hypothesized mechanistic binding was then tested with commercially relevant, in‐process materials, in which competitive binding occurred between the load components (e.g., viruses, target product, and impurities) and the resin. © 2018 American Institute of Chemical Engineers Biotechnol. Prog. , 34:1019–1026, 2018
- Authors:
-
[1];
- Food and Drug Administration DBRRII, Office of Biotechnology Products, Office of Pharmaceutical Quality, Center for Drug Evaluation and Research Silver Spring MD 20993
- WuXI AppTec, Inc. Philadelphia PA
- BioProcess Development, Biologics and Vaccines Merck &, Co., Inc. Kenilworth NJ
- Publication Date:
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1459222
- Resource Type:
- Publisher's Accepted Manuscript
- Journal Name:
- Biotechnology Progress
- Additional Journal Information:
- Journal Name: Biotechnology Progress Journal Volume: 34 Journal Issue: 4; Journal ID: ISSN 8756-7938
- Publisher:
- Wiley Blackwell (John Wiley & Sons)
- Country of Publication:
- United States
- Language:
- English
Citation Formats
Brown, Matthew R., Burnham, Michael S., Lute, Scott C., Johnson, Sarah A., Walsh, Alison A., Brorson, Kurt A., and Roush, David J. Defining the mechanistic binding of viral particles to a multi‐modal anion exchange resin. United States: N. p., 2018.
Web. doi:10.1002/btpr.2648.
Brown, Matthew R., Burnham, Michael S., Lute, Scott C., Johnson, Sarah A., Walsh, Alison A., Brorson, Kurt A., & Roush, David J. Defining the mechanistic binding of viral particles to a multi‐modal anion exchange resin. United States. https://doi.org/10.1002/btpr.2648
Brown, Matthew R., Burnham, Michael S., Lute, Scott C., Johnson, Sarah A., Walsh, Alison A., Brorson, Kurt A., and Roush, David J. Thu .
"Defining the mechanistic binding of viral particles to a multi‐modal anion exchange resin". United States. https://doi.org/10.1002/btpr.2648.
@article{osti_1459222,
title = {Defining the mechanistic binding of viral particles to a multi‐modal anion exchange resin},
author = {Brown, Matthew R. and Burnham, Michael S. and Lute, Scott C. and Johnson, Sarah A. and Walsh, Alison A. and Brorson, Kurt A. and Roush, David J.},
abstractNote = {A multi‐tiered approach to determine the binding mechanism of viral clearance utilizing a multi‐modal anion exchange resin was applied to a panel of four viral species that are typically used in validating viral clearance studies (i.e., X‐MuLV, MVM, REO3, and PrV). First, virus spiked buffer‐only experiments were conducted to evaluate the virus's affinity for single mode and multi‐modal chromatography resins under different buffer conditions in a chromatography column setting. From these results we hypothesize that the mechanisms of binding of the viruses involve binding to both the hydrophobic and anionic functional groups. This mechanistic view agreed with the general surface characteristics of the different virus species in terms of isoelectric point and relative hydrophobicity values. This hypothesized mechanistic binding was then tested with commercially relevant, in‐process materials, in which competitive binding occurred between the load components (e.g., viruses, target product, and impurities) and the resin. © 2018 American Institute of Chemical Engineers Biotechnol. Prog. , 34:1019–1026, 2018},
doi = {10.1002/btpr.2648},
journal = {Biotechnology Progress},
number = 4,
volume = 34,
place = {United States},
year = {Thu Jul 05 00:00:00 EDT 2018},
month = {Thu Jul 05 00:00:00 EDT 2018}
}
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