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Reagents for Assessing Seroreactivity Against Porcine Endogenous Retrovirus: Summary from Public Meeting and Workshop

by Carolyn A. Wilson, PhD, Eda T. Bloom, PhD, Louisa E. Chapman, MD, and Clive Patience, PhD
Volume 2, Issue 2 (March/April 2003)

Xenotransplantation has been defined by the US Public Health Service (PHS) as any procedure that involves the transplantation, implantation, or infusion into a human recipient of either (a) live cells, tissues, or organs from a nonhuman animal source, or (b) human body fluids, cells, tissues, or organs that have had ex vivo contact with live, nonhuman animal cells, tissues, or organs (PHS Guideline on Infectious Disease Issues in Xenotransplantation). In the US, several xenotransplantation clinical trials are in progress under US Food and Drug Administration (FDA) oversight. The PHS and the FDA have issued guidelines and guidance documents to address the potential for cross-species infection posed by the use of xenotransplantation products in humans. To minimize the infectious disease risk, these documents provide recommendations on how to screen and maintain source herds, individual source animals, and when possible, xenotransplantation products themselves. However, while precautions can be put in place to remove exogenous infectious agents, the endogenous retroviruses that a source species may carry cannot be removed...

Citation:
Wilson CA, Bloom ET, Chapman LE, Patience C. Reagents for Assessing Seroreactivity Against Porcine Endogenous Retrovirus: Summary from Public Meeting and Workshop. BioProcess J, 2003; 2(2): 27-30. http://dx.doi.org/10.12665/J22.Wilson.

 
Rapid Development of CHO Cell Lines for High-Level Production of Recombinant Antibodies

by Daniel S. Allison, PhD, Michael Brandenstein, Lynn Davis, Jennifer Running Deer, Nilesh Shah, PhD, and Kristin Ziegler
Volume 2, Issue 2 (March/April 2003)

Organizations developing biopharmaceuticals are often faced with the challenge of developing, as rapidly as possible, a production system for a recombinant protein or antibody intended for use in clinical trials. For expression of antibodies and other proteins with complex post-translational modifications, Chinese hamster ovary (CHO) cells are often the host of choice. However, isolation of CHO cell lines producing even moderate levels of a protein of interest is usually a lengthy process due to the need for at least one and usually several gene amplification steps. Gene amplification, which is usually accomplished through the dihydrofolate reductase (dhfr)/methotrexate system, is a requirement for most CHO expression vectors because the absolute expression level from each copy of an integrated expression plasmid is generally very low...

Citation:
Allison DS, Brandenstein M, Davis L, Running Deer J, Shah N, Ziegler K. Rapid Development of CHO Cell Lines for High-Level Production of Recombinant Antibodies. BioProcess J, 2003; 2(2): 33-40. http://dx.doi.org/10.12665/J22.Allison.

 
Advantages of Therapeutic Protein Production in the Aquatic Plant Lemna

by John R. Gasdaska, PhD, David Spencer, PhD, and Lynn Dickey, PhD
Volume 2, Issue 2 (March/April 2003)

More than 130 drug and vaccine approvals for 95 entities over the last 20 years have generated roughly $30 billion in revenue for the biotech industry. The vast majority of this revenue comes from 30 proteins that have manufacturing bottlenecks resulting from the complexities of consistent protein production. The lag times involved in constructing mammalian cell fermentation facilities keeps supply of immensely successful high-volume drugs like Enbrel, Rituxan, and Remicade well below estimated demand. In other cases, the complexities of peptide synthesis threaten the potential of soon-to-be-launched or recently approved drugs like Fuzeon. The Pharmaceutical Research and Manufacturers of America (PhRMA) has documented more than 371 new biotech drugs in development, supporting the view that demand for many biopharmaceuticals will continue to outstrip supply. That number does not include the multitude of biotech drugs still in research stages...

Citation:
Gasdaska JR, Spencer D, Dickey L. Advantages of Therapeutic Protein Production in the Aquatic Plant Lemna. BioProcess J, 2003; 2(2): 49-56. http://dx.doi.org/10.12665/J22.Gasdaska.

 
Protein A Affinity Captures of Monoclonal Antibodies from Cell Culture Supernatants on 96-Column Microfilter Plates for Medium Throughput Analytical Support of Bioprocess Development

by Jacob Bongers, PhD, Paul N. Boyd, Ruth De Vries, Jim D. Faulkner, Marcia M. Federici, Joselina Gorniak, Anna E. Hills, Maggie M. Huang, Cindee Levow, Gregory J. Mazzola, Allison W. Moore, La Donna Nugent, Leonard T. Olszewski, Ashvin K. Patel, Kankindi Rwego, Thomas M. Smith, Mark Strohsacker, and Eileen Wilson
Volume 2, Issue 2 (March/April 2003)

Large scale genomics spurred the development of massively parallel methods of automated DNA purification and sequencing. These methods started with the 1962 development of a 96-well microtiter plate for miniature-scale serology studies. This simple laboratory device has since been greatly modified and extended to include numerous specialty multiwell plates contructed and/or coated with different materials for various purposes. The original 96-well (8x12 matrix) has expanded to include 384-well and higher densities. More recently, functionality and versatility have been greatly augmented by the incorporation of a filter, or thin membrane, into the bottom of the well. These multiwell microfilter plates can thus be employed in a flow-through mode, in addition to the familiar "put in" and "take out" pipetting and rinsing steps associated with traditional enzyme-linked immunosorbent assay (ELISA) microtiter plate methods...

Citation:
Bongers J et al. Protein A Affinity Captures of Monoclonal Antibodies from Cell Culture Supernatants on 96-Column Microfilter Plates for Medium Throughput Analytical Support of Bioprocess Development. BioProcess J, 2003; 2(2): 41-47. http://dx.doi.org/10.12665/J22.Bongers.

 
Replacement of Wheat Peptone During Development of a Defined Medium for Recombinant Sp2/0 Cells

by Michael C. Borys, PhD, Katherine Hughes, and Jon M. Ryan, PhD
Volume 2, Issue 2 (March/April 2003)

Peptones are protein digests composed mainly of amino acids and small peptides. Peptones have been used in mammalian cell culture medium as a serum substitute to enhance cell growth and product formation. The first part of this study describes our evaluation of peptones from different sources (soy, wheat, yeast, and casein) on the cell growth and productivity of Sp2/0 myeloma cells expressing recombinant prourokinase (r-ProUK). The results of these studies demonstrated that wheat peptone was the most effective plant peptone to increase r-ProUK yield. Addition of 2 g/L wheat peptone to the culture medium increased batch r-ProUK production between 28-67% compared to cells grown in the absence of peptone supplements. Peptones did not increase cell productivity, but increases r-ProUK yield through increased culture longevity...

Citation:
Borys MC, Hughes K, Ryan JM. Replacement of Wheat Peptone During Development of a Defined Medium for Recombinant Sp2/0 Cells. BioProcess J, 2003; 2(2): 57-64. http://dx.doi.org/10.12665/J22.Borys.

 
Electron Microscopy: Current Techniques Used in Product Safety

by Euan W. Milne
Volume 2, Issue 2 (March/April 2003)

Electron microscopy (EM) provides data for viral clearance studies, information on the presence and quantitation of endogenous retroviruses, and the detection and characterization of other potential contaminants. The technique is favored in this field because it is simple, reliable, and can give reliable quantitation for risk assessments. This article describes the main EM techniques currently used for testing cell cultures, culture supernatants, and bulk harvests. It also includes an in-depth description of a thin sectioning technique used to estimate virus titre in culture supernatants and bulk harvests...

Citation:
Milne EW. Electron Microscopy: Current Techniques Used in Product Safety. BioProcess J, 2003; 2(2): 65-68. http://dx.doi.org/10.12665/J22.Milne.

 
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