ArticleJournal of industrial microbiology & biotechnology2010
High-throughput screening and selection of yeast cell lines expressing monoclonal antibodies.
Article in Journal of industrial microbiology & biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 58 citations in OpenAlex.
- High-throughput process development from gene cloning to protein production.Microbial cell factories · 2023Review
- Advances in Cell Engineering of theMetabolites · 2022Review
- In-Solution IgG Titer Determination in Fermentation Broth Using Affibodies and Flow-Induced Dispersion Analysis.ACS omega · 2020Article
- Functional production of human antibody by the filamentous fungusFungal biology and biotechnology · 2020Article
- Improving the secretory expression of active recombinant AaIT in Pichia pastoris by changing the expression strain and plasmid.World journal of microbiology & biotechnology · 2018Article
- Improved microscale cultivation ofFungal biology and biotechnology · 2018Article
- The present state of the art in expression, production and characterization of monoclonal antibodies.Molecular diversity · 2016Review
- Automated pipeline for rapid production and screening of HIV-specific monoclonal antibodies using pichia pastoris.Biotechnology and bioengineering · 2015Article
- Inactivation of a GAL4-like transcription factor improves cell fitness and product yield in glycoengineered Pichia pastoris strains.Applied and environmental microbiology · 2015Article
- Enhanced production of recombinant secretory proteins in Pichia pastoris by optimizing Kex2 P1' site.PloS one · 2013Article
- Expression of recombinant antibodies.Frontiers in immunology · 2013Article
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- Generation of diploid Pichia pastoris strains by mating and their application for recombinant protein production.Microbial cell factories · 2012Article
- Systematic single-cell analysis of Pichia pastoris reveals secretory capacity limits productivity.PloS one · 2012Article
- Review
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Authors and funding
19 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The methylotrophic yeast Pichia pastoris has recently been engineered to express therapeutic glycoproteins with uniform human N-glycans at high titers. In contrast to the current art where producing therapeutic proteins in mammalian cell lines yields a final product with heterogeneous N-glycans, proteins expressed in glycoengineered P. pastoris can be designed to carry a specific, preselected glycoform. However, significant variability exists in fermentation performance between genotypically similar clones with respect to cell fitness, secreted protein titer, and glycan homogeneity. Here, we describe a novel, multidimensional screening process that combines high and medium throughput tools to identify cell lines producing monoclonal antibodies (mAbs). These cell lines must satisfy multiple selection criteria (high titer, uniform N-glycans and cell robustness) and be compatible with our large-scale production platform process. Using this selection process, we were able to isolate a mAb-expressing strain yielding a titer (after protein A purification) in excess of 1 g/l in 0.5-l bioreactors.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.