ArticleBiotechnology and bioengineering2021
Development of a platform process for the production and purification of single-domain antibodies.
Article in Biotechnology and bioengineering, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- Pichia-CLM: A language model-based codon optimization pipeline forProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Systematic perturbation of cultures of K. phaffii by carbon co-feeding show gene signatures associated with production of recombinant proteins.Microbial cell factories · 2026Article
- Characterization of a Potential Therapeutic Anti-Canine PD-1 Single Domain Antibody Produced in Yeast.Veterinary sciences · 2025Article
- CRISPR-Cas9 knockout screen informs efficient reduction of the Komagataella phaffii secretome.Microbial cell factories · 2024Article
- Anti-hemagglutinin monomeric nanobody provides prophylactic immunity against H1 subtype influenza A viruses.PloS one · 2024Article
- Engineered SARS-CoV-2 receptor binding domain improves manufacturability in yeast and immunogenicity in mice.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Rapid optimization of processes for the integrated purification of biopharmaceuticals.Biotechnology and bioengineering · 2021Article
- Development of a platform process for the production and purification of single-domain antibodies.Biotechnology and bioengineering · 2021Article
- Engineered SARS-CoV-2 receptor binding domain improves immunogenicity in mice and elicits protective immunity in hamsters.bioRxiv : the preprint server for biology · 2021Article
Corrections and comments
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Authors and funding
14 authors at 3 institutions in 2 countries.
Funding
Abstract
Single-domain antibodies (sdAbs) offer the affinity and therapeutic value of conventional antibodies, with increased stability and solubility. Unlike conventional antibodies, however, sdAbs do not benefit from a platform manufacturing process. While successful production of a variety of sdAbs has been shown in numerous hosts, purification methods are often molecule specific or require affinity tags, which generally cannot be used in clinical manufacturing due to regulatory concerns. Here, we have developed a broadly applicable production and purification process for sdAbs in Komagataella phaffii (Pichia pastoris) and demonstrated the production of eight different sdAbs at a quality appropriate for nonclinical studies. We developed a two-step, integrated purification process without the use of affinity resins and showed that modification of a single process parameter, pH of the bridging buffer, was required for the successful purification of a variety of sdAbs. Further, we determined that this parameter can be predicted based only on the biophysical characteristics of the target molecule. Using these methods, we produced nonclinical quality sdAbs as few as 5 weeks after identifying the product sequence. Nonclinical studies of three different sdAbs showed that molecules produced using our platform process conferred protection against viral shedding of rotavirus or H1N1 influenza and were equivalent to similar molecules produced in Escherichia coli and purified using affinity tags.
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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.