ArticleApplied microbiology and biotechnology2013
Codon optimization, expression, purification, and functional characterization of recombinant human IL-25 in Pichia pastoris.
Article in Applied microbiology and biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers, 1 of them a synthesis that pooled it.
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9 citing papers in PubMed, 1 synthesis or guideline pooled it, 26 citations in OpenAlex.
- A Systematic Review of the Potential of Pichia pastoris (Komagataella phaffii) as an Alternative Host for Biologics Production.Molecular biotechnology · 2024Pooled it
- Improved secretion of recombinant human IL-25 in HEK293 cells using a signal peptide-pro-peptide domain derived from Trypsin-1.Biotechnology letters · 2021Article
- Accurately cleavable goat β-lactoglobulin signal peptide efficiently guided translation of a recombinant human plasminogen activator in transgenic rabbit mammary gland.Bioscience reports · 2019Article
- Production of Universal Group O Red Blood Cells by Alpha-Indian journal of hematology & blood transfusion : an official journal of Indian Society of Hematology and Blood Transfusion · 2019Article
- Characterization of human S-adenosyl-homocysteine hydrolase in vitro and identification of its potential inhibitors.Journal of enzyme inhibition and medicinal chemistry · 2017Article
- Characterization and high-yield production of non-Engineering in life sciences · 2017Article
- Bioprocess development for extracellular production of recombinant human interleukin-3 (hIL-3) in Pichia pastoris.Journal of industrial microbiology & biotechnology · 2016Article
- Recent advances in the production of recombinant subunit vaccines in Pichia pastoris.Bioengineered · 2016Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interleukin (IL)-25 (also known as IL-17E) is a distinct member of the IL-17 cytokine family which induces IL-4, IL-5, and IL-13 expression and promotes pathogenic T helper (Th)-2 cell responses in various organs. IL-25 has been shown to have crucial role between innate and adaptive immunity and also a key component of the protection of gastrointestinal helminthes. In this study, to produce bioactive recombinant human IL-25 (rhIL-25), the cDNA of mature IL-25 was performed codon optimization based on methylotropic yeast Pichia pastoris codon bias and cloned into the expression vector pPICZαA. The recombinant vector was transformed into P. pichia strain X-33 and selected by zeocin resistance. Benchtop fermentation and simple purification strategy were established to purify the rhIL-25 with about 17 kDa molecular mass. Functional analysis showed that purified rhIL-25 specifically bond to receptor IL-17BR and induce G-CSF production in vitro. Further annexin V-FITC/PI staining assay indicated that rhIL-25 induced apoptosis in two breast cancer cells, MDA-MB-231 and HBL-100. This study provides a new strategy for the large-scale production of bioactive IL-25 for biological and therapeutic applications.
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