ArticleFEMS yeast research2007
Increase of calnexin gene dosage boosts the secretion of heterologous proteins by Hansenula polymorpha.
Article in FEMS yeast research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 35 citations in OpenAlex.
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- Targeted genome editing of plants and plant cells for biomanufacturing.Transgenic research · 2021Review
- Customized yeast cell factories for biopharmaceuticals: from cell engineering to process scale up.Microbial cell factories · 2021Review
- High-level expression of3 Biotech · 2019Article
- The effect of the unfolded protein response on the production of recombinant proteins in plants.Plant cell reports · 2015Review
- Secretion of truncated recombinant rabies virus glycoprotein with preserved antigenic properties using a co-expression system in Hansenula polymorpha.Journal of microbiology (Seoul, Korea) · 2013Article
- Systematic single-cell analysis of Pichia pastoris reveals secretory capacity limits productivity.PloS one · 2012Article
- Modeling and measuring intracellular fluxes of secreted recombinant protein in Pichia pastoris with a novel 34S labeling procedure.Microbial cell factories · 2011Article
- Expression of heparan sulfate sulfotransferases in Kluyveromyces lactis and preparation of 3'-phosphoadenosine-5'-phosphosulfate.Glycobiology · 2011Article
- A secreted serine protease of Paracoccidioides brasiliensis and its interactions with fungal proteins.BMC microbiology · 2010Article
- Calnexin improves the folding efficiency of mutant rhodopsin in the presence of pharmacological chaperone 11-cis-retinal.The Journal of biological chemistry · 2009Article
- Protein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview.Microbial cell factories · 2008Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The type I membrane protein calnexin is a conserved key component of the quality control mechanism in the endoplasmic reticulum. It functions as a molecular chaperone that monitors the folding state of nascent polypeptides entering the endoplasmic reticulum. Calnexin also behaves as a lectin, as its chaperoning activity involves binding of oligosaccharide moieties present on newly imported glycoproteins. We isolated the calnexin gene (HpCNE1) from the methylotrophic yeast Hansenula polymorpha, and used HpCNE1 expression plasmids for super-transformation of H. polymorpha strains secreting target proteins of biotechnological interest. The elevated dosage of HpCNE1 enhanced secretion of the four proteins tested: three glycoproteins and one unglycosylated product. Secretion of bacterial alginate epimerase AlgE1 was increased threefold on average, and secretion of both human interferon-gamma and fungal consensus phytase twofold. With phytase and AlgE1 this improvement was all the more remarkable, as the secretion level was already high in the original strains (g L(-1) range). The same approach improved secretion of human serum albumin, which lacks N-linked glycans, about twofold. Glycosylation of the pro-MFalpha1 leader may account for the effect of calnexin in this case. Our results argue that cooverexpression of calnexin can serve as a generally applicable tool for enhancing the secretion of all types of heterologous protein by H. polymorpha.
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