ArticlePloS one2013
Characterization of the Pichia pastoris protein-O-mannosyltransferase gene family.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 44 citations in OpenAlex.
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- Considerations for Glycoprotein Production.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Pathway engineering facilitates efficient protein expression in Pichia pastoris.Applied microbiology and biotechnology · 2022Review
- Microfluidic screening and genomic mutation identification for enhancing cellulase production in Pichia pastoris.Biotechnology for biofuels and bioproducts · 2022Article
- What makes Komagataella phaffii non-conventional?FEMS yeast research · 2021Review
- Structural, Evolutionary, and Functional Analysis of the Protein O-Mannosyltransferase Family in Pathogenic Fungi.Journal of fungi (Basel, Switzerland) · 2021Review
- Engineering of Yeast Glycoprotein Expression.Advances in biochemical engineering/biotechnology · 2021Article
- Synthetic Glycobiology: Parts, Systems, and Applications.ACS synthetic biology · 2020Review
- Challenging the workhorse: Comparative analysis of eukaryotic micro-organisms for expressing monoclonal antibodies.Biotechnology and bioengineering · 2019Article
- EngineeringRSC advances · 2019Article
- Recombinant O-mannosylated protein production (PstS-1) from Mycobacterium tuberculosis in Pichia pastoris (Komagataella phaffii) as a tool to study tuberculosis infection.Microbial cell factories · 2019Article
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- Engineering yeast for producing human glycoproteins: where are we now?Future microbiology · 2015Article
- Protein expression in Pichia pastoris: recent achievements and perspectives for heterologous protein production.Applied microbiology and biotechnology · 2014Review
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Authors and funding
17 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The methylotrophic yeast, Pichiapastoris, is an important organism used for the production of therapeutic proteins. However, the presence of fungal-like glycans, either N-linked or O-linked, can elicit an immune response or enable the expressed protein to bind to mannose receptors, thus reducing their efficacy. Previously we have reported the elimination of β-linked glycans in this organism. In the current report we have focused on reducing the O-linked mannose content of proteins produced in P. pastoris, thereby reducing the potential to bind to mannose receptors. The initial step in the synthesis of O-linked glycans in P. pastoris is the transfer of mannose from dolichol-phosphomannose to a target protein in the yeast secretory pathway by members of the protein-O-mannosyltransferase (PMT) family. In this report we identify and characterize the members of the P. pastoris PMT family. Like Candida albicans, P. pastoris has five PMT genes. Based on sequence homology, these PMTs can be grouped into three sub-families, with both PMT1 and PMT2 sub-families possessing two members each (PMT1 and PMT5, and PMT2 and PMT6, respectively). The remaining sub-family, PMT4, has only one member (PMT4). Through gene knockouts we show that PMT1 and PMT2 each play a significant role in O-glycosylation. Both, by gene knockouts and the use of Pmt inhibitors we were able to significantly reduce not only the degree of O-mannosylation, but also the chain-length of these glycans. Taken together, this reduction of O-glycosylation represents an important step forward in developing the P. pastoris platform as a suitable system for the production of therapeutic glycoproteins.
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