ArticlePloS one2010
Maltose-binding protein enhances secretion of recombinant human granzyme B accompanied by in vivo processing of a precursor MBP fusion protein.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- Boosting Recombinant Bovine Chymosin inFoods (Basel, Switzerland) · 2026Article
- An outlook to sophisticated technologies and novel developments for metabolic regulation in theFrontiers in bioengineering and biotechnology · 2023Review
- Secretome-based screening of fusion partners and their application in recombinant protein secretion in Saccharomyces cerevisiae.Applied microbiology and biotechnology · 2022Article
- A versatile modular vector set for optimizing protein expression among bacterial, yeast, insect and mammalian hosts.PloS one · 2019Article
- A Novel and Fast Purification Method for Nucleoside Transporters.Frontiers in molecular biosciences · 2016Article
- Enhanced secretion of a methyl parathion hydrolase in Pichia pastoris using a combinational strategy.Microbial cell factories · 2015Article
- Protein production in Yarrowia lipolytica via fusion to the secreted lipase Lip2p.Molecular biotechnology · 2014Article
- EGFR-targeted granzyme B expressed in NK cells enhances natural cytotoxicity and mediates specific killing of tumor cells.PloS one · 2013Article
- How to achieve high-level expression of microbial enzymes: strategies and perspectives.BioengineeredReview
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe apoptosis-inducing serine protease granzyme B (GrB) is an important factor contributing to lysis of target cells by cytotoxic lymphocytes. Expression of enzymatically active GrB in recombinant form is a prerequisite for functional analysis and application of GrB for therapeutic purposes. METHODS AND
findingsWe investigated the influence of bacterial maltose-binding protein (MBP) fused to GrB via a synthetic furin recognition motif on the expression of the MBP fusion protein also containing an N-terminal α-factor signal peptide in the yeast Pichia pastoris. MBP markedly enhanced the amount of GrB secreted into culture supernatant, which was not the case when GrB was fused to GST. MBP-GrB fusion protein was cleaved during secretion by an endogenous furin-like proteolytic activity in vivo, liberating enzymatically active GrB without the need of subsequent in vitro processing. Similar results were obtained upon expression of a recombinant fragment of the ErbB2/HER2 receptor protein or GST as MBP fusions.
conclusionsOur results demonstrate that combination of MBP as a solubility enhancer with specific in vivo cleavage augments secretion of processed and functionally active proteins from yeast. This strategy may be generally applicable to improve folding and increase yields of recombinant proteins.
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