Evidence map›Paper›PMID 37138331›Full record

ArticleMicrobial cell factories2023

Biosensor-guided rapid screening for improved recombinant protein secretion in Pichia pastoris.

Laura Navone, Kaylee Moffitt, James Behrendorff, Pawel Sadowski, Carol Hartley, Robert Speight

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.5field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Screening microorganisms with robust and stable protein expression and secretion capacity.Protein science : a publication of the Protein Society · 2025
    Article
  5. Article
  6. Review
  7. Microorganisms · 2024
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Laura NavoneSchool of Biology and Environmental Science, Faculty of Science, Queensland University of Technology (QUT), Brisbane, QLD, 4000, Australia. laura.navone@qut.edu.au.
Kaylee MoffittSchool of Biology and Environmental Science, Faculty of Science, Queensland University of Technology (QUT), Brisbane, QLD, 4000, Australia.
James BehrendorffSchool of Biology and Environmental Science, Faculty of Science, Queensland University of Technology (QUT), Brisbane, QLD, 4000, Australia.
Pawel SadowskiCentral Analytical Research Facility (CARF), Queensland University of Technology (QUT), Brisbane, QLD, 4000, Australia.
Carol HartleyCSIRO Environment, Canberra, ACT, 2600, Australia.
Robert SpeightSchool of Biology and Environmental Science, Faculty of Science, Queensland University of Technology (QUT), Brisbane, QLD, 4000, Australia.
Queensland University of Technology · AUARC Centre of Excellence in Synthetic Biology · AUCommonwealth Scientific and Industrial Research Organisation · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pichia pastoris (Komagataella phaffii) is widely used for industrial production of heterologous proteins due to high secretory capabilities but selection of highly productive engineered strains remains a limiting step. Despite availability of a comprehensive molecular toolbox for construct design and gene integration, there is high clonal variability among transformants due to frequent multi-copy and off-target random integration. Therefore, functional screening of several hundreds of transformant clones is essential to identify the best protein production strains. Screening methods are commonly based on deep-well plate cultures with analysis by immunoblotting or enzyme activity assays of post-induction samples, and each heterologous protein produced may require development of bespoke assays with multiple sample processing steps. In this work, we developed a generic system based on a P. pastoris strain that uses a protein-based biosensor to identify highly productive protein secretion clones from a heterogeneous set of transformants. The biosensor uses a split green fluorescent protein where the large GFP fragment (GFP1-10) is fused to a sequence-specific protease from Tobacco Etch Virus (TEV) and is targeted to the endoplasmic reticulum. Recombinant proteins targeted for secretion are tagged with the small fragment of the split GFP (GFP11). Recombinant protein production can be measured by monitoring GFP fluorescence, which is dependent on interaction between the large and small GFP fragments. The reconstituted GFP is cleaved from the target protein by TEV protease, allowing for secretion of the untagged protein of interest and intracellular retention of the mature GFP. We demonstrate this technology with four recombinant proteins (phytase, laccase, β-casein and β-lactoglobulin) and show that the biosensor directly reports protein production levels that correlate with traditional assays. Our results confirm that the split GFP biosensor can be used for facile, generic, and rapid screening of P. pastoris clones to identify those with the highest production levels.

Indexed as

PichiaGreen Fluorescent ProteinsRecombinant ProteinsSaccharomycetalesGreen Fluorescent ProteinsRecombinant ProteinsBiosensorProtein productionScreeningSplit GFPYeast

Identifiers

PMID37138331
PMCPMC10155391
OpenAlexW4368356048

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.