Evidence map›Paper›PMID 30742730›Full record

ArticlePlant biotechnology journal2019

Activity-based proteomics reveals nine target proteases for the recombinant protein-stabilizing inhibitor SlCYS8 in Nicotiana benthamiana.

Philippe V Jutras, Friederike Grosse-Holz, Farnusch Kaschani, Markus Kaiser, Dominique Michaud, Renier A L van der Hoorn

Open access · goldAbstract read
In one paragraph

Article in Plant biotechnology journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.1field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Papain-like cysteine proteases inFrontiers in plant science · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Extracellular proteolytic cascade in tomato activates immune protease Rcr3.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Article
  16. Review
  17. Article
  18. Production of Biopharmaceuticals inFrontiers in plant science · 2019
    Article
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 3 countries.

Philippe V JutrasDepartment of Plant Sciences, Plant Chemetics Laboratory, University of Oxford, Oxford, UK.ORCID 0000-0003-3310-4773
Friederike Grosse-HolzDepartment of Plant Sciences, Plant Chemetics Laboratory, University of Oxford, Oxford, UK.ORCID 0000-0002-7093-6838
Farnusch KaschaniChemische Biologie, Zentrum für Medizinische Biotechnologie, Fakultät für Biologie, Universität Duisburg-Essen, Essen, Germany.
Markus KaiserChemische Biologie, Zentrum für Medizinische Biotechnologie, Fakultät für Biologie, Universität Duisburg-Essen, Essen, Germany.
Dominique MichaudCentre de recherche et d'innovation sur les végétaux, Université Laval, Québec, Canada.ORCID 0000-0002-5177-1142
Renier A L van der HoornDepartment of Plant Sciences, Plant Chemetics Laboratory, University of Oxford, Oxford, UK.ORCID 0000-0002-3692-7487
University of Oxford · GBUniversity of Duisburg-Essen · DEUniversité Laval · CA

Funding

European Research Council 258413European Research Council 616449European Research Council 760331
6 · The paper itself

Abstract

Co-expression of protease inhibitors like the tomato cystatin SlCYS8 is useful to increase recombinant protein production in plants, but key proteases involved in protein proteolysis are still unknown. Here, we performed activity-based protein profiling to identify proteases that are inhibited by SlCYS8 in agroinfiltrated Nicotiana benthamiana. We discovered that SlCYS8 selectively suppresses papain-like cysteine protease (PLCP) activity in both apoplastic fluids and total leaf extracts, while not affecting vacuolar-processing enzyme and serine hydrolase activity. A robust concentration-dependent inhibition of PLCPs occurred in vitro when purified SlCYS8 was added to leaf extracts, indicating direct cystatin-PLCP interactions. Activity-based proteomics revealed that nine different Cathepsin-L/-F-like PLCPs are strongly inhibited by SlCYS8 in leaves. By contrast, the activity of five other Cathepsin-B/-H-like PLCPs, as well as 87 Ser hydrolases, was unaffected by SlCYS8. SlCYS8 expression prevented protein degradation by inhibiting intermediate and mature isoforms of granulin-containing proteases from the Resistant-to-Desiccation-21 (RD21) PLCP subfamily. Our data underline the key role of endogenous PLCPs on recombinant protein degradation and reveal candidate proteases for depletion strategies.

Indexed as

ProteomicsCystatinsNicotianaPeptide HydrolasesProtease InhibitorsRecombinant ProteinsCystatinsPeptide HydrolasesProtease InhibitorsRecombinant Proteinsactivity-based protein profilingcystatinNicotiana benthamianapapain-like cysteine proteasesprotease inhibitorproteomicsSlCYS8

Identifiers

PMID30742730
PMCPMC6662110
OpenAlexW2911943528

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.