Evidence map›Paper›PMID 27893815›Full record

ArticlePloS one2016

An Accessory Protease Inhibitor to Increase the Yield and Quality of a Tumour-Targeting mAb in Nicotiana benthamiana Leaves.

Philippe V Jutras, Carla Marusic, Chiara Lonoce, Carole Deflers, Marie-Claire Goulet, Eugenio Benvenuto, Dominique Michaud, Marcello Donini

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
4.8field-weighted citation impact, top 6% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 38 citations in OpenAlex.

  1. Pooled it
  2. Review
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  5. Review
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  8. Product safety aspects of plant molecular farming.Frontiers in bioengineering and biotechnology · 2023
    Review
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  15. Review
  16. Article
  17. Article
  18. Article
  19. Production of Biopharmaceuticals inFrontiers in plant science · 2019
    Article
  20. 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

8 authors at 2 institutions in 2 countries.

Philippe V JutrasDépartement de phytologie, Université Laval, Québec Quebec, Canada.
Carla MarusicLaboratory of Biotechnology ENEA Research Center, Casaccia, Rome, Italy.
Chiara LonoceLaboratory of Biotechnology ENEA Research Center, Casaccia, Rome, Italy.
Carole DeflersDépartement de phytologie, Université Laval, Québec Quebec, Canada.
Marie-Claire GouletDépartement de phytologie, Université Laval, Québec Quebec, Canada.
Eugenio BenvenutoLaboratory of Biotechnology ENEA Research Center, Casaccia, Rome, Italy.
Dominique MichaudDépartement de phytologie, Université Laval, Québec Quebec, Canada.ORCID http://orcid.org/0000-0002-5177-1142
Marcello DoniniLaboratory of Biotechnology ENEA Research Center, Casaccia, Rome, Italy.
National Agency for New Technologies, Energy and Sustainable Economic Development · ITUniversité Laval · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The overall quality of recombinant IgG antibodies in plants is dramatically compromised by host endogenous proteases. Different approaches have been developed to reduce the impact of endogenous proteolysis on IgGs, notably involving site-directed mutagenesis to eliminate protease-susceptible sites or the in situ mitigation of host protease activities to minimize antibody processing in the cell secretory pathway. We here characterized the degradation profile of H10, a human tumour-targeting monoclonal IgG, in leaves of Nicotiana benthamiana also expressing the human serine protease inhibitor α1-antichymotrypsin or the cysteine protease inhibitor tomato cystatin SlCYS8. Leaf extracts revealed consistent fragmentation patterns for the recombinant antibody regardless of leaf age and a strong protective effect of SlCYS8 in specific regions of the heavy chain domains. As shown using an antigen-binding ELISA and LC-MS/MS analysis of antibody fragments, SlCYS8 had positive effects on both the amount of fully-assembled antibody purified from leaf tissue and the stability of biologically active antibody fragments containing the heavy chain Fc domain. Our data confirm the potential of Cys protease inhibitors as convenient antibody-stabilizing expression partners to increase the quality of therapeutic antibodies in plant protein biofactories.

Indexed as

alpha 1-AntichymotrypsinAmino Acid SequenceAntibodies, MonoclonalCystatinsCysteine Proteinase InhibitorsHumansImmunoglobulin GNeoplasmsNicotianaPeptide HydrolasesPlant LeavesPlants, Genetically ModifiedProteolysisRecombinant ProteinsSolanum lycopersicumalpha 1-AntichymotrypsinAntibodies, MonoclonalCystatinsCysteine Proteinase InhibitorsImmunoglobulin GPeptide HydrolasesRecombinant Proteins

Identifiers

PMID27893815
PMCPMC5125672
OpenAlexW2559057013

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.