ArticleFrontiers in plant science2015
Extracellular peptidase hunting for improvement of protein production in plant cells and roots.
Article in Frontiers in plant science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.
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Who cites it
17 citing papers in PubMed, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.
- Nicotiana hairy roots for recombinant protein expression, where to start? A systematic review.Molecular biology reports · 2023Pooled it
- Four guidelines to identify bona fide protease-substrate pairs.Journal of experimental botany · 2025Review
- Antimicrobial Peptides: The Production of Novel Peptide-Based Therapeutics in Plant Systems.Life (Basel, Switzerland) · 2023Review
- Mechanisms controlling plant proteases and their substrates.Cell death and differentiation · 2023Review
- Improving Protein Quantity and Quality-The Next Level of Plant Molecular Farming.International journal of molecular sciences · 2022Review
- Optimising expression and extraction of recombinant proteins in plants.Frontiers in plant science · 2022Review
- Exploring Posttranslational Modifications with the Plant PTM Viewer.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Cellular engineering of plant cells for improved therapeutic protein production.Plant cell reports · 2021Review
- Optimised production of an anti-fungal antibody in Solanaceae hairy roots to develop new formulations against Candida albicans.BMC biotechnology · 2020Article
- Plant proteases and programmed cell death.Journal of experimental botany · 2019Article
- Production of functional recombinant cyclic citrullinated peptide monoclonal antibody in transgenic rice cell suspension culture.Transgenic research · 2019Article
- Assessing Carnivorous Plants for the Production of Recombinant Proteins.Frontiers in plant science · 2019Article
- The Plastid and Mitochondrial Peptidase Network inThe Plant cell · 2017Review
- Agroinfiltration contributes to VP1 recombinant protein degradation.Bioengineered · 2016Article
- An Accessory Protease Inhibitor to Increase the Yield and Quality of a Tumour-Targeting mAb in Nicotiana benthamiana Leaves.PloS one · 2016Article
- Plants as Factories for Human Pharmaceuticals: Applications and Challenges.International journal of molecular sciences · 2015Review
- Commentary: Extracellular peptidase hunting for improvement of protein production in plant cells and roots.Frontiers in plant science · 2015Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plant-based recombinant protein production systems have gained an extensive interest over the past few years, because of their reduced cost and relative safety. Although the first products are now reaching the market, progress are still needed to improve plant hosts and strategies for biopharming. Targeting recombinant proteins toward the extracellular space offers several advantages in terms of protein folding and purification, but degradation events are observed, due to endogenous peptidases. This paper focuses on the analysis of extracellular proteolytic activities in two production systems: cell cultures and root-secretion (rhizosecretion), in Arabidopsis thaliana and Nicotiana tabacum. Proteolytic activities of extracellular proteomes (secretomes) were evaluated in vitro against two substrate proteins: bovine serum albumin (BSA) and human serum immunoglobulins G (hIgGs). Both targets were found to be degraded by the secretomes, BSA being more prone to proteolysis than hIgGs. The analysis of the proteolysis pH-dependence showed that target degradation was mainly dependent upon the production system: rhizosecretomes contained more peptidase activity than extracellular medium of cell suspensions, whereas variations due to plant species were smaller. Using class-specific peptidase inhibitors, serine, and metallopeptidases were found to be responsible for degradation of both substrates. An in-depth in silico analysis of genomic and transcriptomic data from Arabidopsis was then performed and led to the identification of a limited number of serine and metallo-peptidases that are consistently expressed in both production systems. These peptidases should be prime candidates for further improvement of plant hosts by targeted silencing.
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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.