ArticleBiotechnology journal2014
The human anti-HIV antibodies 2F5, 2G12, and PG9 differ in their susceptibility to proteolytic degradation: down-regulation of endogenous serine and cysteine proteinase activities could improve antibody production in plant-based expression platforms.
Article in Biotechnology journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 69 citations in OpenAlex.
- Nicotiana benthamiana's Responses to Agroinfiltration, a Treasure Grove of New Avenues to Improve Protein Yields in Plant Molecular Farming.Plant biotechnology journal · 2026Review
- Translational insights into manufacturability and stability of broadly neutralizing antibodies for pediatric HIV prevention: lessons from plant-produced CAP256-VRC26.25.Frontiers in pediatrics · 2026Article
- Localising enzymes to biomolecular condensates increases their accumulation and benefits engineered metabolic pathway performance in Nicotiana benthamiana.Plant biotechnology journal · 2026Article
- How Can Plant-Derived Natural Products and Plant Biotechnology Help Against Emerging Viruses?International journal of molecular sciences · 2025Review
- Optimized expression of human interleukin-15 inBiotechnology reports (Amsterdam, Netherlands) · 2025Article
- Advances in promoter engineering strategies for enhanced recombinant protein expression in plants.Frontiers in plant science · 2025Review
- SBT5.2s are the major active extracellular subtilases processing IgG antibody 2F5 in the Nicotiana benthamiana apoplast.Plant biotechnology journal · 2024Article
- Improving transient protein expression in agroinfiltrated Nicotiana benthamiana.The New phytologist · 2024Review
- Advances in Subcellular Accumulation Design for Recombinant Protein Production in Tobacco.Biodesign research · 2024Review
- Three Parts of the Plant Genome: On the Way to Success in the Production of Recombinant Proteins.Plants (Basel, Switzerland) · 2022Review
- Prevention of Shiga toxin 1-caused colon injury by plant-derived recombinant IgA.Scientific reports · 2022Article
- Transient proteolysis reduction ofFrontiers in plant science · 2022Article
- Optimising expression and extraction of recombinant proteins in plants.Frontiers in plant science · 2022Review
- Review
- Contributions of the international plant science community to the fight against human infectious diseases - part 1: epidemic and pandemic diseases.Plant biotechnology journal · 2021Review
- Generation of enzymatically competent SARS-CoV-2 decoy receptor ACE2-Fc in glycoengineered Nicotiana benthamiana.Biotechnology journal · 2021Article
- Identification of two subtilisin-like serine proteases engaged in the degradation of recombinant proteins in Nicotiana benthamiana.FEBS letters · 2021Article
- Reteplase Fc-fusions produced in N. benthamiana are able to dissolve blood clots ex vivo.PloS one · 2021Article
- The Instability of Dimeric Fc-Fusions Expressed in Plants Can Be Solved by Monomeric Fc Technology.Frontiers in plant science · 2021Article
- A New Plant Expression System for Producing Pharmaceutical Proteins.Molecular biotechnology · 2020Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
Abstract
The tobacco-related species Nicotiana benthamiana has recently emerged as a promising host for the manufacturing of protein therapeutics. However, the production of recombinant proteins in N. benthamiana is frequently hampered by undesired proteolysis. Here, we show that the expression of the human anti-HIV antibodies 2F5, 2G12, and PG9 in N. benthamiana leaves leads to the accumulation of discrete heavy chain-derived degradation products of 30-40 kDa. Incubation of purified 2F5 with N. benthamiana intercellular fluid resulted in rapid conversion into the 40-kDa fragment, whereas 2G12 proved largely resistant to degradation. Such a differential susceptibility to proteolytic attack was also observed when these two antibodies were exposed to various types of proteinases in vitro. While serine and cysteine proteinases are both capable of generating the 40-kDa 2F5 fragment, the 30-kDa polypeptide is most readily obtained by treatment with the latter class of enzymes. The principal cleavage sites reside within the antigen-binding domain, the VH -CH 1 linker segment and the hinge region of the antibodies. Collectively, these results indicate that down-regulation of endogenous serine and cysteine proteinase activities could be used to improve the performance of plant-based expression platforms destined for the production of biopharmaceuticals.
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Registered trials
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.