ArticleThe New phytologist2024
The proteome of Nicotiana benthamiana is shaped by extensive protein processing.
Article in The New phytologist, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Toward simple, rapid, and deep plant proteome analysis with an in-cell proteomics strategy.Plant physiology · 2026Article
- Polyphenol oxidase depletion in Nicotiana benthamiana enhances recombinant protein purification and preserves native protein integrity.The New phytologist · 2026Article
- Organ-on-a-Chip and Microfluidic Plant Cell Culture Systems: The Next Frontier for Controlled Secondary Metabolite Production and Real-Time Metabolomic Monitoring.Plants (Basel, Switzerland) · 2026Review
- Shedding light on receptor kinase processing.PLoS pathogens · 2025Article
- Toward simple, rapid, and deep plant proteome analysis with an in-cell proteomics strategy.bioRxiv : the preprint server for biology · 2025Article
- Proteomic snapshot of pattern triggered immunity in the Arabidopsis leaf apoplast.The Plant journal : for cell and molecular biology · 2025Article
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Authors and funding
9 authors.
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Abstract
Processing by proteases irreversibly regulates the fate of plant proteins and hampers the production of recombinant proteins in plants, yet only few processing events have been described in agroinfiltrated Nicotiana benthamiana, which has emerged as the main transient protein expression platform in plant science and molecular pharming. Here, we used in-gel digests and mass spectrometry to monitor the migration and topography of 5040 plant proteins within a protein gel. By plotting the peptides over the gel slices, we generated peptographs that reveal where which part of each protein was detected within the protein gel. These data uncovered that 60% of the detected proteins have proteoforms that migrate at lower than predicted molecular weights, implicating extensive proteolytic processing. This analysis confirms the proteolytic removal and degradation of autoinhibitory prodomains of most but not all proteases, and revealed differential processing within pectinemethylesterase and lipase families. This analysis also uncovered intricate processing of glycosidases and uncovered that ectodomain shedding might be common for a diverse range of receptor-like kinases. Transient expression of double-tagged candidate proteins confirmed processing events in vivo. This large proteomic dataset implicates an elaborate proteolytic machinery shaping the proteome of N. benthamiana.
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