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- Title
Expression strategies for the efficient synthesis of antimicrobial peptides in plastids.
- Authors
Hoelscher, Matthijs P.; Forner, Joachim; Calderone, Silvia; Krämer, Carolin; Taylor, Zachary; Loiacono, F. Vanessa; Agrawal, Shreya; Karcher, Daniel; Moratti, Fabio; Kroop, Xenia; Bock, Ralph
- Abstract
Antimicrobial peptides (AMPs) kill microbes or inhibit their growth and are promising next-generation antibiotics. Harnessing their full potential as antimicrobial agents will require methods for cost-effective large-scale production and purification. Here, we explore the possibility to exploit the high protein synthesis capacity of the chloroplast to produce AMPs in plants. Generating a large series of 29 sets of transplastomic tobacco plants expressing nine different AMPs as fusion proteins, we show that high-level constitutive AMP expression results in deleterious plant phenotypes. However, by utilizing inducible expression and fusions to the cleavable carrier protein SUMO, the cytotoxic effects of AMPs and fused AMPs are alleviated and plants with wild-type-like phenotypes are obtained. Importantly, purified AMP fusion proteins display antimicrobial activity independently of proteolytic removal of the carrier. Our work provides expression strategies for the synthesis of toxic polypeptides in chloroplasts, and establishes transplastomic plants as efficient production platform for antimicrobial peptides. Antimicrobial peptides (AMPs) are promising next-generation antibiotics, but are difficult to produce due to the toxicity to bacterial hosts. Here, the authors report the utilization of transplastomic tobacco plants for AMPs production without cytotoxic effects via inducible expression systems and fusions to cleavable carrier protein.
- Subjects
ANTIMICROBIAL peptides; PEPTIDE synthesis; SMALL ubiquitin-related modifier proteins; CARRIER proteins; CHIMERIC proteins; PEPTIDE antibiotics; ANTIBIOTICS
- Publication
Nature Communications, 2022, Vol 13, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-022-33516-1