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Review
. 2024 Mar-Apr:71:108296.
doi: 10.1016/j.biotechadv.2023.108296. Epub 2023 Dec 1.

Recombinant production of antimicrobial peptides in plants

Farhad Nazarian-Firouzabadi  1 , Marcelo Der Torossian Torres  2 , Cesar de la Fuente-Nunez  3
Affiliations
Review

Recombinant production of antimicrobial peptides in plants

Farhad Nazarian-Firouzabadi et al. Biotechnol Adv. 2024 Mar-Apr.

Abstract

Classical plant breeding methods are limited in their ability to confer disease resistance on plants. However, in recent years, advancements in molecular breeding and biotechnological have provided new approaches to overcome these limitations and protect plants from disease. Antimicrobial peptides (AMPs) constitute promising agents that may be able to protect against infectious agents. Recently, peptides have been recombinantly produced in plants at scale and low cost. Because AMPs are less likely than conventional antimicrobials to elicit resistance of pathogenic bacteria, they open up exciting new avenues for agricultural applications. Here, we review recent advances in the design and production of bioactive recombinant AMPs that can effectively protect crop plants from diseases.

Keywords: Antimicrobial peptides; Genetic engineering; Recombinant technology; Transgenic plants.

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Conflict of interest statement

Declaration of Competing Interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Cesar de la Fuente-Nunez provides consulting services to Invaio Sciences and is a member of the Scientific Advisory Boards of Nowture S.L., Peptidus, and Phare Bio. De la Fuente is also on the Advisory Board of the Peptide Drug Hunting Consortium (PDHC). The de la Fuente Lab has received research funding or in-kind donations from United Therapeutics, Strata Manufacturing PJSC, and Procter & Gamble, none of which were used in support of this work.

Figures

Fig. 1.
Fig. 1.. Physicochemical features of plant-derived AMPs.
The AMPs were obtained from the Database of Antimicrobial Activity and Structure of Peptides (DBAASP) server, as well as the physicochemical features that are most relevant to their antimicrobial activity: (A) net charge, (B) normalized hydrophobicity, (C) angle subtended by the hydrophobic residues, and (D) amphiphilicity index.
Fig. 2.
Fig. 2.. The mode of action proposed for the activity of a recombinant AMP against a fungal pathogen.
First, the chitin-binding domain (CBD) aids and guides the AMP to aggregate on the pathogen cell wall surface. Second, the CBD anchors the AMP in the cell wall by covering the surface. Third, AMP permeabilizes the pathogen plasma membrane, resulting in pore formation, cell leakage, and eventually pathogen cell death (Badrhadad et al., 2018).
Fig. 3.
Fig. 3.. AMP-delivery methods to plant cells.
Gene cloning approach for AMP and AMP fusion introduction either by: A) Agrobacterium-mediated transformation; or B) through biolistic method. Gene elements are colored and named flanked by T-DNA borders. C) Nanoparticle-mediated and D) micelle-mediated AMP delivery. Micelles and nanoparticles are loaded with cationic AMPs prior to plant transformation procedure.
See this image and copyright information in PMC

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