ReviewMicrobial cell factories2025
Recombinant production of antimicrobial proteins in bacterial expression systems: Escherichia coli vs. lactic acid bacteria.
Review in Microbial cell factories, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed.
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
backgroundThe development of antimicrobial treatments as alternatives to antibiotics to combat antimicrobial-resistant (AMR) bacteria is a global priority. Antimicrobial peptides and proteins such as Host Defense Peptides (HDPs) and endolysins are one of the alternatives that are being explored. HDPs are small, cationic, and amphiphilic antimicrobial peptides derived from the innate immune system exhibiting a broad-spectrum antimicrobial activity. On the other hand, endolysins are enzymes produced by bacteriophages to hydrolyze the bacterial peptidoglycan layer, offering more specific antimicrobial activity than HDPs. While short peptides can be chemically synthesized, this approach presents several limitations, and recombinant production is also being used. Escherichia coli is the most used bacterial expression system for protein production. Alternative systems based on Generally Recognized as Safe (GRAS) microorganisms such as Lactic Acid Bacteria (LAB) have also been employed. However, so far, no comparative studies have evaluated the production and activity of antimicrobial proteins expressed in E. coli versus LAB and this study aims to address that gap.
resultsTo evaluate potential differences in the production of antimicrobial proteins using E. coli and two LAB (Lactococcus lactis and Lactiplantibacillus plantarum) hosts, various proteins were evaluated. These included two HDPs fused to a GFP, two multidomain HDP-based proteins and one endolysin. The results revealed a clear influence of the expression system on the quality of HDP-based protein, including both GFP fusions and multidomain constructs. Protein yield was higher in E. coli and all HDP-based proteins exhibited higher antimicrobial activity when expressed in E. coli compared to L. lactis and L. plantarum. In contrast, endolysin activity was comparable when produced in E. coli and L. lactis.
conclusionsThese results demonstrate that the choice of bacterial expression host significantly affects not only the yield but, more importantly, the antimicrobial activity of HDP-based proteins. For these proteins, the antimicrobial activity was consistently higher when produced in E. coli. In contrast, endolysins exhibited similar characteristics regardless of whether they were expressed in E. coli or in L. lactis.
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