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Review
. 2022 Apr 8:9:851052.
doi: 10.3389/fvets.2022.851052. eCollection 2022.

Antimicrobial Peptides: Bringing Solution to the Rising Threats of Antimicrobial Resistance in Livestock

Affiliations
Review

Antimicrobial Peptides: Bringing Solution to the Rising Threats of Antimicrobial Resistance in Livestock

Shamsaldeen Ibrahim Saeed et al. Front Vet Sci. .

Abstract

Antimicrobial therapy is the most applied method for treating and preventing bacterial infection in livestock. However, it becomes less effective due to the development of antimicrobial resistance (AMR). Therefore, there is an urgent need to find new antimicrobials to reduce the rising rate of AMR. Recently, antimicrobial peptides (AMPs) have been receiving increasing attention due to their broad-spectrum antimicrobial activity, rapid killing activities, less toxicity, and cell selectivity. These features make them potent and potential alternative antimicrobials to be used in animals. Here, we discuss and summarize the AMPs in animals, classification, structures, mechanisms of action, and their potential use as novel therapeutic alternative antimicrobials to tackle the growing AMR threat.

Keywords: alternative antimicrobial; antimicrobial peptides (AMPs); antimicrobial resistance (AMR); bacterial infection; livestock.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
Classification of AMPs.
Figure 2
Figure 2
The diagram illustrated the main structural classes of AMPs: (A) β-sheet, defensins, and protegrins; (B) extended, indolicidin; (C) α-helical, nisin, and lactoferricin; (D) loop or combined structure, plectasin. The image was created using UCSF Chimera (http://www.cgl.ucsf.edu/chimera).
Figure 3
Figure 3
The interaction between peptide and bacterial cellular membrane. The image was created using BioRender illustrator (https://Biorender.com/).
Figure 4
Figure 4
Mechanism for intracellular antimicrobial peptide activity. The image was created using BioRender illustrator (https://Biorender.com/).
Figure 5
Figure 5
The diagram illustrates the peptide structure for plectasin (A), nisin (B), lactoferricin (C), and indolicin (D). The image was created using UCSF Chimera (http://www.cgl.ucsf.edu/chimera).

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