Review Article

Microbial- and Plant-Derived Bioactive Peptides and Their Applications against Foodborne Pathogens: Current Status and Future Prospects

Table 2

Microbe-derived bioactive peptides and their potential antimicrobial applications.

Name of the peptideMicrobial sourceTarget pathogenMode of actionReferences

PediocinsPediococcus spp.BacteriaDisrupt proton motive force, formation of pores in the cytoplasmic membrane, and cell membrane dysfunction[69]
Listeria monocytogenes

NisinLactococcus lactisBacteriaPore formation and the inhibition of cell wall biosynthesis[7072]
Listeria monocytogenes
Streptococcus aureus
Spore-forming Bacillus Clostridium species

Lacticin 3147Lactococcus lactisBacteriaCell wall disruption and pore formation[70]
Staphylococcus aureus
Enterococcus faecalis
Pneumococcus
Propionibacterium acnes, Streptococcus mutans, and Listeria monocytogenes
Bacillus cereus

Enterocin AEnterococcus faeciumBacteriaInteracts with cell wall and cell receptor, membrane permeabilization causes the leakage, and interferes in DNA replication and mRNA synthesis and transcription[72, 73]
L. monocytogenes
Staphylococcus aureus and Salmonella enterica

PropionicinP. thoenii, P. jensenii, and P. freudenreichiiBacteriaUnknown[74, 75]
Helicobacter pylori
Listeria monocytogenes
Corynebacterium spp.
Vibrio parahaemolyticus
Yersinia enterocolitica
Pseudomonas spp.,
Saccharomyces spp.
Aspergillus spp.
Fungi
Aspergillus wentii and Apiotrichum curvatum
Fusarium tricinctum and Phialophora gregata
Candida, Saccharomyces, and Scopulariopsis genera

LynronneRumen microbiomeBacteriaMembrane permeabilization pore formation and lysis[76, 77]
Staphylococcus aureus
Acinetobacter baumannii
P. aeruginosa

Gramicidin SAneurinibacillus migulanusBacteriaBinding of peptides to Gram-negative LPS and their ability to disrupt Gram-negative cell membranes, accumulation of bacterial membrane phospholipids, and pore formation in the cell membrane[78, 79]
E. coli
Klebsiella pneumoniae and Pseudomonas aeruginosa
Acinetobacter baumannii Staphylococcus aureus
Enterococcus faecium

Gramicidin ABacillus brevisBacteriaMembrane permeabilization, interruption of internal molecular function (DNA and protein functions), formation of hydroxyl free radicals, and the imbalance of NADH metabolism[80, 81]
Staphylococcus aureus

Gramicidin A (1)Bacillus brevisBacteriaDisrupts the transmembrane ion concentration gradient by forming an ion channel in a lipid bilayer[82]
S. pyogenes and S. pneumoniae
Enterococcus faecalis
Streptococcus agalactiae

Endolysins (phage-derived AMP)Bacteriophages of A. baumanniiBacteriaCause hydrolysis of bacterial cell wall[83]
Acinetobacter baumannii
Fungi
Aspergillus fumigatus
Candida albicans

TyrocidinesBacillus aneurinolyticusBacteriaBinds to bacterial membranes and disrupts structural integrity, resulting in bacterial cell death, disruption of the asexual cycle of the parasite and inhibit the respiration of parasitized red cells[8487]
B. Subtilis
C. albicans
Parasite
Caenorhabditis elegans
Plamodium gallinaceum

ValinomycinStreptomyces cavourensis, S. fulvissimus, S. roseochromogenes, and S. griseusBacteriaDegradation of glycolytic ATP affects respiration and disrupts the K+ ion gradient across the cell membrane, and the unbalanced distribution of ions in the bacterium causes cell death and fungal cell wall and cell membrane permeabilization[8890]
Streptococcus faecalis and Micrococcus lysodeikticus
Staphylococcus aureus
Fungi
Candida albicans
Cryptococcus albidus

Aureobasidin A 1 (cyclodepsipeptides)Aureobasidium pullulans R106FungiAffect spore germination rate, germination initiation, polarized growth of germ tube, and elongation rate; inhibit inositolphosphoryl-ceramide (IPC) synthase; inhibition of sphingolipid biosynthesis resulting in loss of intracellular structure and vacuolization; and membrane trafficking which disturbed cell proliferation of the parasite[91]
Penicillium digitatum
P. italicum, P. expansum, Botrytis cinerea, and Monilinia fructicola
C. albicans, S. cerevisiae, and C. neoformans
A. fumigates, Schizosaccharomyces pombe, and A. nidulans
A. Niger and A. oryzae
Parasite
Toxoplasma gondii
Leishmania amazonensis

Colistin (polymyxin E)Paenibacillus polymyxaBacteriaIncrease the permeability of the bacterial membrane, leading to leakage of the cytoplasmic content and causing cell death, and bind to lipid portion A and neutralize and inhibit vital respiratory enzymes[92]
E. coli and A. baumannii
P. aeruginosa and Stenotrophomonas maltophilia
Enterobacter spp.
Klebsiella spp.
Citrobacter spp.
Salmonella spp., and Shigella spp.

OmphalitisOmphalotus oleariusNematodesUnknown[93]
Meloidogyne incognita and Caenorhabditis elegans

DaptomycinStreptomyces roseosporusBacteria staphylococci and enterococciBacterial cell membrane, causing rapid membrane depolarization and a potassium ion efflux, followed by the arrest of DNA, RNA, and protein synthesis, resulting in bacterial cell death[94, 95]

Pargamicin AAmycolatopsis sp.BacteriaDisruption of the membrane potential, leading to loss of the membrane function[94, 95]
S. aureus and E. faecalis

NocardithiocinNocardia pseudobrasiliensisBacteriaCell membrane or cell wall permeability[94, 96]
Mycobacterium
Gordonia species
M. tuberculosis

XylapeptideXylaria sp.BacteriaUnknown[94]
Bacillus subtilis
B. cereus, B. megaterium, and Micrococcus luteus
S. aureus and Shigella castellani
Fungus
C. albicans

LugduninStaphylococcus lugdunensisBacteriaImpairment of membrane integrity or ion transport and proton leakage in synthetic, protein-free membrane vesicles[94, 97, 98]
Staphylococcus aureus and vancomycin-resistant Enterococcus

VenturamideOscillatoria sp.ParasiteUnknown[94]
P. falciparum

Xenoamicin AXenorhabdus doucetiae and Xenorhabdus mauleoniiParasiteInteracts with the cytoplasmic membrane[94, 99]
P. falciparum
T. brucei rhodesiense

SzentiamideXenorhabdus szentirmaiiParasiteInteracts with the cytoplasmic membrane[99]
Plasmodium falciparum
Trypanosoma cruzi
Bacteria
M. luteus

ApicidinFusarium semitectumParasiteInhibit histone deacetylase of parasite[100, 101]
Plasmodium falciparum and T. gondii
Plasmodium berghei

ThiostreptonStreptomyces azureus and Streptomyces laurentiiParasiteInhibition of protein synthesis by proteasome β subunits and inhibition of mRNA translation[100]
Plasmodium berghei

AmphomycinStreptomyces canusParasiteInhibits the biosynthesis of the glycolipid precursor of glycosylphosphatidylinositol (GPI) protein by which the variant surface glycoproteins (VSGs) are anchored in the membrane of the parasites[100]
Trypanosoma brucei
T. b. gambiense
T. b. rhodesiense

Leucinostatins (A and B) and alamethicinPaecilomyces sppParasitePore formation in the membranes and interruption of cellular homeostasis, resulting in the death of the parasite[100]
Trypanosoma brucei
T. b. brucei and T. b. rhodesiense

Haloduracin (lantibiotic)Bacillus haloduransBacteriaPore formation, cell membrane attack, and the inhibition of cell wall synthesis[102]
B. anthracis
Vancomycin-resistant Enterococcus faecium, Bacillus cereus, and methicillin-resistant
Staphylococcus aureus

AlbicidinXanthomonas albilineansBacteriaInhibit DNA replication, transcription, supercoiling, gene regulation, and catalytic DNA cleavage-religation cycle of the GyrA subunit[103, 104]
Enterobacter aerogenes
Escherichia coli
Haemophilus influenza
Klebsiella pneumonia
Shigella sonnei and Staphylococcus aureus

GriselimycinStreptomyces griseusBacteriaInhibit nucleic acid biosynthesis by sliding clamp of DNA polymerase III[104, 105]
Mycobacterium tuberculosis

Colicin EEscherichia coliBacteriaInhibit nucleic acid biosynthesis by cleaving the targeted cell’s DNA or tRNA and digests the peptidoglycan precursors, leading to cell death pore formation in the inner membrane and degrade the internal molecular components[71, 104, 106, 107]
Shiga-toxin-producing E. coli
Enteroinvasive
E. coli and Shigella
Enterobacter
Klebsiella and Morganella
Salmonella, Shigella, and Yersinia

DudawalamidesMoorea producensParasiteUnknown[94]
P. falciparum, Trypanosoma cruzi, and Leishmania donovani

AmbobactinStreptomyces ambofaciensBacteriaTarget cytoplasmic membrane[94, 108]
Bacillus subtilis
Escherichia coli
Erwinia carotovora
Pseudomonas syringae
Fungi
Ralstonia solanacearum and Xanthomonas oryzae

TeixobactinEleftheria terraeBacteriaInhibits bacterial cell wall synthesis by binding to the precursor of peptidoglycan and teichoic acid[94]
S. aureus
Streptococcus pneumonia, M. tuberculosis, Clostridium difficile, and Bacillus anthracis

MaribasinsBacillus marinusFungiUnknown[109]
Alternaria solani, Fusarium oxysporum, Rhizoctonia solani, and Verticillium albo-atrum

ClavariopsinsClavariopsin aquaticaFungiInhibit the synthesis of fungal cell walls[91]
C. albicans, Aspergillus fumigatus, and A. niger

AnidulafunginAspergillus oryzaeFungiInhibition on β-(1,3)-glucan synthase[109]
Candida

GE81112Streptomyces sp.BacteriaInhibit bacterial protein synthesis machinery[110]
S. pneumoniae, E. faecalis, E. coli and B. subtilis, and S. pyogenes

Carmaphycin BSymploca sp.ParasiteTargets Plasmodium proteasome[96]
Plasmodium falciparum

Kakadumycin AStreptomyces sp.BacteriaBinding to DNA prevents RNA synthesis[111]
Bacillus anthracis
Enterococcus faecium, Staphylococcus simulans, and Staphylococcus aureus
S. pneumonia
Listeria monocytogenes
Parasite
Plasmodium falciparum

FengycinsBacillus subtilisFungiDisrupt the mitochondrial membrane potential, production of reactive oxygen species, and chromatin condensation in fungal hyphal cells resulting in hyphal cell death[112]
Magnaporthe grisea
Aspergillus niger
Mucor rouxii
Rhizopus stolonifer
Gibberella zeae and Fusarium graminearum
Sclerotinia sclerotiorum