International Journal of Microbiology

Review Article

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

Table 1

Plant-derived bioactive peptides and their potential antimicrobial applications.


Name of the peptide	Plant source	Target pathogen	Mode of action	References

Thionins	Wheat, barley, oats, rice, rye, mistletoe, oil nut, and Abyssinian cabbage	Bacteria	Pore formation, ion channel formation, cell membrane disruption, and protein synthesis inhibition	[13]
		Gram-positive or Gram-negative bacteria such as Pseudomonas, Xanthomonas, Agrobacterium, Erwinia, and Corynebacterium

Purothionin	Wheat	Bacteria	Interfere with DNA synthesis by inhibiting the activity of the enzyme ribonucleotide reductase, and also inhibit the activity of β-glucuronidase	[13, 16]
		Pseudomonas solanacearum, Xanthomonas phaseoli, Xanthomonas campestris, Erwinia amylovora, Corynebacterium flaccumfaciens, Corynebacterium michiganense, Corynebacterium poinsettiae, Corynebacterium sepedonicum, and Corynebacterium fascians

WAMP_1a and WAMP_1b	Seeds of T. kiharae	Fungi	Growth inhibition and induced destruction	[17, 18]
		Fusarium solani, Fusarium oxysporum, and Helminthosporium sativum
		Bacteria
		Gram-positive
		Clavibacter michiganense, Gram-negative
		Pseudomonas syringae
		Erwinia carotovora

Lc-Def	Lentil	Fungi	Electrostatic interaction with anionic lipid components of fungal membranes	[18]
		Aspergillus niger, Aspergillus versicolor, Botrytis cinerea, Fusarium culmorum, Fusarium solani, and Neurospora crassa

AFP-J	Potato tuber (Solanum tuberosum cv. L Jopung)	Fungi	Inhibit serine protease activity	[12, 19]
		Trichosporon beigelii, S. cerevisiae, and Candida albicans
		Bacteria
		Staphylococcus aureus, Listeria monocytogenes, and Escherichia coli

Potide-G	Potato tubers	Bacteria	Suppressed proteolytic activity of trypsin, chymotrypsin, and papain	[12]
		Staphylococcus aureus, Listeria monocytogenes, Escherichia coli, and Clavibacter michiganensis subsp. michiganense
		Fungi
		C. albicans and R. solani
		Virus Potato virus Y

PKPI and PPI-I	Potato sprout	Fungi	Inhibit fungal protease, spore germination, hyphal elongation, and the development of necrotic lesions	[12]
		Botrytis cinerea

Potato pseudothionin solanum tuberosum 1 (Pth-St1)	Potato tubers	Bacteria	Bind to the membrane receptor, chelation of Ca²⁺, and consequently, pores are being formed	[12, 20, 21]
		Clavibacter michiganensis and Pseudomonas solanacearum
		Fungi
		F. solani

PKI1 and PPI3B2	Potato	Fungi	Fungal proteases affect spore germination, hyphal elongation, and development of necrotic lesions	[22]
		Botrytis cinerea

PLPKI	Potato	Phytophthora infestans and Rhizoctonia solani	Inhibited the activity of extracellular proteases	[23]

PSPI-21 and PKSI	Potato tubers	Fungi	Serine proteinases inhibitor (affect the growth of oomycete mycelium and fungal mycelium) induces complete destruction of oomycete zoospores and partial destruction of fungal macroconidia	[24]
		Phytophthora infestans and Fusarium culmorum

Snakins (SN1 and SN2)	Potato	Bacteria	Rapid aggregation of both Gram-positive and Gram-negative bacteria	[12, 25]
		C. michiganensis subsp. Sepedonicus, Ralstonia solanacearum, and R. meliloti
		Fungi
		B. cinerea, Fusarium oxysporum f. sp. Conglutinans, F. solani, Bipolaris maydis, Aspergillus flavus, and Colletotrichum graminicola

2S albumin-like protease inhibitor	Barley seeds	Fungi	Permeabilize fungal membranes	[19, 26]
		Alternaria brassicicola, Botrytis cinerea, Fusarium culmorum, Fusarium oxysporum f.sp. lycopersici, Pyricularia oryzae, and Verticillium dahlia

Trypsin and chymotrypsin inhibitors	Cabbage leaves	Fungi	Blocked the synthesis of chitin in the cell wall, and weakened the fungal hyphae, thus inducing the leakage of intracellular contents from susceptible fungal species	[19, 27]
		Botrytis cinerea and Fusarium solani

ZmESR-6	Kernels of maize	Bacteria	Inhibit protein synthesis and block ion channels	[28, 29]
		Clavibacter Michiganensis, Xanthomonas campestris, and Rhizobium meliloti
		Fungi
		Fusarium oxysporum f.sp. Conglutinans, Fusarium oxysporum f.sp.lycopersici, and Plectosphaerella cucumerina

Fabatin	Broad bean	Bacteria	Insertion into the plasma membranes of bacterial cells, leading to depolarization of the membrane and cell lysis	[29–31]
		Escherichia coli, Enterococcus hirae, and Pseudomonas aeruginosa

VaD1	Azuki bean	Bacteria	Inhibit protein synthesis	[29, 32]
		Staphylococcus epidermis, Xanthomonas campestris pv. vesicatoria, and Salmonella typhimurium
		Fungi
		Fusarium oxysporum, Fusarium oxysporum, and Trichophyton rubrum
So-D2 and So-D7	Spinach	Bacteria	Damage the cell wall via repression of gene expression or via restricting bacterial replication, causing cell lysis	[29, 33]
		Clavibacter sepedonicus and Ralstonia solanacearum

Tu-AMP1 and Tu-AMP2	Tulipa gesneriana	Bacteria	Positively charged proteins interact with negatively charged membrane phospholipids, following a membrane permeability modification	[21, 29]
		Erwinia carotovora subsp. Carotovora, A. tumefaciens, Clavibacter michiganensis, and Curtobacterium flaccumfaciens pv. oortii

Pp-AMP 1 and Pp- AMP 2	Japanese bamboo shoots	Bacteria	Binds to specific phospholipids and cause the exposure of toxicity, resulting in cationic imbalance	[21]
		E. carotovora, A. radiobacter, A. rhizogenes, C. michiganensis, and C. flaccumfaciens

MtDef5	Medicago truncatula	Bacteria	Permeabilizes the plasma membrane, translocates into the cells of this bacterial pathogen and binds to DNA, membrane permeabilization, and fungal growth arrest	[29, 34]
		Xanthomonas campestris pv. Campestris
		Fungi
		Fusarium graminearum and Neurospora crassa

Tad1	Winter wheat	Pseudomonas cichorii	Unknown	[29]

OsDef7 and OsDef8	Rice Oryza sativa	Bacteria	Interact with the negatively charged phospholipids on the bacterial membrane surface and fungal membrane destabilization	[29, 35]
		Xanthomonas oryzae, pv. oryzae, X. oryzae pv. oryzicola, Erwinia carotovora subsp. atroseptica, Pseudomonas aeruginosa, and Dickeya dadantii
		Fungi
		Helminthosporium oryzae and Fusarium oxysporum f.sp. cubense

PvD1	Seeds	Fungi	Oxidative damage related to the induction of ROS and NO production, cytoplasmic fragmentation, formation of multiple cytoplasmic vacuoles, and membrane permeabilization in the cells of this organism	[36, 37]
		C. albicans
		Protozoa
		Leishmania amazonensis

Limenin	Phaseolus limensis	Bacteria	Membrane collapse by interacting with lipid molecules on the bacterial cell surface, inhibiting the translation of fungi. HIV-1 reverse transcriptase inhibition	[29, 38, 39]
		Mycobacterium phlei, Proteus vulgaris, Bacillus megaterium, and Bacillus subtilis
		Fungi
		Botrytis cinerea, Fusarium oxysporum, and Mycosphaerella arachidicola
		Virus
		HIV-1

Ct-AMP1	Clitoria ternatea	Fungi	Cause a reduction in hyphal thickness and an apparent collapse of the plasma membrane leading to an apparent fragmentation of the cytoplasm	[29, 40]
		Botrytis cinerea, Cladosporium sphaerospermum, Fusarium culmorum Leptosphaeria maculans, Penicillium digitatum, Trichoderma viride, Septoria tritici, and Verticillium albo-atrum

J1-1	Capsicum annuum	Bacteria	Binds with phosphoinositides (PIs) and PA	[29]
		Pseudomonas aeruginosa
		Fungi
		Fusarium oxysporum and Botrytis cinerea

MsDef1	M. sativa	Fungi	Ion channel blocking and hyperbranching	[41]
		F. graminearum

HaDEF1	Sunflower	Fungi	Membrane permeabilization and apoptosis	[41]
		O. Cumana, O. Ramosa, S. cerevisiae, and A. brassicicola

Fa-AMP1 and Fa-AMP2	Buckwheat seeds	Bacteria	Disruption of microbial membranes and phospholipid liposomes, an interaction with a specific receptor as an ion channel or a sphingolipid	[21, 29]
		Erwinia carotovora subsp. carotovora, Agrobacterium tumefaciens, Clavibacter michiganensis, and Curtobacterium flaccumfaciens pv. oortii
		Fungi
		Fusarium oxysporum and Geotrichum candidum

α-Hordothionins	Barley	Bacteria	Interacting electrically with fungal lipid bilayer and linking to the membrane surface, leading to permeabilization and disruption of the membrane organization	[21, 42]
		Clavibacter michiganensis subsp. michiganensis and Xanthomonas campestris pv. vesicatoria

Pa-AMP-1	Pokeweed seeds	Fungi	Interact with the phospholipids of cell membranes, resulting in the inhibition of fungal growth	[42, 43]
		Alternaria panax and Fusarium sp., Rhizoctonia solani

Cp-thionin II (γ-thionins)	Cowpea seeds	Bacteria	Insertion into the plasma membranes of bacterial cells, leading to depolarization of the membrane, cell lysis, and permeabilization of the hyphae, leading to leakage and granulation of the plasma membrane, and increased generation of reactive oxygen species (ROS) causes fungal growth inhibition	[29, 30, 44]
		Pseudomonas syringae, Staphylococcus aureus, and Escherichia coli
		Fungi
		F. culmorum

Dm-AMP1	Dahlia merckii	Fungi	Causes a reduction in hyphal thickness and an apparent collapse of the plasma membrane leading to an apparent fragmentation of the cytoplasm	[29, 40]
		Botrytis cinerea, Cladosporium sphaerospermum, Fusarium culmorum Leptosphaeria maculans, Penicillium digitatum Trichoderma viride, Septoria tritici Verticillium albo-atrum

Hs-AFP1	Heuchera sanguinea	Fungi	Causes germ tubes and hyphae to swell and form multiple hyphal buds, membrane permeabilization, ROS, and apoptosis	[40, 41]
		Botrytis cinerea, Cladosporium sphaerospermum, Fusarium culmorum, Leptosphaeria maculans, C. albicans, C. krusei, A.flavus, Penicillium digitatum, Trichoderma viride, Septoria tritiei, and Verticillium albo-atrum

Rs-AFP2	Radishes	Fungi	Causes germ tubes and hyphae to swell and form multiple hyphal buds, membrane permeabilization, ROS, apoptosis, inhibit cell growth, and ion flux	[40, 41]
		Botrytis cinerea Cladosporium sphaerospermum, Fusarium culmorum Neurospora crassa Leptosphaeria maculans, Penicillium digitatum Trichoderma viride Septoria tritici Verticillium albo-atrum

Hc-AFP	Heliophila coronopifolia	Fungi	Hyperbranching, fungal tip swelling, increased granulation of hyphae and spores, as well as hyphal and spore, and membrane permeabilization disruption	[41]
		Botrytis cinerea
		Fusarium solani

Ah-AMP1	Horse chestnut	Fungi	Reducing hyphal thickness and collapse of the plasma membrane causes an apparent fragmentation of the cytoplasm	[29, 40]
		Botrytis cinerea, Cladosporium sphaerospermum, Fusarium culmorum, Leptosphaeria maculans, Penicillium digitatum Trichoderma viride Septoria tritici, and Verticillium albo-atrum

NaD1 γ-thionin-like protein	Nicotiana alata	Fungi	Interacting with the cell wall causes the destruction of internal membrane integrity by membrane permeabilization and targets internal organelles by inducing the development of reactive oxygen species (ROS) and fungal cell death	[37, 41, 45]
		Leptosphaeria maculans, V. dahlia, Thielaviopsis basicola, Aspergillus nidulans, C. albicans, C. neoformans, C. gattii, and Fusarium oxysporum

BCP-2 alpha thionin	Barley grain	Fungi	Bind to glucosylceramides and sphingolipids, leading to fungal cell lysis	[21, 44, 46]
		Botrytis cinerea
		Trichoderma viride

Mo-CBP₂ (chitin-binding protein)	Seeds	Fungi	Increased the cell membrane permeabilization and produce reactive oxygen species, have DNase activity	[47]
		Candida albicans, C. parapsilosis, C. krusei, and C. tropicalis

Mo-CBP₃	Seeds	Fungi	Inhibited spore germination and mycelial growth induced the production of ROS and caused disorganization of both the cytoplasm and the plasma membrane leading to cell death	[48]
		Fusarium solani, F. oxysporum, Colletotrichum musae, and C. gloeosporioides

Cy-AMP1	Cycad seeds	Fungi	Bind to chitin of fungus surface	[49, 50]
		F. oxysporum
		G. candidum

Lunatusin	Chinese lima bean	Bacteria	Causes membrane collapse by interacting with lipid molecules on the bacterial cell surface, inhibits mycelial growth of fungi, and inhibits HIV-1 reverse transcriptase protein-protein inhibition	[16, 38, 49]
		Bacillus megaterium, B. subtilis, P. vulgaris, and Mycobacterium phlei
		Fungi
		Fusarium oxysporum, Mycosphaerella arachidicola, and Botrytis cinerea
		Virus
		HIV-1

Vulgarinin	Haricot beans	Bacteria	Cell membrane disruption, growth inhibition, and death of bacteria, interaction with phosphorylinositol containing sphingolipids or glycosylceramides cause subsequent fungal cell death, and inhibit HIV-1 reverse transcriptase, protease, and integrase	[16, 38, 51]
		Mycobacterium phlei, Bacillus megaterium, B. subtilis, P. vulgaris
		Fungi
		Botrytis cinerea, Fusarium oxysporum, Physalospora piricola, and Mycosphaerella arachidicola
		Virus
		HIV-1

Hispidalin	Benincasa hispida	Bacteria	Amphipathicity and cationic charge of peptide facilitates the peptide attachment and insertion into the bacterial membrane to create transmembrane pores resulting in membrane permeabilization. Fungal hyphae growth inhibition	[16, 52]
		S. enterica, S. aureus, E. coli, and P. aeruginosa
		Fungi
		A. flavus, F. solani, C. geniculate, and P. chrysogenum

(Cg24-I)	Carica candamarcensis, C. papaya, and Cryptostegia grandiflora	Fungi	Inhibition of mycelia growth and spore germination	[16, 53]
		F. solani, R. solani, and F. oxysporum

CpLP cysteine-like proteases	Calotropis procera	Fungi	Fungal growth inhibition, production of ROS lead to oxidative stress, loss of cell function, and ultimately cell death by apoptosis or necrosis	[54]
		Colletotrichum gloeosporioides, Fusarium oxysporum, Fusarium solani, Rhizoctonia solani, Neurospora sp., and Aspergillus Niger

IbAMP1 plant defensin	Seeds	Bacteria	Increase permeability to the cell membrane, permitting efflux of ATP and interfering with intracellular molecular processes (DNA, RNA, and protein synthesis)	[55, 56]
		E. coli O157: H7 and Staphylococcus aureus

WAMPs (hevein-like AMPs)	Wheat	Fungi	Cell wall/membrane disruption, the peptide penetrates through the fungal cell walls and interferes with fungal growth by binding or cross-linking the newly-synthesized chitin chains, penetrating into the fungal hyphae and localized at the septum and hyphal tips, resulting in hyphal tip burst and leakage of the cytoplasmic constituents. Active against fungal metalloproteases	[57, 58]
		C. cucumerinum, A. alternata F. oxysporum, and B. sorokiniana

AX (cysteine-rich proteins)	Sugar beet leaves	Fungi	Reduction of hyphal growth	[59]
		C. beticola

Ay-AMP	Amaranthus hypochondriacus seeds	Fungi	Degrades chitin of the fungal cell walls and accumulates at septa and hyphal tips by the union to the fungus cell wall chitin, inhibiting the growth	[60]
		Candida albicans, Trichoderma sp., Fusarium solani, Penicillium chrysogenum, Geotrichum candidum, Aspergillus candidus, Aspergillus. ochraceus, and Alternaria alternata

Pn-AMPs (hevein-type)	Seeds of morning glory	Fungi	Penetrated very rapidly into fungal hyphae and localized at septum and hyphal tips of fungi, which caused the burst of hyphal tips. The burst of hyphae resulted in disruption of the fungal membrane and leakage of the cytoplasmic materials	[61]
		Botrytis cinerea, Phytophthora parasitica, Fusarium oxysporum, Rhizoctonia solani, and Saccharomyces cerevisiae

GAFP (hevein-type)	Ginkgo biloba	Fungi	Burst of hyphal tips increased hyphal membrane permeabilization	[7]
		Fusarium graminearum, Fusarium moniliforme, Pellicularia sasakii Ito, and Alternaria alternata

Ns-D1 and Ns-D2	Nigella sativa seeds	Fungi	Inhibited hyphal growth	[7, 62]
		Aspergillus niger, Fusarium oxysporum, Fusarium graminearum, Fusarium culmorum, Bipolaris sorokiniana, and Botrytis cinerea

PINA and PINB (puroindoline)	Wheat	Fungi	Interactions with cellular membranes and ion channel formation in the membranes	[7]
		Alternaria brassicicola, Ascochyta pisi, Botrytis cinerea, Verticillium dahliae, Fusarium culmorum, and Cochliobolus heterostrophus

Ha-AP10 (lipid transfer proteins)	Sunflower seeds (Helianthus annuus)	Fungi	Membrane permeabilization by electrostatic interaction with anionic membrane phospholipids induces liposome leakage and permeabilization of fungal spores	[55, 63]
		Fusarium solani

WjAMP1 (hevein-like AMPs)	Leaves of Wasabia japonica L.	Bacteria	Peptide binding to the membrane can activate several pathways that will cause cell death	[7, 38, 64]
		Escherichia coli
		Agrobacterium tumefaciens
		Pseudomonas cichorii
		P. plantarii
		P. glumae
		Fungi	Inhibit spore germination and hyphal growth, interaction with fungal membrane lipids resulting in the formation of membrane pores, and leakage of cytoplasmic materials
		Botrytis cinerea
		Fusarium solani
		Magnaporthe grisea
		Alternaria alternata

LTP protein (lipid transfer proteins)	Wheat	Fungi	Fungal membranes form a pore resulting in an efflux of intracellular ions culminating in cell death	[7]
		Rhizoctonia solani
		Curvularia lunata
		Alternaria sp.
		Bipolaris oryzae
		Cylindrocladium
		Scoparium
		Botrytis cinerea
		Sarocladium oryzae

Kalata B (cyclotide)	Oldenlandia affinis	Bacteria	Induces leakage of contents from phospholipid vesicles and forms large pores in lipid bilayers, has lytic ability causing membrane leakage of helminth, and inhibits the development of nematode larvae and motility of adult worms	[7, 65]
		Staphylococcus aureus
		E. coli
		Nematode
		Haemonchus contortus
		Trichostrongylus colubriformis

Shepherins (glycine- and histidine-rich peptides)	Capsella bursa-pastoris	Bacteria	Insertion into the membrane, triggering disruption of lipid bilayer physical integrity, membrane thinning/formation of transient pores, and destabilization of internal membranes, leading to disruption of the endosome	[66, 67]
		Erwinia herbicola, Escherichia coli, and Pseudomonas putida
		Fungi
		S. cerevisiae
		C. albicans
		Cryptococcus neoformans