Northeast Red Beans Produce a Thermostable and pH-Stable Defensin-Like Peptide with Potent Antifungal Activity

Chan, Yau Sang; Ng, Tzi Bun

doi:10.1007/s12013-012-9508-1

Cited by 35 publications

(26 citation statements)

References 41 publications

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“…Another study showed that an antimicrobial protein derived from Bacillus subtilis FB123, named BSAMP, was highly thermostable after treatment at 100°C; its antimicrobial activity did not change [23]. Northeast red beans produce thermostable and pH-stable defensin-like peptides that fully maintain their antimicrobial activity at temperatures as high as 100°C and at pH values ranging from 0 to 12 [24]. The apparent stability of these peptides following exposure to heat or different pH values could potentially be attributed to their ability to promote in vitro aggregation of the acidic phospholipid dimyristoylphosphatidylserine or interactions that result in a reduction to their cationic charges [25].…”

Section: Discussionmentioning

confidence: 99%

Study of the Antimicrobial Activity of Tilapia Piscidin 3 (TP3) and TP4 and Their Effects on Immune Functions in Hybrid Tilapia (Oreochromis spp.)

Pan

Tsai

et al. 2017

PLoS ONE

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To address the growing concern over antibiotic-resistant microbial infections in aquatic animals, we tested several promising alternative agents that have emerged as new drug candidates. Specifically, the tilapia piscidins are a group of peptides that possess antimicrobial, wound-healing, and antitumor functions. In this study, we focused on tilapia piscidin 3 (TP3) and TP4, which are peptides derived from Oreochromis niloticus, and investigated their inhibition of acute bacterial infections by infecting hybrid tilapia (Oreochromis spp.) with Vibrio vulnificus and evaluating the protective effects of pre-treating, co-treating, and post-treating fish with TP3 and TP4. In vivo experiments showed that co-treatment with V. vulnificus and TP3 (20 μg/fish) or TP4 (20 μg/fish) achieved 95.3% and 88.9% survival rates, respectively, after seven days. When we co-injected TP3 or TP4 and V. vulnificus into tilapia and then re-challenged the fish with V. vulnificus after 28 days, the tilapia exhibited survival rates of 35.6% and 42.2%, respectively. Pre-treatment with TP3 (30 μg/fish) or TP4 (20 μg/fish) for 30 minutes prior to V. vulnificus infection resulted in high survival rates of 28.9% and 37.8%, respectively, while post-treatment with TP3 (20 μg/fish or 30 μg/fish) or TP4 (20 μg/fish) 30 minutes after V. vulnificus infection yielded high survival rates of 33.3% and 48.9%. In summary, pre-treating, co-treating, and post-treating fish with TP3 or TP4 all effectively decreased the number of V. vulnificus bacteria and promoted significantly lower mortality rates in tilapia. The minimum inhibitory concentrations (MICs) of TP3 and TP4 that were effective for treating fish infected with V. vulnificus were 7.8 and 62.5 μg/ml, respectively, whereas the MICs of kanamycin and ampicillin were 31.2 and 3.91 μg/ml. The antimicrobial activity of these peptides was confirmed by transmission electron microscopy (TEM) and scanning electron microscopy (SEM), both of which showed that V. vulnificus disrupted the outer membranes of cells, resulting in the loss of cell shape and integrity. We examined whether TP3 and TP4 increased the membrane permeability of V. vulnificus by measuring the fluorescence resulting from the uptake of 1-N-phenyl-naphthylamine (NPN). Treating fish with TP3 and TP4 under different pH and temperature conditions did not significantly increase MIC values, suggesting that temperature and the acid-base environment do not affect AMP function. In addition, the qPCR results showed that TP3 and TP4 influence the expression of immune-responsive genes, including interleukin (IL)-1β, IL-6, and IL-8. In this study, we demonstrate that TP3 and TP4 show potential for development as drugs to combat fish bacterial infections in aquaculture.

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Section: Discussionmentioning

confidence: 99%

Study of the Antimicrobial Activity of Tilapia Piscidin 3 (TP3) and TP4 and Their Effects on Immune Functions in Hybrid Tilapia (Oreochromis spp.)

Pan

Tsai

et al. 2017

PLoS ONE

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“…Several other plant defensins with antifungal activity have also been studied. Specific information about some of those defensins can be found on the following references: Medicago sativa defensin 1 ( Ms Def1) and Medicago truncatula defensin 4 ( Mt Def4; Spelbrink et al, 2004; Ramamoorthy et al, 2007a,b; Sagaram et al, 2011); Dahlia merckii AMP 1 ( Dm AMP1; Thevissen et al, 1999, 2000a,b, 2003b; Jha et al, 2009; Salahinejad et al, 2013); Phaseolus vulgaris defensin 1 ( Pv D1; Games et al, 2008; Mello et al, 2011; Wu et al, 2011; Chan et al, 2012; Wong et al, 2012; Chan and Ng, 2013); Nicotiana alata defensin 1 ( Na D1; Lay et al, 2003, 2012; van der Weerden et al, 2008, 2010; Hayes et al, 2013). …”

Section: Recently Studied Antifungal Defensinsmentioning

confidence: 99%

Defensins: antifungal lessons from eukaryotes

Gonçalves²,

2014

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Over the last years, antimicrobial peptides (AMPs) have been the focus of intense research toward the finding of a viable alternative to current antifungal drugs. Defensins are one of the major families of AMPs and the most represented among all eukaryotic groups, providing an important first line of host defense against pathogenic microorganisms. Several of these cysteine-stabilized peptides present a relevant effect against fungi. Defensins are the AMPs with the broader distribution across all eukaryotic kingdoms, namely, Fungi, Plantae, and Animalia, and were recently shown to have an ancestor in a bacterial organism. As a part of the host defense, defensins act as an important vehicle of information between innate and adaptive immune system and have a role in immunomodulation. This multidimensionality represents a powerful host shield, hard for microorganisms to overcome using single approach resistance strategies. Pathogenic fungi resistance to conventional antimycotic drugs is becoming a major problem. Defensins, as other AMPs, have shown to be an effective alternative to the current antimycotic therapies, demonstrating potential as novel therapeutic agents or drug leads. In this review, we summarize the current knowledge on some eukaryotic defensins with antifungal action. An overview of the main targets in the fungal cell and the mechanism of action of these AMPs (namely, the selectivity for some fungal membrane components) are presented. Additionally, recent works on antifungal defensins structure, activity, and cytotoxicity are also reviewed.

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“…Research on common bean proteins have been focused on the antioxidant capacity of hydrolysates and their potential for ACE inhibition, metal chelation, and NF‐κB suppressor activity (Oseguera‐Toledo and others ; Carrasco‐Castilla and others ; Valdez‐Ortiz and others ; Rui and others ), antitumor activity (Chan and others ; Luna‐Vital and others , ), antihypertensive properties (Hernández‐Alvarez and others 2013; Rui and others ; Boschin and others ), antioxidant capacity (Valdez Ortiz and others ; Betancur‐Ancona and others 2014; Guzmán‐Méndez and others ); and antifungal activity (Wu and others ; Chan and others ; Wong and others ; Chan and Ng ). However, the novelty of this scientific research was to discover, for the 1st time, the biological potential of peptides from commercially precooked common bean hydrolysates on enzymes related to type‐2 diabetes as DPP‐IV as well as provide information about functional properties of commercially available processed products.…”

Section: Introductionmentioning

confidence: 99%

Impact of Commercial Precooking of Common Bean (Phaseolus vulgaris) on the Generation of Peptides, After Pepsin–Pancreatin Hydrolysis, Capable to Inhibit Dipeptidyl Peptidase‐IV

Mojica

Chen

Mejı́a

2014

Journal of Food Science

117

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The objective of this research was to determine the bioactive properties of the released peptides from commercially available precook common beans (Phaseolus vulgaris). Bioactive properties and peptide profiles were evaluated in protein hydrolysates of raw and commercially precooked common beans. Five varieties (Black, Pinto, Red, Navy, and Great Northern) were selected for protein extraction, protein and peptide molecular mass profiles, and peptide sequences. Potential bioactivities of hydrolysates, including antioxidant capacity and inhibition of α-amylase, α-glucosidase, dipeptidyl peptidase-IV (DPP-IV), and angiotensin converting enzyme I (ACE) were analyzed after digestion with pepsin/pancreatin. Hydrolysates from Navy beans were the most potent inhibitors of DPP-IV with no statistical differences between precooked and raw (IC50 = 0.093 and 0.095 mg protein/mL, respectively). α-Amylase inhibition was higher for raw Red, Navy and Great Northern beans (36%, 31%, 27% relative to acarbose (rel ac)/mg protein, respectively). α-Glucosidase inhibition among all bean hydrolysates did not show significant differences; however, inhibition values were above 40% rel ac/mg protein. IC50 values for ACE were not significantly different among all bean hydrolysates (range 0.20 to 0.34 mg protein/mL), except for Red bean that presented higher IC50 values. Peptide molecular mass profile ranged from 500 to 3000 Da. A total of 11 and 17 biologically active peptide sequences were identified in raw and precooked beans, respectively. Peptide sequences YAGGS and YAAGS from raw Great Northern and precooked Pinto showed similar amino acid sequences and same potential ACE inhibition activity. Processing did not affect the bioactive properties of released peptides from precooked beans. Commercially precooked beans could contribute to the intake of bioactive peptides and promote health.

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Northeast Red Beans Produce a Thermostable and pH-Stable Defensin-Like Peptide with Potent Antifungal Activity

Cited by 35 publications

References 41 publications

Study of the Antimicrobial Activity of Tilapia Piscidin 3 (TP3) and TP4 and Their Effects on Immune Functions in Hybrid Tilapia (Oreochromis spp.)

Study of the Antimicrobial Activity of Tilapia Piscidin 3 (TP3) and TP4 and Their Effects on Immune Functions in Hybrid Tilapia (Oreochromis spp.)

Defensins: antifungal lessons from eukaryotes

Impact of Commercial Precooking of Common Bean (Phaseolus vulgaris) on the Generation of Peptides, After Pepsin–Pancreatin Hydrolysis, Capable to Inhibit Dipeptidyl Peptidase‐IV

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