Viper metalloproteinase (<i>Agkistrodon halys</i> pallas) with antimicrobial activity against multi‐drug resistant human pathogens

Samy, Ramar Perumal; Gopalakrishnakone, P.; Chow, Vincent T. K.; Ho, Bow

doi:10.1002/jcp.21373

Cited by 26 publications

(24 citation statements)

References 43 publications

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“…Minimum Inhibitory Concentrations (MICs) of CaTx-II against different bacteria were determined by the MH and TS broth dilution method [31]. A single bacterial colony was used to inoculate each MH and TS broth (5 ml/tube) subsequently incubated at 37°C for 6–8 h (exponential-phase cells) before adjusting with sterile medium to a 0.5 McFarland turbidity standard.…”

Section: Methodsmentioning

confidence: 99%

Wound Healing Activity and Mechanisms of Action of an Antibacterial Protein from the Venom of the Eastern Diamondback Rattlesnake (Crotalus adamanteus)

et al. 2014

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Basic phospholipase A2 was identified from the venom of the eastern diamondback rattlesnake. The Crotalus adamanteus toxin-II (CaTx-II) induced bactericidal effects (7.8 µg/ml) on Staphylococcus aureus, while on Burkholderia pseudomallei (KHW), and Enterobacter aerogenes were killed at 15.6 µg/ml. CaTx-II caused pore formation and membrane damaging effects on the bacterial cell wall. CaTx-II was not cytotoxic on lung (MRC-5), skin fibroblast (HEPK) cells and in mice. CaTx-II-treated mice showed significant wound closure and complete healing by 16 days as compared to untreated controls (**P<0.01). Histological examination revealed enhanced collagen synthesis and neovascularization after treatment with CaTx-II versus 2% Fusidic Acid ointment (FAO) treated controls. Measurement of tissue cytokines revealed that interleukin-1 beta (IL-1β) expression in CaTx-II treated mice was significantly suppressed versus untreated controls. In contrast, cytokines involved in wound healing and cell migration i.e., monocyte chemotactic protein-1 (MCP-1), fibroblast growth factor-basic (FGF-b), chemokine (KC), granulocyte-macrophage colony-stimulating factor (GM-CSF) were significantly enhanced in CaTx-II treated mice, but not in the controls. CaTx-II also modulated nuclear factor-kappa B (NF-κB) activation during skin wound healing. The CaTx-II protein highlights distinct snake proteins as a potential source of novel antimicrobial agents with significant therapeutic application for bacterial skin infections.

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Section: Methodsmentioning

confidence: 99%

Wound Healing Activity and Mechanisms of Action of an Antibacterial Protein from the Venom of the Eastern Diamondback Rattlesnake (Crotalus adamanteus)

et al. 2014

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“…The CP-F1 fraction was further separated by a C8 column (Jupitor Phenomex) in 0.1% aqueous trifluoroacetic acid (TFA) (Sigma Co, USA), and eluted with a linear gradient of 80% acetonitrile (ACN) in 0.1% TFA. These fractions were monitored at 215 nm [62], [63]. Total protein in the entire above fractions was estimated using the Bradford [64] reagent (Bio-Rad, Hercules, CA, USA) before immediate processing or storage at −80°C.…”

Section: Methodsmentioning

confidence: 99%

Identification of a Novel Calotropis procera Protein That Can Suppress Tumor Growth in Breast Cancer through the Suppression of NF-κB Pathway

Samy

Rajendran

et al. 2012

PLoS ONE

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Breast cancer is the most common cancer among women. To date, improvements in hormonal and cytotoxic therapies have not yet led to a sustained remission or cure. In the present study, we investigated the in vitro and in vivo antitumor activities of a novel Calotropis procera protein (CP-P) isolated from root bark. CP-P protein inhibited the proliferation and induced apoptosis of breast cancer cells through the suppression of nuclear factor kappaB (NF-kB) activation. CP-P, when administered individually or in combination with cyclophosphamide (CYC, 0.2 mg/kg) to rats with 7, 12-dimethyl benz(a)anthracene (DMBA)-induced breast cancer decreased tumor volume significantly without affecting the body weight. To elucidate the anticancer mechanism of CP-P, antioxidant activities such as superoxide dismutase (SOD), catalase (CAT), glutathione-s-transferase (GST) and non-enzymatic antioxidant - reduced glutathione (GSH), vitamin E and C generation in the breast were analyzed by various assays. SOD, CAT, GST, GSH, vitamin E and C levels were high in combination-treated groups (CP-P+CYC) versus the CYC alone-treated groups. Also, the combination was more effective in down-regulating the expression of NF-kB-regulated gene products (cyclin D1 and Bcl-2) in breast tumor tissues. Our findings indicate that CP-P possesses significant antitumor activity comparable to a commonly used anticancer drug, cyclophosphamide, and may form the basis of a novel therapy for breast cancer.

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“…AHM variants with high bacteriostatic activity (Minimum Inhibitory Concentration or MIC = 2 -60 M) also tended to be less cytotoxic against U-937 human monocytic cells up to 1 mM concentrations. [76]. Crotamine inhibits several strains of E. coli with MICs of 25-100 g/ml, and it kills through membrane permeablilization [77].…”

Section: Antimicrobial Effects Of Snake Venom Pla 2 Smentioning

confidence: 99%

Snake Venom Phospholipases A2: A Novel Tool Against Bacterial Diseases

Samy¹,

Gopalakrishnakone²,

Stiles³

et al. 2012

Current Medicinal Chemistry

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The majority of snake venom phospholipases A(2) (svPLA(2)s) are toxic and induce a wide spectrum of biological effects. They are cysteine-rich proteins that contain 119-134 amino acids and share similar structures and functions. About 50% of the residues are incorporated into α-helices, whereas only 10% are in β-sheets. Fourteen conserved cysteines form a network of seven disulfide bridges that stabilize the tertiary structure. They show a high degree of sequence and structural similarity, and are believed to have a common calcium- dependent catalytic mechanism. Additionally, svPLA(2)s display an array of biological actions that are either dependent or independent of catalysis. The PLA(2)s of mammalian origin also exert potent bactericidal activity by binding to anionic surfaces and enzymatic degradation of phospholipids in the target membranes, preferentially of Gram-positive species. The bactericidal activity against Gram-negatives by svPLA(2) requires a synergistic action with bactericidal/permeability-increasing protein (BPI), but is equally dependent on enzymatic- based membrane degradation. Several hypotheses account for the bactericidal properties of svPLA(2)s, which include "fatal depolarization" of the bacterial membrane, creation of physical holes in the membrane, scrambling of normal distribution of lipids between the bilayer leaflets, and damage of critical intracellular targets after internalization of the peptide. The present review discusses several svPLA(2)s and derived peptides that exhibit strong bactericidal activity. The reports demonstrate that svPLA(2)-derived peptides have the potential to counteract microbial infections. In fact, the C-terminal cationic/hydrophobic segment (residues 115-129) of svPLA(2)s is bactericidal. Thus identification of the bactericidal sites in svPLA(2)s has potential for developing novel antimicrobials.

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Viper metalloproteinase (Agkistrodon halys pallas) with antimicrobial activity against multi‐drug resistant human pathogens

Cited by 26 publications

References 43 publications

Wound Healing Activity and Mechanisms of Action of an Antibacterial Protein from the Venom of the Eastern Diamondback Rattlesnake (Crotalus adamanteus)

Wound Healing Activity and Mechanisms of Action of an Antibacterial Protein from the Venom of the Eastern Diamondback Rattlesnake (Crotalus adamanteus)

Identification of a Novel Calotropis procera Protein That Can Suppress Tumor Growth in Breast Cancer through the Suppression of NF-κB Pathway

Snake Venom Phospholipases A2: A Novel Tool Against Bacterial Diseases

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