Viperatoxin‐II: A novel viper venom protein as an effective bactericidal agent

Samy, Ramar Perumal; Stiles, Bradley G.; Chinnathambi, Arunachalam; Zayed, Mohamed E.; Alharbi, Sulaiman Ali; Franco, Octávio L.; Rowan, Edward G.; Kumar, Alan Prem; Lim, Lina H.K.; Sethi, Gautam

doi:10.1016/j.fob.2015.10.004

Cited by 23 publications

(14 citation statements)

References 64 publications

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“…The bacterial infection especially antibiotic-resistant strains are of the top leading causes of death worldwide (7). Several studies described the antimicrobial effect of snake venoms (19). In the present study, the antibacterial activity of Cerastes cerastes crude venom against the selective bacterial strains was evaluated by disc diffusion technique, the venom was effective against Gram-positive bacteria Staphylococcus aureus and Gram-negative bacteria Salmonella typhimurium.…”

Section: Histopathological Resultsmentioning

confidence: 83%

In vitro antibacterial and bio-histological effects of cerastes cerastes venom on albino mice

Shabaan

Feky

Latif

et al. 2018

Biochemistry Letters

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Background: Snake venoms contain mixtures of proteins that have different pathological and pharmaceutical effects. In the present study, we evaluated, in vitro the anti-bacterial activity of Cerastes cerastes (C. cerastes) crude venom. Results revealed it has broad antibacterial activity against S. typhimurium and S. aureus, and resistant to E. coli. In vivo, we analyzed the biochemical and histological effects of the sublethal dose of the venom. 45 Swiss albino mice were divided into 3 groups (15 mice/ group): control group; 1/10 LD50 group and 1/2 LD 50 group. Mice were dissected 48 hours after the injection and blood were collected. CBC, ALT, AST, urea, creatinine, total CPK, and LDH were measured. Histopathological changes induced by the venom in skin, liver, heart and kidney tissues were examined. A significant increase in RBCs in 1/10 LD50 group, while a significant decrease of which in 1/2 LD 50 group was observed. Thrombocytopenia, Leukocytosis and highly significant increase in monocytes were observed in both treated groups during the study. A significant increase was observed for lymphocytes and neutrophils in 1/2 LD 50 group. Serum levels of AST, ALT, urea, creatinine, total CPK and LDH were highly increased in both envenomed groups. The histopathological changes in liver, heart, skin and kidney tissues indicated that venom has hemotoxic effect in mice.

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Section: Histopathological Resultsmentioning

confidence: 83%

In vitro antibacterial and bio-histological effects of cerastes cerastes venom on albino mice

Shabaan

Feky

Latif

et al. 2018

Biochemistry Letters

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“…The antibacterial mechanism of many bioactive peptides involves pores formation and cell membrane damage of bacteria (Ramar Perumal Samy et al., ), enhancement of membrane permeability (Santamaria et al., ), inhibiting the synthesis of cell‐wall, nucleic‐acid, and protein (Brogden, ), effective interaction with lipopolysaccharides (LPS) on the cell membranes of bacteria (Santamaría et al., ), and suppression of NF‐κB activation which regulates malignant growth factor TGF‐β1 (Samy et al., ). The formation of pores and damage of cell membrane mainly involves the combination of hydrophobic peptides into the acidic lipid membrane of bacteria (Chandra et al., ), and it is also worth mentioning that corn protein are rich in hydrophobic amino acids, such as Leu, Ile, and Ala (Li et al., ).…”

Section: Biological Activities and Corresponding Mechanisms Of Bioactmentioning

confidence: 99%

A Comprehensive Review of Corn Protein‐derived Bioactive Peptides: Production, Characterization, Bioactivities, and Transport Pathways

Zhu

Hou

2018

Comp Rev Food Sci Food Safe

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Bioactive peptides are specific peptide fragments that positively exert various functional and biological activities and ultimately influence health. Corn protein are potential precursor proteins for bioactive peptides. This review encompasses the studies reported to date on the production, isolation, purification, and characterization technologies of bioactive corn peptides (CPs), with particular attention being devoted to these peptides’ different health effects, including antioxidant, antihypertensive, hepatoprotective, alcohol‐metabolism‐facilitating, anti‐inflammatory, anticancer, antimicrobial, and dipeptidyl peptidase IV (DPP‐IV) inhibitory activities. The review also describes studies examining the potential mechanisms believed to be involved in these bioactivities, and the possible absorption and transport pathways of CPs are summarized.

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“…Among these, snake venoms have shown promising antimicrobial activities on different pathogens, such as bacteria, fungi and protozoa [11][12][13]. Of the proteins found in these venoms, phospholipases A 2 (PLA 2 s) represent one of the main classes of molecules responsible for such activities [12,[14][15][16].…”

mentioning

confidence: 99%

Identification of the Molecular Determinants of the Antibacterial Activity of LmutTX, a Lys49 Phospholipase A₂ Homologue Isolated from Lachesis muta muta Snake Venom (Linnaeus, 1766)

Diniz-Sousa

Caldeira

Kayano

et al. 2017

Basic Clin Pharma Tox

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Snake venom phospholipases A (PLA s) are responsible for numerous pathophysiological effects in snakebites; however, their biochemical properties favour antimicrobial actions against different pathogens, thus constituting a true source of potential microbicidal agents. This study describes the isolation of a Lys49 PLA homologue from Lachesis muta muta venom using two chromatographic steps: size exclusion and reverse phase. The protein showed a molecular mass of 13,889 Da and was devoid of phospholipase activity on an artificial substrate. The primary structure made it possible to identify an unpublished protein from L. m. muta venom, named LmutTX, that presented high identity with other Lys49 PLA s from bothropic venoms. Synthetic peptides designed from LmutTX were evaluated for their cytotoxic and antimicrobial activities. LmutTX was cytotoxic against C2C12 myotubes at concentrations of at least 200 μg/mL, whereas the peptides showed a low cytolytic effect. LmutTX showed antibacterial activity against Gram-positive and Gram-negative bacteria; however, S. aureusATCC 29213 and MRSA strains were more sensitive to the toxin's action. Synthetic peptides were tested on S. aureus, MRSA and P. aeruginosaATCC 27853 strains, showing promising results. This study describes for the first time the isolation of a Lys49 PLA from Lachesis snake venom and shows that peptides from specific regions of the sequence may constitute new sources of molecules with biotechnological potential.

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Viperatoxin‐II: A novel viper venom protein as an effective bactericidal agent

Abstract: Graphical abstract

Cited by 23 publications

References 64 publications

In vitro antibacterial and bio-histological effects of cerastes cerastes venom on albino mice

In vitro antibacterial and bio-histological effects of cerastes cerastes venom on albino mice

A Comprehensive Review of Corn Protein‐derived Bioactive Peptides: Production, Characterization, Bioactivities, and Transport Pathways

Identification of the Molecular Determinants of the Antibacterial Activity of LmutTX, a Lys49 Phospholipase A₂ Homologue Isolated from Lachesis muta muta Snake Venom (Linnaeus, 1766)

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Viperatoxin‐II: A novel viper venom protein as an effective bactericidal agent

Abstract: Graphical abstract

Cited by 23 publications

References 64 publications

In vitro antibacterial and bio-histological effects of cerastes cerastes venom on albino mice

In vitro antibacterial and bio-histological effects of cerastes cerastes venom on albino mice

A Comprehensive Review of Corn Protein‐derived Bioactive Peptides: Production, Characterization, Bioactivities, and Transport Pathways

Identification of the Molecular Determinants of the Antibacterial Activity of LmutTX, a Lys49 Phospholipase A2 Homologue Isolated from Lachesis muta muta Snake Venom (Linnaeus, 1766)

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Identification of the Molecular Determinants of the Antibacterial Activity of LmutTX, a Lys49 Phospholipase A₂ Homologue Isolated from Lachesis muta muta Snake Venom (Linnaeus, 1766)