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

Ramar Perumal Samy1, Bradley G Stiles2, Arunachalam Chinnathambi3

  • 1Venom and Toxin Research Programme, Department of Anatomy, Yong Loo Lin School of Medicine, National University Health System (NUHS), National University of Singapore, Singapore 117597; Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, NUHS, National University of Singapore, Singapore 117597; Department of Physiology, NUS Immunology Programme, Centre for Life Sciences, Yong Loo Lin School of Medicine, NUHS, National University of Singapore, Singapore 117456.

FEBS Open Bio
|January 22, 2016
PubMed

Insights

Novel proteins from Indian Russell's viper venom, called Viperatoxin (VipTx-I and VipTx-II), show antimicrobial activity. VipTx-II effectively kills bacteria like methicillin-resistant Staphylococcus aureus (MRSA) by damaging cell membranes.

Area of Science:

  • Biochemistry
  • Microbiology
  • Toxicology

Background:

  • Methicillin-resistant Staphylococcus aureus (MRSA) infections pose a significant public health threat.
  • There is an urgent need for novel therapeutic agents against drug-resistant bacteria.
  • Indian Russell's viper venom is a potential source of bioactive compounds.

Purpose of the Study:

  • To purify and characterize novel proteins from Indian Russell's viper venom.
  • To evaluate the antimicrobial potential of these proteins against pathogenic bacteria.
  • To investigate the mechanism of action of the identified antimicrobial protein.

Main Methods:

  • Purification of 15-kDa proteins (Viperatoxin, VipTx-I and VipTx-II) from whole venom.
  • In vitro antimicrobial assays (plate and broth-dilution) against various bacterial strains.
  • N-terminal amino acid sequencing, molecular weight determination (SDS-PAGE), and electron microscopy.

Main Results:

  • VipTx-II exhibited potent in vitro antimicrobial activity against S. aureus, B. pseudomallei, P. vulgaris, and P. mirabilis.
  • Minimum inhibitory concentrations (MICs) for VipTx-II were as low as 6.25 μg/ml against B. pseudomallei.
  • Electron microscopy revealed that VipTx-II induced bacterial membrane damage and pore formation.
  • VipTx-II showed low cytotoxicity on human THP-1 cells at higher concentrations.

Conclusions:

  • VipTx-II is a promising antimicrobial agent derived from snake venom.
  • The protein's bactericidal effect is mediated by membrane damage.
  • VipTx-II's low cytotoxicity suggests potential for in vivo antimicrobial applications.
Keywords:
BactericidalDaboia russelli russelliMALDI-TOF/MS, matrix-assisted laser desorption ionization-time of flight/mass spectrometerMDR, multi-drug resistantMH, Mueller HintonMICs, minimum inhibitory concentrationsMRSA, methicillin-resistant Staphylococcus aureusMTXs, myotoxinsPLA2, phospholipase A2Phospholipase A2SEM, scanning electron microscopyTEM, transmission electron microscopyTS, Tryptic SoyaVipTx-I and VipTx-II, viperatoxins I and IIViperatoxin-IViperatoxin-II

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