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Biochemistry (Moscow)

, Volume 79, Issue 11, pp 1237–1244 | Cite as

Antibacterial potential of a basic phospholipase A2 (VRV-PL-V) of Daboia russellii pulchella (Russell’s viper) venom

  • S. Sudarshan
  • B. L. DhananjayaEmail author
Article

Abstract

Microbial/bacterial resistance against antibiotics is considered as a potentially serious threat to public health. Further, as these antibiotics elicit side effects, there is interest in developing new molecules with novel modes of action from diverse organisms. Along these lines, in this study the antibacterial potential of the basic protein VRV-PL-V (Vipera russellii venom phospholipase A2 fraction V) of Daboia russellii pulchella venom was evaluated. VRV-PL-V demonstrated a potent antibacterial activity against all the human pathogenic strains tested. It inhibited more effectively Gram-positive bacteria like Staphylococcus aureus and Bacillus subtilis when compared to Gram-negative bacteria like Escherichia coli, Vibrio cholerae, Klebsiella pneumoniae, and Salmonella paratyphi. It inhibited bacterial growth with MIC values ranging from 13 to 24 μg/ml. The antibacterial potential of VRV-PL-V was comparable to the standards used like gentamycin, chloramphenicol, and streptomycin. There was a strong correlation between PLA2 activities and hemolytic and antibacterial activity. It was found that even in the presence of p-bromophenacyl bromide (an inhibitor of PLA2 enzymatic activity), there was marked antibacterial activity, suggesting dissociation or partial overlapping of the bactericidal/antimicrobial domains. Therefore, this study shows that although there is a strong correlation between enzymatic and antimicrobial activities of VRV-PL-V, it may also possess other properties that mimic bactericidal/membrane permeability-increasing protein.

Key words

snake venom phospholipase A2 antimicrobial Daboia russellii pulchella human pathogenic bacteria 

Abbreviations

MIC

minimum inhibitory concentration

p-BPB

p-bromophenacyl bromide

svPLA2

snake venom phospholipase A2

VRV-PL-V

Vipera russellii venom phospholipase A2 fraction V

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Copyright information

© Pleiades Publishing, Ltd. 2014

Authors and Affiliations

  1. 1.Venom Research UnitAdichunchanagiri Biotechnology and Cancer Research Institute (ABCRI)Mandya DistrictIndia
  2. 2.Toxinology/Toxicology and Drug Discovery Unit, Center for Emerging Technologies, Jain Global CampusJain UniversityKanakapura Taluk, RamanagaraIndia

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