4.2 Article

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

Journal

BIOCHEMISTRY-MOSCOW
Volume 79, Issue 11, Pages 1237-1244

Publisher

MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1134/S000629791411011X

Keywords

snake venom; phospholipase A(2); antimicrobial; Daboia russellii pulchella; human pathogenic bacteria

Funding

  1. Balagangadharanatha Swamiji Institute for Technology (BGS-IT)
  2. Sri Adichunchangiri College of Pharmacy

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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 A(2) 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 mu g/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 PLA(2) 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.

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