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Antibacterial potential of a basic phospholipase A2 (VRV-PL-V) of Daboia russellii pulchella (Russell’s viper) venom
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  • 作者:S. Sudarshan (1)
    B. L. Dhananjaya (1) (2)
  • 关键词:snake venom ; phospholipase A2 ; antimicrobial ; Daboia russellii pulchella ; human pathogenic bacteria
  • 刊名:Biochemistry (Moscow)
  • 出版年:2014
  • 出版时间:November 2014
  • 年:2014
  • 卷:79
  • 期:11
  • 页码:1237-1244
  • 全文大小:197 KB
  • 参考文献:1. Norrby, S. R., Nord, C. E., Finch, R., and European Society of Clinical Microbiology and Infectious Diseases (2005) Lack of development of new antimicrobial drugs: a potential serious threat to public health, / Lancet Infect. Dis., 5, 115-19. CrossRef
    2. Choudhury, R., Panda, S., and Singh, D. V. (2012) Emergence and dissemination of antibiotic resistance: a global problem, / Ind. J. Med. Microbiol., 30, 384-90. CrossRef
    3. Echols, R. M. (2012) A long and winding road; evolution of antimicrobial drug development -crisis management, / Expert Rev. Anti Infect. Ther., 10, 1311-319. CrossRef
    4. Ghafur, A. (2013) The Chennai declaration: a solution to the antimicrobial resistance problem in the Indian subcontinent, / Clin. Infect. Dis., 56, 1190. CrossRef
    5. Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms, / Nature, 415, 389-95. CrossRef
    6. Samy, R. P., Gopalakrishnakone, P., Stiles, B. G., Girish, K. S., Swamy, S. N., Hemshekhar, M., Tan, K. S., Rowan, E. G., Sethi, G., and Chow, V. T. (2012) Snake venom phospholipases A2: a novel tool against bacterial diseases, / Curr. Med. Chem., 19, 6150-162. CrossRef
    7. Perumal Samy, R., Pachiappan, A., Gopalakrishnakone, P., Thwin, M. M., Hian, Y. E., Chow, V. T., Bow, H., and Weng, J. T. (2006) / In vitro antimicrobial activity of natural proteins and animal venoms tested against / Burkholderia pseudomallei, / BMC Infect. Dis., 6, 1-6. CrossRef
    8. Kini, R. M. (1997) Phospholipase A2: a complex multifunctional protein puzzle, in / Venom Phospholipase A 2 / Enzymes: Structure, Function and Mechanism (Kini, R. M., ed.) John Wiley & Sons, Chichester, U. K.
    9. Gutierrez, J. M., and Lomonte, B. (2013) Phospholipase A2: unveiling the secrets of a functionally versatile group of snake venom toxins, / Toxicon, 62, 27-9. CrossRef
    10. Soares, A. M., Mancin, A. C., Cecchini, A. L., Arantes, E. C., Franca, S. C., Gutierrez, J. M., and Giglio, J. R. (2001) Effects of chemical modifications of croprotein B, the phospholipase A2 subunit of croprotein from / Crotalus durissus terrificus snake venom, on its enzymatic and pharmacological activities, / Int. J. Biochem. Cell Biol., 33, 877-88. CrossRef
    11. Toyama, M. H., de Oliveira, D. G., Beriam, L. O. S., Novello, J. C., Rodrigues-Simioni, L., and Marangoni, S. (2003) Structural, enzymatic and biological properties of new PLA2 isoform from / Crotalus durissus terrificus venom, / Toxicon, 41, 1033-038. CrossRef
    12. Sampaio, S. C., Brigatte, P., Sousa-e-Silva, M. C. C., dos-Santos, E. C., Rangel-Santos, A. C., Rangel-Santos, A. C., Curi, R., and Cury, Y. (2003) Contribution of croprotein for the inhibitory effect of / Crotalus durissus terrificus snake venom on macrophage function, / Toxicon, 41, 899-07. CrossRef
    13. Paramo, L., Lomonte, B., Pizarro-Cerda, J., Bengoechea, J. A., Gorvel, J. P., and Moreno, E. (1998) Bactericidal activity of Lys49 and Asp49 myotoxic phospholipases A2 from / Bothrops asper snake venom: syntheti
  • 作者单位:S. Sudarshan (1)
    B. L. Dhananjaya (1) (2)

    1. Venom Research Unit, Adichunchanagiri Biotechnology and Cancer Research Institute (ABCRI), Balagangadharanatha Nagara, Mandya District, Karnataka, 571 448, India
    2. Toxinology/Toxicology and Drug Discovery Unit, Center for Emerging Technologies, Jain Global Campus, Jain University, Kanakapura Taluk, Ramanagara, 562112, Karnataka, India
  • ISSN:1608-3040
文摘
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.

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