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Enhancing antimicrobial activity of mastoparan-B by amino acid substitutions
Mars J. Yang,Wen-Yuh Lin,Chun-Hsien Lin,Ching-Lin Shyu,Roger F. Hou,Wu-Chun Tu 한국응용곤충학회 2013 Journal of Asia-Pacific Entomology Vol.16 No.4
This study evaluated antimicrobial and hemolytic activities of mastoparan-B (MP-B) isolated fromthe venomof the hornet, Vespa basalis, and its analogs after substituting certain amino acid (aa) residues.MP-B exhibited significantly different antimicrobial activities against bacteria species/strains tested, especially two Escherichia coli strains, Staphylococcus xylosus and Citrobacter koseri at low dosages, and was non-specific against certain Gram-positive and -negative bacteria. Our results indicated that hydrophobicitymodification by single aa substitution may enhance their antimicrobial activities. An aa substituted MP-B, viz., MP-B-1, inwhich Trp substituted for Leu3, became more effective than the original peptide at inhibiting or killing the bacterial species tested, especially Klebsiella pneumonia, Salmonella typhimurium, and Salmonella Cholerasuis, and even up to 8 timesmore effective in some cases. However, MP-B-2 was virtually similar to MP-B against each bacterial species assayed,while MP-B-3 reduced its effectiveness greatly compared to others. On the other hand, MP-B and its analogs were not effective against the beneficial probiotics and they were not hemolytic to erythrocytes at the dosages tested. Our results suggested that MP-B becomes more potent against specific pathogenic bacteria and safe to the probiotics after undergoing appropriate amino acid substitutions.