Abstract
An antimicrobial peptide was extracted from the antagonistic actinomycetes G19. It was designated as G19-F. By using MALDI-TOF mass spectrometry, the molecular weight of G19-F was determined. The primary structure of the antimicrobial peptide was determined using N-terminal sequencing and mass spectrometry. Results showed that the peptide had eleven amino acids, with the sequence D-V-C-D-G-G-D-G-D-E-D, and a calculated molecular mass of 1,096 Da. G19-F showed antimicrobial activity against peach crown gall caused by Agrobacterium tumefaciens. The antimicrobial peptide maintained its activity after being heated to 100 °C and exhibited stability from pH 4 to 10. Its activity has also remained after ultraviolet irradiation. The mechanism by which G19-F inhibits A. tumefaciens was to increase permeability of the cell membrane and destroy the cell wall structure. Furthermore, as a novel peptide, it has a potential for cure A. tumefaciens infection.
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This research was supported by the Beijing Natural Science Foundation (No. 5112010) and the Beijing Education Board (No. KM200910020001).
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Wang, S., Ji, J., Ma, H. et al. A novel antibacterial peptide active against peach crown gall (Agrobacterium tumefaciens) isolated from cyanide-tolerant actinomycetes G19. World J Microbiol Biotechnol 31, 69–74 (2015). https://doi.org/10.1007/s11274-014-1765-2
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DOI: https://doi.org/10.1007/s11274-014-1765-2