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        Purification, characterisation and identification of acidocin LCHV, an antimicrobial peptide produced by Lactobacillus acidophilus n.v. Er 317/402 strain Narine

        Author
        Mkrtchyan, Hermine
        Gibbons, Simon
        Heidelberger, Sibylle
        Zloh, Mire
        Limaki, Hamidreza Khalatbari
        Attention
        2299/10562
        Abstract
        In the last two decades, antimicrobial peptides (AMPs) have been gaining attention as antimicrobial alternatives to chemical food preservatives and commonly used antibiotics. Lactobacillus acidophilus n.v. Er 317/402 strain Narine produces a small AMP with a molecular weight of 1.1kDa, designated acidocin LCHV. In this study, the AMP was extremely heat stable (90min at 130 degrees C), was active over a wide pH range and was found to be sensitive to proteolytic enzymes (trypsin, pepsin and proteinase K). Acidocin LCHV has a broad spectrum of activity both against Gram-positive and Gram-negative pathogens, including several that are classified as Especially Dangerous Infections by the World Health Organization as well as meticillin-resistant Staphylococcus aureus (MRSA) and Clostridium difficile. Matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry (MALDI-TOF/MS) was used to determine the molecular mass and sequence of the purified peptide. Complete killing with immediate impact on cells was observed within a very short period of time (10min).
        Publication date
        2010
        Published in
        International Journal of Antimicrobial Agents
        Published version
        https://doi.org/10.1016/j.ijantimicag.2009.11.017
        Other links
        http://hdl.handle.net/2299/10562
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