Abstract
An extracellular antifungal protein of 28 kDa (exAFP-C28) was identified from an endophytic fungus Colletotrichum sp. DM-06. After purification, the MIC value of exAFP-C28 against Candida albicans, a well-known human pathogenic fungus was found to be 32 μg/mL that unaffected the human red blood cells. The antifungal activity associated with exAFP-C28 was manifested by the increased membrane permeability of C. albicans cells followed by disruption. Proteomics and bioinformatics analyses revealed that several peptide fragments of exAFP-C28 have identity with the bacterial 50S ribosomal protein L10, and a stretch of 55 amino acids of two peptide fragments corresponding to the Nterminus of L10 protein is capable of forming amphipathic helix required for membrane penetration. Taken together, our results suggest that the exAFP-C28 protein from Colletotrichum sp. DM-06 is a promising therapeutic agent in controlling candidiasis disease in animals including humans.
Keywords: Antifungal protein, Candida albicans, Colletotrichum sp. DM-06, endophytic fungus, extracellular protein, pathogenic fungus
Protein & Peptide Letters
Title:Identification of an Extracellular Antifungal Protein from the Endophytic Fungus Colletotrichum sp. DM06
Volume: 20 Issue: 2
Author(s): Prabuddha Dey, Maulik R. Kamdar, Santi M. Mandal and Mrinal K. Maiti
Affiliation:
Keywords: Antifungal protein, Candida albicans, Colletotrichum sp. DM-06, endophytic fungus, extracellular protein, pathogenic fungus
Abstract: An extracellular antifungal protein of 28 kDa (exAFP-C28) was identified from an endophytic fungus Colletotrichum sp. DM-06. After purification, the MIC value of exAFP-C28 against Candida albicans, a well-known human pathogenic fungus was found to be 32 μg/mL that unaffected the human red blood cells. The antifungal activity associated with exAFP-C28 was manifested by the increased membrane permeability of C. albicans cells followed by disruption. Proteomics and bioinformatics analyses revealed that several peptide fragments of exAFP-C28 have identity with the bacterial 50S ribosomal protein L10, and a stretch of 55 amino acids of two peptide fragments corresponding to the Nterminus of L10 protein is capable of forming amphipathic helix required for membrane penetration. Taken together, our results suggest that the exAFP-C28 protein from Colletotrichum sp. DM-06 is a promising therapeutic agent in controlling candidiasis disease in animals including humans.
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Dey Prabuddha, R. Kamdar Maulik, M. Mandal Santi and K. Maiti Mrinal, Identification of an Extracellular Antifungal Protein from the Endophytic Fungus Colletotrichum sp. DM06, Protein & Peptide Letters 2013; 20 (2) . https://dx.doi.org/10.2174/0929866511320020008
DOI https://dx.doi.org/10.2174/0929866511320020008 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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