Anti- Yersinia Activity of Cryptdin-2: A Paneth Cell Peptide
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Anti-Yersinia Activity of Cryptdin-2: A Paneth Cell Peptide Simran Preet • Jugsharan Singh Virdi Praveen Rishi
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Received: 26 June 2012 / Revised: 15 October 2012 / Accepted: 4 March 2013 / Published online: 20 April 2013 Ó The National Academy of Sciences, India 2013
Abstract In view of the emerging antibiotic(s) resistance in pathogens, there is a renewed interest in clinical medicine to exploit novel agents with a wide range of actions over several pathogens. Therefore, in the present study, bactericidal efficacy of cryptdin-2 against Yersinia enterocolitica was evaluated. Cryptdin-2 exhibited strong bactericidal activity against Y. enterocolitica at the minimum bactericidal concentration (MBC) of 21 lg/ml. Scanning electron microscopic investigations of cryptdin-2 treated bacterial cells revealed that the peptide was able to induce significant morphological alterations in terms of destructive pore formation and damaged membrane confirming its membrane dependent bactericidal activity. N-phenyl napthylamine (NPN) uptake assay in the presence of sublethal, lethal as well as twice the lethal concentrations further confirmed the membrane-dependent mode of action of cryptdin-2 which indicated that the peptide could permeabilize the membrane of Y. enterocolitica. Additionally, the peptide interfered with DNA, RNA as well as protein synthesis in Y. enterocolitica, with maximum inhibition observed for protein synthesis. Thus, the biochemical and biophysical alterations observed in the treated cells in terms of macromolecular synthesis and membrane permeabilization respectively, correlated well with the bactericidal activity. In view of the antibacterial efficacy of the peptide against Salmonella typhimurium and Entamoeba histolytica, observed in our earlier studies, S. Preet P. Rishi (&) Department of Microbiology, Basic Medical Sciences Block, Panjab University, Sector-14, Chandigarh 160014, India e-mail: [email protected] J. S. Virdi Department of Microbiology, University of Delhi, South Campus, Benito-Juarez Road, New Delhi 110021, India
along with its inhibitory potential against Y. enterocolitica as demonstrated in the present study, suggests that it may be exploited as a broad-spectrum antimicrobial agent against enteric infections. Keywords Cryptdin-2 Yersinia enterocolitica Membrane permeabilization Morphological alterations Macromolecular synthesis
Introduction Emergence of drug resistance amongst enteric pathogens as well as difficulty in keeping pace with the development of newer antibiotics, has forced researchers to look for novel strategies against these infectious agents [1]. In this context, development of cationic antimicrobial peptides (AMPs) for the treatment of such infections has recently become a major area of investigation [2, 3]. Among naturally occurring AMPs, defensins form a unique family of cysteine rich cationic polypeptides with 3 or 4 disulfide bridges [4]. Mouse enteric alpha-defensins called cryptdins are broad-spectrum AMPs due to their ability to kill
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