1Research Scholar, Department of Biotechnology, National Fellow, ICAR-Directorate of Coldwater Fisheries Research, Bhimtal, Nainital, 263136, Uttarakhand, India
2Research Scholar, Department of Biotechnology, Kumaun University, Bhimtal Campus, Nainital, 263136, Uttarakhand
3Head, Department of Biotechnology, Kumaun University, Bhimtal Campus, Nainital, 263136, Uttarakhand
4National Fellow, National Fellow, Department of Biotechnology, ICAR-Directorate of Coldwater Fisheries Research, Bhimtal, Nainital, 263136, Uttarakhand, India
*Corresponding author E-mail: compton.pande@.yahoo.co.in
Online published on 21 January, 2017.
Antimicrobial peptides extensively expressed in vertebrates, and invertebrates have assorted mechanisms of action and protect against pathogens. Liver-expressed antimicrobial peptide (LEAP) is a multifunctional cysteine-rich peptide that provides protection against infectious pathogens besides iron regulation. We have identified and cloned cDNA encoding LEAP from Tor putitora (TP-LEAP) as 440 bp fragment, with an open reading frame (ORF) of 279 nucleotides. The ORF encodes a pre-propeptide of 93 and a mature peptide of 25 amino acids. 3D model of the mature TP-LEAP, predominantly a β sheet, was generated and validated. Motif analysis and docking of TP-LEAP with iron transporter ferroportin revealed that the disulfide bonds are responsible for a stable structure besides interaction with ferroportin. Arg8 and Cys11, of mature TP-LEAP, formhydrogen bonds with Asn332 and Thr323 with bond lengths of 2.48Å and 2.55Å, respectively. TP-LEAP was phylogenetically closely related to Schizothorax richardsonii and Cyprinus carpio.
Liver-expressed antimicrobial peptide (LEAP), Antimicrobial peptides (AMPs), Hepcidin, Innate immunity, Microbes
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