The Protein Journal

, Volume 33, Issue 1, pp 1–10

Characterization and Structural Analysis of Hepcidin Like Antimicrobial Peptide From Schizothorax richardsonii (Gray)

Article

DOI: 10.1007/s10930-013-9530-1

Cite this article as:
Chaturvedi, P., Dhanik, M. & Pande, A. Protein J (2014) 33: 1. doi:10.1007/s10930-013-9530-1
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Abstract

Innate immune system is a primary line of defense in fish that protects it from the invading pathogens. Antimicrobial peptides (AMPs) are widely distributed in nature and are essential components of innate immunity. These molecules enable the host’s innate immune system to fight against a variety of infectious agents. One such AMP, hepcidin, is a cysteine rich amphipathic peptide. We have amplified, cloned and characterized hepcidin like AMP from Schizothorax richardsonii that inhabits one of the most difficult aquatic ecosystems in the Indian Himalayas. The cDNA encoding hepcidin like peptide was amplified as a 371 bp fragment with an open reading frame (ORF) of 279 nucleotides flanked by 5′ and 3′ UTRs of 70 and 22 bases respectively. This ORF encodes a peptide of 93 amino acids with a signal peptide of 24 amino acids and a mature peptide of 25 amino acids. The mature hepcidin like peptide of S. richardsonii has eight cystine residues that participate in the formation of four disulfide bonds, a unique feature of hepcidin like AMPs. A 3D model of hepcidin like mature peptide was generated using Modeller 9.10 which was validated using PROCHECK and ERRAT. Phylogenetic analysis of hepcidin like AMP from S. richardsonii revealed that it was closely related to hepcidin from olive barb (Puntius sarana).

Keywords

Antimicrobial peptides Hepcidin Innate immunity Schizothorax richardsonii Infectious agents 

Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  • Preeti Chaturvedi
    • 1
  • Meenakshi Dhanik
    • 1
  • Amit Pande
    • 1
  1. 1.Directorate of Coldwater Fisheries ResearchBhimtal, NainitalIndia

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