Bright Singh, I S; Rosamma, Philip; Chaithanya, E R; Anil Kumar, P R; Sherine, Sonia Cubelio; Naveen, Sathyan(Springer, May 23, 2013)
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Abstract:
Hepcidin is a family of short cysteine-rich
antimicrobial peptides (AMPs) participating in various
physiological functions with inevitable role in host immune
responses. Present study deals with identification and
characterisation of a novel hepcidin isoform from coral fish
Zanclus cornutus. The 81 amino acid (aa) preprohepcidin
obtained from Z. cornutus consists of a hydrophobic aa rich
22 mer signal peptide, a highly variable proregion of 35 aa
and a bioactive mature peptide with 8 conserved cysteine
residues which contribute to the disulphide back bone. The
mature hepcidin, Zc-hepc1 has a theoretical isoelectric
point of 7.46, a predicted molecular weight of 2.43 kDa
and a net positive charge of ?1. Phylogenetic analysis
grouped Z. cornutus hepcidin with HAMP2 group hepcidins
confirming the divergent evolution of hepcidin-like
peptide in fishes. Zc-hepc1 can attain a b-hairpin-like
structure with two antiparallel b-sheets. This is the first
report of an AMP from the coral fish Z. cornutus.
Description:
Probiotics & Antimicro. Prot. (2013) 5:187–194
DOI 10.1007/s12602-013-9139-x
Bright Singh, I S; Rosamma, Philip; Swapna, Antony P; Naveen, Sathyan; Anil Kumar, P R; Chaithanya, E R; Sajeevan, V N(Springer, November 25, 2012)
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Abstract:
Hepcidin is cysteine-rich short peptide of
innate immune system of fishes, equipped to perform prevention
and proliferation of invading pathogens like bacteria
and viruses by limiting iron availability and activating
intracellular cascades. Hepcidins are diverse in teleost
fishes, due to the varied aquatic environments including
exposure to pathogens, oxygenation and iron concentration.
In the present study, we report a 87-amino acid (aa)
preprohepcidin (Hepc-CB1) with a signal peptide of 24 aa,
a prodomain of 39 aa and a bioactive mature peptide of 24
aa from the gill mRNA transcripts of the deep-sea fish
spinyjaw greeneye, Chlorophthalmus bicornis. Molecular
characterisation and phylogenetic analysis categorised the
peptide to HAMP2-like group with a mature peptide of
2.53 kDa; a net positive charge (?3) and capacity to form
b-hairpin-like structure configured by 8 conserved cysteines.
The present work provides new insight into the mass
gene duplication events and adaptive evolution of hepcidin
isoforms with respect to environmental influences and
positive Darwinian selection. This work reports a novel
hepcidin isoform under the group HAMP2 from a nonacanthopterygian
deep-sea fish, C. bicornis
Description:
Probiotics & Antimicro. Prot. (2013) 5:1–7
DOI 10.1007/s12602-012-9120-0