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