Antimicrobial
peptides are crucial elements of the host non-specific innate immune system
which play a major role as natural antibiotics by providing first line defense
against microbial incursion. (Hancock etal., 2006, Zasloff.,2002). AMPs are
generally short, cationic, amphipathic and structurally diverse molecules that
are widely present in nearly all life form 1. These molecules display
extensive and strong antimicrobial activity against microbial assault primarily
by destroying membrane integrity of the invading pathogens. Apart from being antimicrobial, AMPs perform
immunomodulatory roles also by recruiting and activating innate and adaptive
immune cells; hence they were named as host defense peptides. Majority
of the AMPs are encoded by distinct genes, and a large number of structurally
different HDPs normally exist in a single species. Different groups of AMPs
reported in birds include NK-lysin (Cuperus et al. 2013; Ishige et al. 2014),
cathelicidin (Cuperus et al. 2013), liver-expressed antimicrobial peptide 2
(Cuperus et al. 2013) and avian ?-defensin (Cuperus et al. 2013; Ishige et al.
2015a) which endow them with tremendous innate immunity.

Liver-expressed
antimicrobial peptide 2 (LEAP-2) is the second blood-derived peptide isolated
firstly from human blood and displays antimicrobial activity and predominant
expression in the liver. (Krause et al., 2003). This peptide
belongs to cystein rich family of AMPs characterized by the presence of a four
cystein conserved motif and two intracellular disulphide bridges. LEAP2 has
been characterized from few organisms like human, monkey, pig, mouse, cow, and
chicken 8-12. In chicken, Cleap2 gene consists of three exons
and two introns, has been reported to be localized in chromosome 13 of
chicken genome. Like other cationic HDP, LEAP2 also possess a signal
peptide, a prepropeptide and an active mature peptide. Cleap2 gene encodes a 76 amino acid  prepropeptide which is enzymatically processed
by furin family of propeptide convertase to release mature peptide of 40 amino
acid. The RXXR motif at cleavage site between prodomain and mature region of
LEAP2 is conserved throughout vertebrates. Studies suggest that Human and
channel catfish LEAP2 gene express several splicing variants as a result of
alternative splicing. It is possible that LEAP2 gene employ splicing as a major
mechanism of its regulation.

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In the present study, we compared the nucleotide and protein
sequences of avian LEAP2

 

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