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Molecular Characterization and Gene Expression Profiling ... - CUSAT

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Chapter 1<br />

Lantibiotics contain small ring structures enclosed by a thioether bond <strong>and</strong><br />

their structure <strong>and</strong> properties have recently been reviewed (Montville <strong>and</strong><br />

Chen, 1998). One of the lantibiotics, nisin, is currently used as an<br />

antimicrobial agent for food preservation <strong>and</strong> this peptide has relatively high<br />

activity against Gram-positive bacteria due to its specific high affinity with<br />

Lipid II, a precursor in the bacterial cell wall synthesis (Breukink <strong>and</strong> de<br />

Kruijff, 1999; Breukink et al., 1999). Recently synthesized six <strong>and</strong> eight<br />

residue cyclic D,L-α-peptides have been found to exhibit high efficacy to kill<br />

bacteria with low haemolytic activity (Fernadez-Lopez et al., 2001). Upon<br />

binding to lipid membranes the cyclic peptides can stack to form hollow, β-<br />

sheet-like tubular structures increasing membrane permeability. With short<br />

size, easy to synthesize <strong>and</strong> being proteolytically stable, this class of peptides<br />

holds considerable potential in fighting existing <strong>and</strong> emerging infectious<br />

diseases.<br />

1.7.7 Induction <strong>and</strong> Regulation of AMP expression<br />

AMPs in multicellular organisms are found on external surfaces such<br />

as the skin or the lungs or they are sequestered in granules of neutrophils,<br />

from where they can be released to kill microbes. Some AMPs are<br />

synthesized constitutively, for instance the histatins (Tsai <strong>and</strong> Bobek, 1998)<br />

<strong>and</strong> human β- defensin-1 (Yang et al., 2002). Others are often induced in<br />

response of an infection (Hoffmann et al., 1999) <strong>and</strong> thus can be considered<br />

as acute-phase proteins, e.g. LL- 37 (Frohm et al., 1997) <strong>and</strong> human β-<br />

defensin-2 (Harder et al., 2000; Schutte <strong>and</strong> McCray, 2002; Yang et al., 2002).<br />

The large majority of AMPs synthesized by multicellular organisms<br />

are encoded by the genome. Insects <strong>and</strong> mammals typically express multiple<br />

AMPs. For example, at least ten sheep genes encode AMPs, including eight<br />

cathelicidins <strong>and</strong> two β-defensins (Huttner et al., 1998). The bovine genome<br />

contains genes for at least eleven cathelicidins (Scocchi et al., 1997) <strong>and</strong> over<br />

twenty β-defensins (Ryan et al., 1998). The AMPs are produced mainly<br />

<strong>Molecular</strong> <strong>Characterization</strong> <strong>and</strong> <strong>Gene</strong> <strong>Expression</strong> <strong>Profiling</strong> of Antimicrobial Peptides in Penaeid Shrimps<br />

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