NK-lysin of channel catfish: Gene triplication, sequence variation, and expression analysis

Wang, Qun; Wang, Yaping; Xu, Peng; Liu, Zhanjiang

doi:10.1016/j.molimm.2005.09.023

Cited by 70 publications

(25 citation statements)

References 52 publications

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“…The results of Southern blot hybridization of four different BAC clones suggest that the Japanese flounder NK-lysin gene exists as a single copy gene in one locus similar with that of fugu NK-lysin. Recently however, Wang et al [25] reported that the channel catfish NK-lysin genes were triplicated in one locus of its genome and consisted of two tandem repeats of three genes each. They also found that zebrafish genome has at least seven NK-lysin genes, six of which exist on chromosome 17 and one on chromosome 5.…”

Section: Nucleotide Sequences Of the Japanese Flounder Nk-lysin Cdna mentioning

confidence: 99%

Characterization of Japanese flounder (Paralichthys olivaceus) NK-lysin, an antimicrobial peptide

Hirono

Kondo

Koyama

et al. 2007

Fish & Shellfish Immunology

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Section: Nucleotide Sequences Of the Japanese Flounder Nk-lysin Cdna mentioning

confidence: 99%

Characterization of Japanese flounder (Paralichthys olivaceus) NK-lysin, an antimicrobial peptide

Hirono

Kondo

Koyama

et al. 2007

Fish & Shellfish Immunology

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“…They have an important role in innate immunity responses (Ganz, 2003;Zanetti, 2004), killing bacteria by permeabilization of the cytoplasmic membrane (Brogden, 2005), and also through inhibition of essential microbial processes, such as protein, cell-wall and nucleic acid syntheses (Patrzykat et al, 2002). Seven antimicrobial peptides have been described in channel catfish, including NK-lysin type 1, NK-lysin type 2, NK-lysin type 3 (Wang et al, 2006), bactericidal permeability-increasing protein (BPI) , cathepsin D (Dunham et al, 2002), hepcidin and liver-expressed AMP 2 (LEAP2) (Bao et al, 2006). Among these catfish described CAMPs, hepcidin, NK-lysin type 1, NK-lysin type 3 and cathepsin D seem to play a role during E. ictaluri infection (Pridgeon et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

Mechanisms of intrinsic resistance to antimicrobial peptides of Edwardsiella ictaluri and its influence on fish gut inflammation and virulence

et al. 2013

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The genus Edwardsiella comprises a genetically distinct taxon related to other members of the family Enterobacteriaceae. It consists of bacteria differing strongly in their biochemical and physiological features, natural habitats, and pathogenic properties. Intrinsic resistance to cationic antimicrobial peptides (CAMPs) is a specific property of the genus Edwardsiella. In particular, Edwardsiella ictaluri, an important pathogen of the catfish (Ictalurus punctatus) aquaculture and the causative agent of a fatal systemic infection, is highly resistant to CAMPs. E. ictaluri mechanisms of resistance to CAMPs are unknown. We hypothesized that E. ictaluri lipopolysaccharide (LPS) plays a role in both virulence and resistance to CAMPs. The putative genes related to LPS oligo-polysaccharide (O-PS) synthesis were in-frame deleted. Individual deletions of wibT, gne and ugd eliminated synthesis of the O-PS, causing auto-agglutination, rough colonies, biofilm-like formation and motility defects. Deletion of ugd, the gene that encodes the UDP-glucose dehydrogenase enzyme responsible for synthesis of UDP-glucuronic acid, causes sensitivity to CAMPs, indicating that UDP-glucuronic acid and its derivatives are related to CAMP intrinsic resistance. E. ictaluri OP-S mutants showed different levels of attenuation, colonization of lymphoid tissues and immune protection in zebrafish (Danio rerio) and catfish. Orally inoculated catfish with O-PS mutant strains presented different degrees of gut inflammation and colonization of lymphoid tissues. Here we conclude that intrinsic resistance to CAMPs is mediated by Ugd enzyme, which has a pleiotropic effect in E. ictaluri influencing LPS synthesis, motility, agglutination, fish gut inflammation and virulence.

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“…NK-lysins are much larger peptides than the classic antimicrobial peptides and have a globular 3D structure. Their primary sequences are rich in positively charged amino acids and contain conserved cysteines that make intradisulfide bonds (3).…”

mentioning

confidence: 99%

Effects of a single nucleotide polymorphism in the chicken NK-lysin gene on antimicrobial activity and cytotoxicity of cancer cells

Lee

Kim

Jang

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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NK-lysin is an effector protein of the innate immune system and an important component of host protection. We isolated a SNP in the NK-lysin coding sequence among different chicken breeds. This A to G substitution at the position 271 nucleotide in the ORF results in an Asn (N) to Asp (D) amino acid alteration. We synthesized two 30-aa peptides (N29N and N29D) to compare the biological activity of the helix 2-loop-helix 3 region of NK-lysin resulting from the polymorphic gene. Both peptides were found to be cytotoxic in bacteria and tumor cell cultures at micromolar concentrations. The N29N peptide, however, exhibited greater antibacterial and anticancer activity than the N29D peptide. Circular dichroism spectroscopy of the two peptides in negatively charged single unilamellar vesicles showed spectra typical of α-helical peptides. The helical profile of N29D was reduced substantially compared with that of N29N. However, no structural change was observed in neutral vesicles. ζ-Potential measurements of liposomes incubated with increasing peptide concentrations allowed surface charge neutralization with a negatively charged lipid, but not with a zwitterionic lipid. This result suggests that a difference in electrostatic interaction between lipid membranes and the helical peptides results from the polymorphic gene and is subsequently an important factor in cell lytic activity of variant NK-lysin peptides.antimicrobial peptides | genetic variation | innate immunity

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NK-lysin of channel catfish: Gene triplication, sequence variation, and expression analysis

Cited by 70 publications

References 52 publications

Characterization of Japanese flounder (Paralichthys olivaceus) NK-lysin, an antimicrobial peptide

Characterization of Japanese flounder (Paralichthys olivaceus) NK-lysin, an antimicrobial peptide

Mechanisms of intrinsic resistance to antimicrobial peptides of Edwardsiella ictaluri and its influence on fish gut inflammation and virulence

Effects of a single nucleotide polymorphism in the chicken NK-lysin gene on antimicrobial activity and cytotoxicity of cancer cells

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