Expression analysis and biological activity of moronecidin from rock bream, Oplegnathus fasciatus

Bae, Jin-Sol; Shim, Sang Hee; Hwang, Seong Don; Park, Myoung-Ae; Jee, Bo-Young; An, Cheul‐Min; Kim, Young‐Ok; Kim, Juwon; Park, Chan-Il

doi:10.1016/j.fsi.2014.07.023

Cited by 21 publications

(8 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Members of the piscidin family include piscidin, pleurocidin [ 43 ], moronecidin, misgurin, epinecidin [ 44 ], gaduscidin [ 45 ] and dicentracin and while they share an overall similar structure, they share little sequence homology amongst the mature peptides. Piscidin and piscidin family member genes have been identified in a number of fish species and include one piscidin family member in seabass ( Dicentrarchus labrax ) [ 46 ], icefish ( Chionodraco hamatus ) [ 47 ], rock bream ( Oplegnathus fasciatus ) [ 48 ], large yellow croaker ( Larimichthys crocea ) [ 49 , 50 ], striped trumpeter ( Latris lineata ) [ 51 ], mandarin fish ( Siniperca chuatsi ) [ 43 ], yellowtail flounder ( Pleuronectes ferruginea Storer), American plaice ( Hippoglossoides platessoides Fabricius), witch flounder ( Glyptocephalus cynoglossus L.), Atlantic halibut ( Hippoglossus hippoglossus L.) [ 52 ]; two in Atlantic cod ( Gadus morhua ) [ 45 , 53 ] along with a novel splice variant [ 54 ]; three in grouper ( Epinephelus coioides ) [ 44 ]; four in hybrid striped bass ( Morone chrysops x Morone saxatilis ) [ 55 , 56 , 57 ]; four genes and 3 pseudogenes in the winter flounder ( Pseudopleuronectes americanus ) [ 58 , 59 ]; and five in Nile tilapia ( Oreochromis niloticus ) [ 60 ]. The majority of the piscidin genes have a four-exon/three-intron genomic organization [ 43 , 55 , 61 ].…”

Section: Piscidinsmentioning

confidence: 99%

“…However, the piscidin 4 genes result in a 44 amino acid mature peptide that is ~5.5 kDa [ 56 , 57 ]. The mature piscidin peptides have an amphipathic α-helical conformation with the hydrophilic side being cationic and capable of interacting with pathogen membranes in a parallel fashion [ 48 , 62 , 63 , 64 ]. Collectively, piscidin family members seem to be undergoing positive selection [ 53 , 65 ], suggesting they may be undergoing diversification as a means to adapt to rapidly changing pathogens and would support the low sequence identity amongst the mature peptides of piscidin family members.…”

Section: Piscidinsmentioning

confidence: 99%

“…Piscidin family members demonstrate antimicrobial or growth inhibition activity towards a wide array of Gram-negative and Gram-positive bacteria [ 48 , 52 , 54 , 55 , 56 , 58 , 60 , 62 , 73 ] with differing bacterial selectivity in a time-dependent fashion [ 62 ] and over a considerable temperature and salt range [ 55 ]. Piscidins also possess anti-viral activity under a broad range of physiological conditions and temperatures [ 74 ], anti-fungal activity [ 75 , 76 ], anti-parasite activity at physiological concentrations of piscidins found in fish species [ 49 , 54 , 77 , 78 , 79 ] and anti-tumor activity towards mammalian cells [ 80 , 81 , 82 , 83 ].…”

Section: Piscidinsmentioning

confidence: 99%

“…The upstream promoter regions of members of the piscidin family contain putative binding sites for NF-IL-6, alpha-IRE, gamma-IRE [ 58 , 61 ], AP-1 [ 58 ], C/EBPβ [ 55 ] and hepatocyte nuclear factor (HNF-1) [ 44 ] transcription factors, with HNF-1 shown to be required for the transcriptional activation of epinecidin in response to LPS [ 44 ]. Although the receptors, intracellular signaling pathway and transcription factors involved in the regulation of piscidin family members in response to pathogens have yet to be explicitly identified and characterized, it appears that LPS [ 43 ], Gram-negative and Gram-positive bacteria [ 45 , 47 , 48 , 54 , 60 , 66 , 90 ], poly I:C [ 47 , 66 ], viruses [ 47 , 48 ] and parasites [ 46 , 51 , 91 , 92 , 93 , 94 ] enhance the expression of piscidin family members in fish spleen, kidney, skin, and intestinal tissues as well as in mast cells ( Table 1 , Table 2 , Table 3 and Table 4 and references therein). However, it is important to note that the regulation of piscidin transcript and protein levels is pathogen, fish, tissue and piscidin dependent, thus requiring detailed studies of each fish species, pathogen, tissue, and piscidin family member.…”

Section: Piscidinsmentioning

confidence: 99%

See 3 more Smart Citations

Antimicrobial Peptides as Mediators of Innate Immunity in Teleosts

Katzenback

2015

Biology

116

View full text Add to dashboard Cite

Antimicrobial peptides (AMPs) have been identified throughout the metazoa suggesting their evolutionarily conserved nature and their presence in teleosts is no exception. AMPs are short (18–46 amino acids), usually cationic, amphipathic peptides. While AMPs are diverse in amino acid sequence, with no two AMPs being identical, they collectively appear to have conserved functions in the innate immunity of animals towards the pathogens they encounter in their environment. Fish AMPs are upregulated in response to pathogens and appear to have direct broad-spectrum antimicrobial activity towards both human and fish pathogens. However, an emerging role for AMPs as immunomodulatory molecules has become apparent—the ability of AMPs to activate the innate immune system sheds light onto the multifaceted capacity of these small peptides to combat pathogens through direct and indirect means. Herein, this review focuses on the role of teleost AMPs as modulators of the innate immune system and their regulation in response to pathogens or other exogenous molecules. The capacity to regulate AMP expression by exogenous factors may prove useful in modulating AMP expression in fish to prevent disease, particularly in aquaculture settings where crowded conditions and environmental stress pre-dispose these fish to infection.

show abstract

Section: Piscidinsmentioning

confidence: 99%

Section: Piscidinsmentioning

confidence: 99%

Section: Piscidinsmentioning

confidence: 99%

Section: Piscidinsmentioning

confidence: 99%

See 2 more Smart Citations

Antimicrobial Peptides as Mediators of Innate Immunity in Teleosts

Katzenback

2015

Biology

116

View full text Add to dashboard Cite

show abstract

“…As well as CAMPs, other AMPs have been identified in fish including hepcidin (Douglas et al, 2003), defensins (Jin et al, 2010), moronecidin (Bae et al, 2014), misgurin (Park et al, 1997), parasin (Cho et al, 2002), piscidin (Lin et al, 2012) and daxin (Oren et al, 1996). Hepcidins in mammals are heavily involved in regulation and homeostasis of iron metabolism (Kulaksiz et al, 2005).…”

Section: Neutrophil Functionmentioning

confidence: 99%

Immune defence mechanisms of barramundi (Lates calcarifer) peripheral blood against Streptococci

Masterman¹

View full text Add to dashboard Cite

IMMUNE DEFENCE MECHANISMS OF BARRAMUNDI (Lates calcarifer) PERIPHERAL BLOOD AGAINST STREPTOCOCCIAquaculture now supplies more than half of the fish used for human consumption and is a major contributor to global food security. As aquaculture growth must be sustained to continue to supply increasing population-driven demand for food fish, efficiency must be increased. In spite of major inroads in disease control through mass vaccination of farm fish, bacterial diseases continue to cause substantial losses, particularly in tropical and warmtemperate regions where aquaculture is expanding fastest. To develop new vaccines, and improve existing vaccines for effective disease control in these regions, an improved understanding of the mechanisms of pathogen immune evasion and dissemination within the host may identify new vaccine targets. Streptococcus agalactiae and Streptococcus iniae are significant pathogens of warm and temperate farmed and wild fish. Both have a broad host range, express a polysaccharide capsule as a major virulence determinant and cause similar pathologies characterized by rapid sepsis, followed by meningitis and death. S. iniae causes significant mortality in barramundi, Lates calcarifer. Interestingly, S. agalactiae ST261, although causing mortality in wild fish along the Queensland coast, does not appear to cause mortality in barramundi farmed in close proximity. This difference provides a basis for comparison, in order to explore the requirements for blood colonization and sepsis by S. iniae in barramundi, and to increase our understanding of sepsis in fish.S. iniae grew rapidly in barramundi blood, doubling in less than 30 minutes in a whole blood bactericidal assay. In contrast, S. agalactiae was unable to multiply. Moreover, E. coli DH5 was completely killed in barramundi blood during the same incubation period, suggesting 3 that antibacterial humoral and cellular immune defences were functional within the blood bactericidal model. A capsular defective strain of S. iniae also survived in the bloodbactericidal assay, however the rapid proliferation was reduced, suggesting that while the capsule is important for bacterial colonisation it is not the only means used to evade bloodborne defences. As gram-positive pathogens are particularly susceptible to lysozyme due to the dominance of muramic acids in the cell wall, the role of lysozyme was investigated.Lysozyme levels in barramundi serum and plasma were undetectable in a lysis assay using Micrococcus lysodeitikus, indicating very low levels of circulating lysozyme in healthy barramundi.The first responder immune cells in blood are neutrophils and these are critical in the prevention of sepsis; for example, granulocytopenia (circulating granulocyte deficiency) is associated with increased susceptibility to Escherichia coli K1 and Klebsiella pneumoniae sepsis in neonates, and this can be partially repaired by injection of granulocyte colony stimulating factor (G-CSF) to increase neutrophil numbers (Deshmukh et al., 2014). This critic...

show abstract