Functional characterization of codCath, the mature cathelicidin antimicrobial peptide from Atlantic cod (Gadus morhua)

Broekman, Daniela C.; Zenz, Alexandra; Guðmundsdóttir, Bjarnheiður K.; Lohner, Karl; Maier, Valerie H.; Guðmundsson, Guðmundur H.

doi:10.1016/j.peptides.2011.09.012

Cited by 44 publications

(34 citation statements)

References 61 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition, antimicrobial peptides from teleost fish have been linked to multifunctional activities. Among them can be cited pardaxin ( Pardachirus marmoratus ), hepcidin ( Oreochromis mossambicus ), epinecidin ( Epinephelus coioides ), piscidin ( Morone chrysops ), misgurin ( Misgurnus anguillicaudatus ), NRC peptides ( Pleuronectes americanus ), myxinidin ( Myxine glutinosa ) and CodCath ( Gadus morhua ) [53]–[60].…”

Section: Discussionmentioning

confidence: 99%

Structural and Functional Characterization of a Multifunctional Alanine-Rich Peptide Analogue from Pleuronectes americanus

Migliolo

Silva

et al. 2012

PLoS ONE

View full text Add to dashboard Cite

Recently, defense peptides that are able to act against several targets have been characterized. The present work focuses on structural and functional evaluation of the peptide analogue Pa-MAP, previously isolated as an antifreeze peptide from Pleuronectes americanus. Pa-MAP showed activities against different targets such as tumoral cells in culture (CACO-2, MCF-7 and HCT-116), bacteria (Escherichia coli ATCC 8739 and Staphylococcus aureus ATCC 25923), viruses (HSV-1 and HSV-2) and fungi (Candida parapsilosis ATCC 22019, Trichophyton mentagrophytes (28d&E) and T. rubrum (327)). This peptide did not show toxicity against mammalian cells such as erythrocytes, Vero and RAW 264.7 cells. Molecular mechanism of action was related to hydrophobic residues, since only the terminal amino group is charged at pH 7 as confirmed by potentiometric titration. In order to shed some light on its structure-function relations, in vitro and in silico assays were carried out using circular dichroism and molecular dynamics. Furthermore, Pa-MAP showed partial unfolding of the peptide changes in a wide pH (3 to 11) and temperature (25 to 95°C) ranges, although it might not reach complete unfolding at 95°C, suggesting a high conformational stability. This peptide also showed a conformational transition with a partial α-helical fold in water and a full α-helical core in SDS and TFE environments. These results were corroborated by spectral data measured at 222 nm and by 50 ns dynamic simulation. In conclusion, data reported here show that Pa-MAP is a potential candidate for drug design against pathogenic microorganisms due to its structural stability and wide activity against a range of targets.

show abstract

Section: Discussionmentioning

confidence: 99%

Structural and Functional Characterization of a Multifunctional Alanine-Rich Peptide Analogue from Pleuronectes americanus

Migliolo

Silva

et al. 2012

PLoS ONE

View full text Add to dashboard Cite

show abstract

“…For example, cod cathelicidin (codCATH) is highly active against those Gram-negative bacterial species examined, but almost inactive against the Gram-positive species. It also exhibits potent antifungal activity against C. albicans [13]. In contrast, the hagfish cathelicidins are active against both Gram-positive and -negative bacteria, but inactive against Candida [15].…”

Section: Cathelicidinsmentioning

confidence: 99%

Antimicrobial Peptides from Fish

2014

View full text Add to dashboard Cite

Antimicrobial peptides (AMPs) are found widely distributed through Nature, and participate in the innate host defense of each species. Fish are a great source of these peptides, as they express all of the major classes of AMPs, including defensins, cathelicidins, hepcidins, histone-derived peptides, and a fish-specific class of the cecropin family, called piscidins. As with other species, the fish peptides exhibit broad-spectrum antimicrobial activity, killing both fish and human pathogens. They are also immunomodulatory, and their genes are highly responsive to microbes and innate immuno-stimulatory molecules. Recent research has demonstrated that some of the unique properties of fish peptides, including their ability to act even in very high salt concentrations, make them good potential targets for development as therapeutic antimicrobials. Further, the stimulation of their gene expression by exogenous factors could be useful in preventing pathogenic microbes in aquaculture.

show abstract

“…The highest expression of Plecoglossus altivelis cathelicidin was observed in most tissues at 24 hr after bacterial infection (Lu et al, ). Atlantic Cod cathelicidin showed potent antimicrobial activity against gram‐negative bacteria and fungi in low salt conditions in vitro (Broekman, Zenz, et al, ). In catfish, NK‐lysin showed an initial reduction in expression at 4 hr, after which its expression increased from 3 to 7 days after Edwardsiella ictaluri challenge (Wang et al, ).…”

Section: Discussionmentioning

confidence: 99%

Expression analysis of cathelicidin and NK‐lysin in Dabry’s sturgeon ( Acipenser dabryanus )

et al. 2019

View full text Add to dashboard Cite

Antimicrobial peptides (AMPs) are a conserved component of the innate immune response in many species. In the present study, the cDNA sequences encoding two AMPs (cathelicidin and NK‐lysin, comprising 1,576 and 606 bp, respectively) were cloned from Dabry's sturgeon (Acipenser dabryanus). Phylogenetic analysis demonstrated that the two AMPs were clustered together with homologous protein sequences from other fish. NK‐lysin was highly expressed during early embryonic development, suggesting maternal transmission. Tissue distribution analysis showed that cathelicidin had the highest expression in the liver and NK‐lysin was most abundantly expressed in the spleen. In response to Poly I:C treatment, the expression of cathelicidin was upregulated at 12 and 24 hr post induction (hpi), but downregulated at 72 hpi. NK‐lysin mRNA expression increased after treatment with Poly I:C, reaching a peak at 24 hpi. Lipopolysaccharide treatment also induced the expression of two antimicrobial peptide genes. Lipopolysaccharide treatment significantly upregulated the expression of cathelicidin at 6, 24, and 48 hpi, and upregulated NK‐lysin expression at 6 and 12 hpi. These results suggested that two AMPs could participate in the immune response induced by poly I:C or LPS stimulation.

show abstract

Functional characterization of codCath, the mature cathelicidin antimicrobial peptide from Atlantic cod (Gadus morhua)

Cited by 44 publications

References 61 publications

Structural and Functional Characterization of a Multifunctional Alanine-Rich Peptide Analogue from Pleuronectes americanus

Structural and Functional Characterization of a Multifunctional Alanine-Rich Peptide Analogue from Pleuronectes americanus

Antimicrobial Peptides from Fish

Expression analysis of cathelicidin and NK‐lysin in Dabry’s sturgeon ( Acipenser dabryanus )

Contact Info

Product

Resources

About