Limits...
Identification of a novel cathelicidin antimicrobial peptide from ducks and determination of its functional activity and antibacterial mechanism.

Gao W, Xing L, Qu P, Tan T, Yang N, Li D, Chen H, Feng X - Sci Rep (2015)

Bottom Line: The cDNA sequence of dCATH encodes a predicted 146-amino-acid polypeptide composed of a 17-residue signal peptide, a 109-residue conserved cathelin domain and a 20-residue mature peptide.Phylogenetic analysis demonstrated that dCATH is highly divergent from other avian peptides.The effects on bacterial outer and inner membranes, as examined by scanning electron microscope and transmission electron microscopy, indicate that dCATH kills microbial cells by increasing permeability, causing a loss of membrane integrity.

View Article: PubMed Central - PubMed

Affiliation: College of Animal Science and Technology, Northeast Agricultural University, Harbin 150030, P.R. China.

ABSTRACT
The family of antimicrobial peptide, cathelicidins, which plays important roles against infections in animals, has been identified from many species. Here, we identified a novel avian cathelicidin ortholog from ducks and named dCATH. The cDNA sequence of dCATH encodes a predicted 146-amino-acid polypeptide composed of a 17-residue signal peptide, a 109-residue conserved cathelin domain and a 20-residue mature peptide. Phylogenetic analysis demonstrated that dCATH is highly divergent from other avian peptides. The α-helical structure of the peptide exerted strong antimicrobial activity against a broad range of bacteria in vitro, with most minimum inhibitory concentrations in the range of 2 to 4 μM. Moreover, dCATH also showed cytotoxicity, lysing 50% of mammalian erythrocytes in the presence or absence of 10% fetal calf serum at concentrations of 32 μM or 20 μM and killing 50% HaCaT cells at a concentration of 10 μM. The effects on bacterial outer and inner membranes, as examined by scanning electron microscope and transmission electron microscopy, indicate that dCATH kills microbial cells by increasing permeability, causing a loss of membrane integrity.

No MeSH data available.


Related in: MedlinePlus

(A) Multiple sequence alignment analysis of the duck dCATH with representative avian cathelicidins. dCATH is aligned with classic cathelicidins (CATH1-3 (Phasianus colchicus), CATH1-3 (Coturnix coturnix), fowlicidin1-3 (Gallus), CMAP (Gallus), CLCATH2-3 (Columba livia), Cathelicidin1-2 (Anas platyrhynchos)). (B,C) Phylogenetic analysis of dCATH and other avian cathelicidins on the basis of the complete peptide (B) and mature domain (C). The phylogenetic dendrogram was constructed by the Neighbor-joining method based on the proportion difference of aligned amino acid sites of the sequence. Only branches supported by a bootstrap value (expressed as percentage of 1000 bootstrap samples supporting the branch) are shown at the branching points.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC4660463&req=5

f2: (A) Multiple sequence alignment analysis of the duck dCATH with representative avian cathelicidins. dCATH is aligned with classic cathelicidins (CATH1-3 (Phasianus colchicus), CATH1-3 (Coturnix coturnix), fowlicidin1-3 (Gallus), CMAP (Gallus), CLCATH2-3 (Columba livia), Cathelicidin1-2 (Anas platyrhynchos)). (B,C) Phylogenetic analysis of dCATH and other avian cathelicidins on the basis of the complete peptide (B) and mature domain (C). The phylogenetic dendrogram was constructed by the Neighbor-joining method based on the proportion difference of aligned amino acid sites of the sequence. Only branches supported by a bootstrap value (expressed as percentage of 1000 bootstrap samples supporting the branch) are shown at the branching points.

Mentions: The predicted polypeptide was contrasted with classic cathelicidins from different avian species, displayed characteristic features of cathelicidins and showed high similarity (Fig. 2A). The avian multi-sequence alignments were performed based on the proregion and mature domain. Surprisingly, the cathelicidins share a high degree of similarity, particularly in the proregion sequence region, implying that cathelicidins may be more closely related.


Identification of a novel cathelicidin antimicrobial peptide from ducks and determination of its functional activity and antibacterial mechanism.

Gao W, Xing L, Qu P, Tan T, Yang N, Li D, Chen H, Feng X - Sci Rep (2015)

(A) Multiple sequence alignment analysis of the duck dCATH with representative avian cathelicidins. dCATH is aligned with classic cathelicidins (CATH1-3 (Phasianus colchicus), CATH1-3 (Coturnix coturnix), fowlicidin1-3 (Gallus), CMAP (Gallus), CLCATH2-3 (Columba livia), Cathelicidin1-2 (Anas platyrhynchos)). (B,C) Phylogenetic analysis of dCATH and other avian cathelicidins on the basis of the complete peptide (B) and mature domain (C). The phylogenetic dendrogram was constructed by the Neighbor-joining method based on the proportion difference of aligned amino acid sites of the sequence. Only branches supported by a bootstrap value (expressed as percentage of 1000 bootstrap samples supporting the branch) are shown at the branching points.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4660463&req=5

f2: (A) Multiple sequence alignment analysis of the duck dCATH with representative avian cathelicidins. dCATH is aligned with classic cathelicidins (CATH1-3 (Phasianus colchicus), CATH1-3 (Coturnix coturnix), fowlicidin1-3 (Gallus), CMAP (Gallus), CLCATH2-3 (Columba livia), Cathelicidin1-2 (Anas platyrhynchos)). (B,C) Phylogenetic analysis of dCATH and other avian cathelicidins on the basis of the complete peptide (B) and mature domain (C). The phylogenetic dendrogram was constructed by the Neighbor-joining method based on the proportion difference of aligned amino acid sites of the sequence. Only branches supported by a bootstrap value (expressed as percentage of 1000 bootstrap samples supporting the branch) are shown at the branching points.
Mentions: The predicted polypeptide was contrasted with classic cathelicidins from different avian species, displayed characteristic features of cathelicidins and showed high similarity (Fig. 2A). The avian multi-sequence alignments were performed based on the proregion and mature domain. Surprisingly, the cathelicidins share a high degree of similarity, particularly in the proregion sequence region, implying that cathelicidins may be more closely related.

Bottom Line: The cDNA sequence of dCATH encodes a predicted 146-amino-acid polypeptide composed of a 17-residue signal peptide, a 109-residue conserved cathelin domain and a 20-residue mature peptide.Phylogenetic analysis demonstrated that dCATH is highly divergent from other avian peptides.The effects on bacterial outer and inner membranes, as examined by scanning electron microscope and transmission electron microscopy, indicate that dCATH kills microbial cells by increasing permeability, causing a loss of membrane integrity.

View Article: PubMed Central - PubMed

Affiliation: College of Animal Science and Technology, Northeast Agricultural University, Harbin 150030, P.R. China.

ABSTRACT
The family of antimicrobial peptide, cathelicidins, which plays important roles against infections in animals, has been identified from many species. Here, we identified a novel avian cathelicidin ortholog from ducks and named dCATH. The cDNA sequence of dCATH encodes a predicted 146-amino-acid polypeptide composed of a 17-residue signal peptide, a 109-residue conserved cathelin domain and a 20-residue mature peptide. Phylogenetic analysis demonstrated that dCATH is highly divergent from other avian peptides. The α-helical structure of the peptide exerted strong antimicrobial activity against a broad range of bacteria in vitro, with most minimum inhibitory concentrations in the range of 2 to 4 μM. Moreover, dCATH also showed cytotoxicity, lysing 50% of mammalian erythrocytes in the presence or absence of 10% fetal calf serum at concentrations of 32 μM or 20 μM and killing 50% HaCaT cells at a concentration of 10 μM. The effects on bacterial outer and inner membranes, as examined by scanning electron microscope and transmission electron microscopy, indicate that dCATH kills microbial cells by increasing permeability, causing a loss of membrane integrity.

No MeSH data available.


Related in: MedlinePlus