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. 2008 Sep 16;3(9):e3217.
doi: 10.1371/journal.pone.0003217.

"V体育2025版" Snake cathelicidin from Bungarus fasciatus is a potent peptide antibiotics

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Snake cathelicidin from Bungarus fasciatus is a potent peptide antibiotics

Yipeng Wang et al. PLoS One. .

Abstract

Background: Cathelicidins are a family of antimicrobial peptides acting as multifunctional effector molecules of innate immunity, which are firstly found in mammalians VSports手机版. Recently, several cathelicidins have also been found from chickens and fishes. No cathelicidins from other non-mammalian vertebrates have been reported. .

Principal findings: In this work, a cathelicidin-like antimicrobial peptide named cathelicidin-BF has been purified from the snake venoms of Bungarus fasciatus and its cDNA sequence was cloned from the cDNA library, which confirm the presence of cathelicidin in reptiles. As other cathelicidins, the precursor of cathelicidin-BF has cathelin-like domain at the N terminus and carry the mature cathelicidin-BF at the C terminus, but it has an atypical acidic fragment insertion between the cathelin-like domain and the C-terminus. The acidic fragment is similar to acidic domains of amphibian antimicrobial precursors. Phylogenetic analysis revealed that the snake cathelicidin had the nearest evolution relationship with platypus cathelicidin. The secondary structure of cathelicidin-BF investigated by CD and NMR spectroscopy in the presence of the helicogenic solvent TFE is an amphipathic alpha-helical conformation as many other cathelicidins. The antimicrobial activities of cathelicidin BF against forty strains of microorganisms were tested. Cathelicidin-BF efficiently killed bacteria and some fungal species including clinically isolated drug-resistance microorganisms. It was especially active against Gram-negative bacteria. Furthermore, it could exert antimicrobial activity against some saprophytic fungus. No hemolytic and cytotoxic activity was observed at the dose of up to 400 microg/ml. Cathelicidin-BF could exist stably in the mice plasma for at least 2. 5 hours. V体育安卓版.

Conclusion: Discovery of snake cathelicidin with atypical structural and functional characterization offers new insights on the evolution of cathelicidins. Potent, broad spectrum, salt-independent antimicrobial activities make cathelicidin-BF an excellent candidate for clinical or agricultural antibiotics V体育ios版. .

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Conflict of interest statement

Competing Interests: The authors have declared that no competing interests exist.

Figures

Figure 1
Figure 1. The cDNA sequence encoding cathelicidin-BF and the predicted precursor amino acid sequence.
The amino sequence of purified cathelicidin-BF is boxed. The stop codon is indicated by a star (*). The potential polyadentlation signal (AATAAA) is underlined.
Figure 2
Figure 2. Multiple sequence alignment of snake cathelicidin with other representative cathelicidins.
Cathelicidin-BF precursor is aligned with porcine, bovine, human, chicken and hagfish cathelicdins. Dashes are inserted to optimize the alignment, and conserved residues are shaded. Two intramolecular disulfide bonds in the cathelin pro-sequence are shown. Mature cathelicinds are underlined, and their net charge (in parenthesis) and length are also indicated. The acidic fragment insertion in cathelicidin-BF is boxed.
Figure 3
Figure 3. Phylogenetic analysis of cathelicidins.
Phylogenetic dendrogram obtained by neighbour-joining analysis based on the proportion difference (p-distance) of aligned amino acid sites of the full-length peptide sequences. Only bootstrap values >50% (expressed as percentages of 1000 resamplings) are shown at branching points. Snake cathelicidin-BF is boxed.
Figure 4
Figure 4. RT-PCR analysis of cathelicidin gene expression pattern in various snake tissues using gene-specific primers with actin as a control.

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