Affordable Access

deepdyve-link deepdyve-link
Publisher Website

Novel cathelicidin-derived antimicrobial peptides from Equus asinus.

Authors
  • Lu, Zekuan
  • Wang, Yipeng
  • Zhai, Lei
  • Che, Qiaolin
  • Wang, Hui
  • Du, Shuyuan
  • Wang, Duo
  • Feng, Feifei
  • Liu, Jingze
  • Lai, Ren
  • Yu, Haining
Type
Published Article
Journal
FEBS Journal
Publisher
Wiley (Blackwell Publishing)
Publication Date
May 01, 2010
Volume
277
Issue
10
Pages
2329–2339
Identifiers
DOI: 10.1111/j.1742-4658.2010.07648.x
PMID: 20423460
Source
Medline
License
Unknown

Abstract

In the present study, EA-CATH1 and EA-CATH2 were identified from a constructed lung cDNA library of donkey (Equus asinus) as members of cathelicidin-derived antimicrobial peptides, using a nested PCR-based cloning strategy. Composed of 25 and 26 residues, respectively, EA-CATH1 and EA-CATH2 are smaller than most other cathelicidins and have no sequence homology to other cathelicidins identified to date. Chemically synthesized EA-CATH1 exerted potent antimicrobial activity against most of the 32 strains of bacteria and fungi tested, especially the clinically isolated drug-resistant strains, and minimal inhibitory concentration values against Gram-positive bacteria were mostly in the range of 0.3-2.4 microg mL(-1). EA-CATH1 showed an extraordinary serum stability and no haemolytic activity against human erythrocytes in a dose up to 20 microg mL(-1). CD spectra showed that EA-CATH1 mainly adopts an alpha-helical conformation in a 50% trifluoroethanol/water solution, but a random coil in aqueous solution. Scanning electron microscope observations of Staphylococcus aureus (ATCC2592) treated with EA-CATH1 demonstrated that EA-CATH could cause rapid disruption of the bacterial membrane, and in turn lead to cell lysis. This might explain the much faster killing kinetics of EA-CATH1 than conventional antibiotics revealed by killing kinetics data. In the presence of CaCl(2), EA-CATH1 exerted haemagglutination activity, which might potentiate an inhibition against the bacterial polyprotein interaction with the host erythrocyte surface, thereby possibly restricting bacterial colonization and spread.

Report this publication

Statistics

Seen <100 times