Abstract：
:The interaction of two cathelicidin antimicrobial peptides, LL-37 and SMAP-29, with three bacterial polysaccharides, respectively, produced by Pseudomonas aeruginosa, Burkholderia cepacia and Klebsiella pneumoniae, was investigated to identify possible mechanisms adopted by lung pathogens to escape the action of innate immunity effectors. In vitro assays indicated that the antibacterial activity of both peptides was inhibited to a variable extent by the three polysaccharides. Circular dichroism experiments showed that these induced an alpha-helical conformation in the two peptides, with the polysaccharides from K. pneumoniae and B. cepacia showing, respectively, the highest and the lowest effect. Fluorescence measurements also indicated the presence of peptide-polysaccharide interactions. A model is proposed in which the binding of peptides to the polysaccharide molecules induces, at low polysaccharide to peptide ratios, a higher order of aggregation, due to peptide-peptide interactions. Overall, these results suggest that binding of the peptides by the polysaccharides produced by lung pathogens can contribute to the impairment of peptide-based innate defenses of airway surface.
journal_name
Peptidesjournal_title
Peptidesauthors
Herasimenka Y,Benincasa M,Mattiuzzo M,Cescutti P,Gennaro R,Rizzo Rdoi
10.1016/j.peptides.2005.01.020subject
Has Abstractpub_date
2005-07-01 00:00:00pages
1127-32issue
7eissn
0196-9781issn
1873-5169pii
S0196-9781(05)00036-7journal_volume
26pub_type
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