Interaction of antimicrobial peptides with bacterial polysaccharides from lung pathogens

Herasimenka, Yury; Benincasa, Monica; Mattiuzzo, Maura; Cescutti, Paola; Gennaro, Renato; Rizzo, Roberto

doi:10.1016/j.peptides.2005.01.020

Cited by 59 publications

(46 citation statements)

References 20 publications

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“…It also seems to make the peptides rather "sticky," so that they strongly interact with medium components in a manner that sequesters them ("S-form"), considerably reducing activity in full medium (11) and this may also explain the lowering of the LL-37 antimicrobial activity in serum (36) or lung surfactant (37). It could also provide a means for bacteria to develop resistance to the direct antimicrobial activity of the peptides, via secretion of exopolysaccharides (38). Peptides of the cercopithecinae RL-37 group instead exist exclusively in the F-form in bulk solution, having both a low tendency to structure/aggregate in solution or to bind to medium components.…”

Section: Discussionmentioning

confidence: 99%

Evolution of the Primate Cathelicidin

Zelezetsky

Pontillo

Puzzi

et al. 2006

Journal of Biological Chemistry

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Cathelicidin genes homologous to the human CAMP gene, coding for the host defense peptide LL-37, have been sequenced and analyzed in 20 primate species, including Great Apes, hylobatidae, cercopithecidae, callithricidae, and cebidae. The region corresponding to the putative mature antimicrobial peptide is subject to a strong selective pressure for variation, with evidence for positive selection throughout the phylogenetic tree relating the peptides, which favors alterations in the charge while little affecting overall hydrophobicity or amphipathicity. Selected peptides were chemically synthesized and characterized, and two distinct types of behavior were observed. Macaque and leaf-eating monkey RL-37 peptides, like other helical antimicrobial peptides found in insect, frog, and mammalian species, were unstructured in bulk solution and had a potent, salt and medium independent antimicrobial activity in vitro, which may be the principal function also in vivo. Human LL-37 and the orangutan, hylobates, and callithrix homologues instead showed a salt-dependent structuring and likely aggregation in bulk solution that affected antimicrobial activity and its medium dependence. The two types of peptides differ also in their interaction with host cells. The evolution of these peptides has thus resulted in distinct mechanisms of action that affect the direct antimicrobial activity and may also modulate accessory antimicrobial functions due to interactions with host cells.

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Section: Discussionmentioning

confidence: 99%

Evolution of the Primate Cathelicidin

Zelezetsky

Pontillo

Puzzi

et al. 2006

Journal of Biological Chemistry

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“…Accordingly, ApoA-1 was found to specifically inhibit the bactericidal ability of cathelicidin LL-37 (47). Many other factors present at infection sites, such as mucins, negatively charged DNA, and F-actin can compromise CAP bactericidal activity as well (8,27,48). To assess the D2S potential to kill bacteria in different environments, using a Fuji Film LAS-300 system, we evaluated changes of P. aeruginosa Xen5 luminescence (ϳ10 8 CFU/ml) in PBS or PBS mixed with 50% of plasma, ascites, cerebrospinal fluid, saliva, or bronchoalveolar lavage (BAL) fluid at different time points, up to 6 h after D2S addition (10 and 30 M).…”

Section: Methodsmentioning

confidence: 99%

Combined Antibacterial and Anti-Inflammatory Activity of a Cationic Disubstituted Dexamethasone-Spermine Conjugate

Bucki

Leszczyńska²,

Byfield

et al. 2010

Antimicrob Agents Chemother

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The rising number of antibiotic-resistant bacterial strains represents an emerging health problem that has motivated efforts to develop new antibacterial agents. Endogenous cationic antibacterial peptides (CAPs) that are produced in tissues exposed to the external environment are one model for the design of novel antibacterial compounds. Here, we report evidence that disubstituted dexamethasone-spermine (D2S), a cationic corticosteroid derivative initially identified as a by-product of synthesis of dexamethasone-spermine (

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“…Since EPS can neutralize ROS and render neutrophils unable to kill Bcc bacteria by oxidative means, the antimicrobial action of those cells will be entirely dependent on the non-oxidative cationic antimicrobial peptides. However, Bcc bacteria are also resistant to non-oxidative antimicrobial peptides and this ability was attributed to the presence of EPS (Herasimenka et al, 2005). In fact, due to the negative charge given by acetyl substituents, cepacian was shown to interact with positively charged antimicrobial peptides forming complexes that lower the antimicrobial peptides biological activity (Herasimenka et al, 2005).…”

Section: Cepacian As a Virulence Factormentioning

confidence: 99%

“…However, Bcc bacteria are also resistant to non-oxidative antimicrobial peptides and this ability was attributed to the presence of EPS (Herasimenka et al, 2005). In fact, due to the negative charge given by acetyl substituents, cepacian was shown to interact with positively charged antimicrobial peptides forming complexes that lower the antimicrobial peptides biological activity (Herasimenka et al, 2005). If EPS produced by Bcc can both neutralize oxidative species and interact with non-oxidative antimicrobial peptides, then it might be an important virulence factor, since it would leave neutrophils without means to clear the offending bacteria.…”

Section: Cepacian As a Virulence Factormentioning

confidence: 99%