Structural features and biological activities of the cathelicidin-derived antimicrobial peptides

Gennaro, Renato; Zanetti, Margherita

doi:10.1002/1097-0282(2000)55:1<31::aid-bip40>3.0.co;2-9

Cited by 292 publications

(184 citation statements)

References 174 publications

(208 reference statements)

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“…Although it is possible that cBD-1 is the predominant ␤-defensin expressed in these tissues, it is more likely that the inability to amplify additional defensins is due to PCR conditions used and nucleotide differences between the defensin specific primer and its potential template molecules. Nonetheless, the success of this strategy will probably permit the ultimate amplification of other defensins as well as other APs, such as cathelicidins (18). cBD-1 mRNA was abundantly transcribed in chinchilla NP mucosa, skin, and tongue mucosa as compared with ET, trachea, and lung.…”

Section: Discussionmentioning

confidence: 99%

Identification and Characterization of a Mucosal Antimicrobial Peptide Expressed by the Chinchilla (Chinchilla lanigera) Airway

Harris

Wilk

Bevins

et al. 2004

Journal of Biological Chemistry

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Cationic antimicrobial peptides (APs) are produced at mucosal surfaces and play a key role as a first line of defense against infection. To understand how APs might impact disease progression in otitis media (OM), our goal was to identify and characterize APs expressed by the epithelium lining the uppermost airway of the chinchilla, the established rodent host for the study of the bacterial-viral pathogenesis in OM. Using a molecular approach, we cloned a cDNA encoding a homolog of human ␤-defensin 3, designated chinchilla ␤-defensin-1 (cBD-1), and found by Northern analysis expression of the corresponding mRNA in nasopharyngeal and tongue mucosae as well as skin. By reverse transcription-PCR, cBD-1 mRNA was also detected in RNA isolated from trachea, lung, and Eustachian tube tissues. The predicted mature form of cBD-1, expressed as a recombinant peptide in Escherichia coli, demonstrated bactericidal activity against the three primary opportunistic pathogens of OM as well as Candida albicans. Continued study of this and other APs will allow us to determine their role in bacterial colonization of the upper airway as well as how viruses might contribute to the pathogenesis of OM by modulating AP expression.

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Section: Discussionmentioning

confidence: 99%

Identification and Characterization of a Mucosal Antimicrobial Peptide Expressed by the Chinchilla (Chinchilla lanigera) Airway

Harris

Wilk

Bevins

et al. 2004

Journal of Biological Chemistry

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“…Two evolutionary groups of antimicrobial peptides, the cathelicidins and the defensins, provide endogenous peptide-based defense against microbial invasion (11)(12)(13). Cathelicidins and defensins are produced by many cell types and have broad spectrum antimicrobial activity against bacteria, fungi, and viruses.…”

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confidence: 99%

Chicken cathelicidin-B1, an antimicrobial guardian at the mucosal M cell gateway

Goitsuka

Chen

Benyon

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

100

105

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Mucosal epithelial M cells provide an efficient portal of entry for microorganisms. Initially defined by their irregular microvilli and abundant transcytotic channels in the avian bursa of Fabricius, M cells also are found in the lymphoid follicle-associated epithelium of the mammalian appendix, Peyer's patches, and other mucosal surfacelymphoid interfaces. We describe here a previously unrecognized cathelicidin gene in chickens, chCATH-B1, that is expressed exclusively in the epithelium of the bursa of Fabricius. Like the mature peptides of previously identified cathelicidins, the carboxyl-terminal peptide of chCATH-B1 has broad antimicrobial activity against Gram-positive and Gram-negative bacteria. chCATH-B1 expression is restricted to the secretory epithelial cell neighbors of the M cells, whereas its mature peptide is transported to become concentrated on the fibrillar network surrounding basolateral surfaces of the M cells that overlie the bursal lymphoid follicles. We conclude that chCATH-B1 is well placed to serve a protective antimicrobial role at the M cell gateway.antimicrobial peptides ͉ follicle-associated epithelium ͉ innate immunity ͉ bursa of Fabricius

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“…One of them could be human cathelicidin antimicrobial peptide (hCAP-18) (6Ð8), which is produced by human neutrophils but can also be found in a variety of human tissues (9,10). hCAP-18 belongs to the protein family of cathelicidins, which have bactericidal activity by means of their highaffinity binding to the outer bacterial cell wall (8).…”

mentioning

confidence: 99%

Effects of human cathelicidin antimicrobial peptide LL‐37 on lipopolysaccharide‐induced nitric oxide release from rat aorta in vitro

Ciornei

Egesten

Bodelsson

2003

Acta Anaesthesiol Scand

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Background: Lipopolysaccharides (LPS), released by Gram‐negative bacteria, cause vascular expression of inducible nitric oxide synthase (iNOS) leading to nitric oxide (NO) production and septic shock. Human cathelicidin antimicrobial peptide (LL‐37) can bind and neutralize LPS. We wanted to study whether LL‐37 affects LPS or interleukin‐1β (IL‐1β)‐induced production, release and function of NO in intact rat aorta rings and cultured rat aorta smooth muscle cells.Methods: Isolated segments of thoracic aorta and cultured cells were incubated in the presence of LPS, LL‐37, LPS + IL‐37, IL‐1β, IL‐1β + IL‐37 or in medium alone. Smooth muscle contraction in response to phenylephrine and accumulation of the sdegradation products of NO, nitrate and nitrite, were measured on aorta segments. Levels of iNOS were assessed by Western blot and cytotoxic effects were detected by measurement of DNA fragmentation in cultured cells. Number of viable cells were determined after Trypan blue treatment.Results: Both LPS and IL‐1β reduced contractility in response to phenylephrine and increased NO production as well as iNOS expression. LL‐37 inhibited the LPS depression of vascular contractility induced only by LPS. LL‐37 reduced both the LPS‐ and IL‐1β‐induced NO production and iNOS expression. LL‐37 at high concentrations induced DNA fragmentation and decreased the number of living cells.Conclusion: IL‐37 reduces NO production induced by LPS and IL‐1β. The reduction does not seem to result only from neutralization of LPS but also from a cytotoxic effect, possibly via induction of apoptosis.

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Structural features and biological activities of the cathelicidin-derived antimicrobial peptides

Cited by 292 publications

References 174 publications

Identification and Characterization of a Mucosal Antimicrobial Peptide Expressed by the Chinchilla (Chinchilla lanigera) Airway

Identification and Characterization of a Mucosal Antimicrobial Peptide Expressed by the Chinchilla (Chinchilla lanigera) Airway

Chicken cathelicidin-B1, an antimicrobial guardian at the mucosal M cell gateway

Effects of human cathelicidin antimicrobial peptide LL‐37 on lipopolysaccharide‐induced nitric oxide release from rat aorta in vitro

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