Deficiency of antibacterial peptides in patients with morbus Kostmann: an observation study

Pütsep, Katrin; Carlsson, Göran; Boman, Hans G.; Andersson, Mats

doi:10.1016/s0140-6736(02)11201-3

Cited by 452 publications

(388 citation statements)

References 27 publications

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“…In addition, a lack of cathelicidin and other antimicrobial peptides correlates with increased infections in patients with atopic dermatitis or Kostman syndrome (19,35). These observations provide compelling evidence that cathelicidins act as innate antibiotics to kill or inhibit microbes.…”

Section: Discussionmentioning

confidence: 93%

Cathelicidin Antimicrobial Peptides Block Dendritic Cell TLR4 Activation and Allergic Contact Sensitization

Nardo

Braff

Taylor

et al. 2007

The Journal of Immunology

140

117

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Cathelicidins are antimicrobial peptides of the innate immune system that establish an antimicrobial barrier at epithelial interfaces and have been proposed to have a proinflammatory function. We studied the role of cathelicidin in allergic contact dermatitis, a model requiring dendritic cells of the innate immune response and T cells of the adaptive immune response. Deletion of the murine cathelicidin gene Cnlp enhanced an allergic contact response, whereas local administration of cathelicidin before sensitization inhibited the allergic response. Cathelicidins inhibited TLR4 but not TLR2 mediated induction of dendritic cell maturation and cytokine release, and this inhibition was associated with an alteration of cell membrane function and structure. Further analysis in vivo connected these observations because inhibition of sensitization by exogenous cathelicidin was dependent on the presence of functional TLR4. These observations provide evidence that cathelicidin antimicrobial peptides mediate an anti-inflammatory response in part by their activity at the membrane.

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Section: Discussionmentioning

confidence: 93%

Cathelicidin Antimicrobial Peptides Block Dendritic Cell TLR4 Activation and Allergic Contact Sensitization

Nardo

Braff

Taylor

et al. 2007

The Journal of Immunology

140

117

View full text Add to dashboard Cite

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“…The sAMPs play a pivotal role in maintaining mucosal immune integrity (Allgrove et al 2008;Bals and Hiemstra 2004;Papacosta and Nassis 2011;West et al 2006) by working synergistically to curtail invading bacteria, viruses, and fungi (De Smet and Contreras 2005;Radek and Gallo 2007;West et al 2006) and are vital in both the prevention and clearance of many types of infection (Bowdish et al 2005;Davison et al 2009;West et al 2006). In particular, infections of the oral cavity and upper respiratory tract (URTI) are associated with depressed levels of sAMPs (Table 1) (Bartlett et al 2008;Bishop and Gleeson 2009;Dale et al 2006;Doss et al 2010;Laube et al 2006;Putsep et al 2002;Tanida et al 2003;Tao et al 2005;Ueta et al 2000;West et al 2006), highlighting their prominent role in first--line immune defense.…”

Section: Introductionmentioning

confidence: 99%

Fitness level impacts salivary antimicrobial protein responses to a single bout of cycling exercise

et al. 2015

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“…The only known cathelicidin peptide expressed in humans is LL-37, a 37-aa C-terminal domain of human (h)CAP-18 (4). The importance of cathelicidins as an effective defense against pathogenic microorganisms is illustrated by the high occurrence of periodontal disease in patients with severe congenital neutropenia accompanied by a deficiency of LL-37 in saliva (5), as well as an animal study showing severe bacterial skin infections in mice lacking murine cathelicidin-related CAPs (6). Overexpression of hCAP-18 after pulmonary gene transfer in mice results in increased Pseudomonas aeruginosa clearance in the course of pulmonary challenge (7).…”

mentioning

confidence: 99%

Cathelicidin LL-37 Increases Lung Epithelial Cell Stiffness, Decreases Transepithelial Permeability, and Prevents Epithelial Invasion by Pseudomonas aeruginosa

Byfield

Kowalski

Cruz

et al. 2011

The Journal of Immunology

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In addition to its antibacterial activity, the cathelicidin-derived LL-37 peptide induces multiple immunomodulatory effects on host cells. Atomic force microscopy, F-actin staining with phalloidin, passage of FITC-conjugated dextran through a monolayer of lung epithelial cells, and assessment of bacterial outgrowth from cells subjected to Pseudomonas aeruginosa infection were used to determine LL-37’s effect on epithelial cell mechanical properties, permeability, and bacteria uptake. A concentration-dependent increase in stiffness and F-actin content in the cortical region of A549 cells and primary human lung epithelial cells was observed after treatment with LL-37 (0.5–5 μM), sphingosine 1-phosphate (1 μM), or LPS (1 μg/ml) or infection with PAO1 bacteria. Other cationic peptides, such as RK-31, KR-20, or WLBU2, and the antibacterial cationic steroid CSA-13 did not reproduce the effect of LL-37. A549 cell pretreatment with WRW4, an antagonist of the transmembrane formyl peptide receptor-like 1 protein attenuated LL-37’s ability to increase cell stiffness. The LL-37–mediated increase in cell stiffness was accompanied by a decrease in permeability and P. aeruginosa uptake by a confluent monolayer of polarized normal human bronchial epithelial cells. These results suggested that the antibacterial effect of LL-37 involves an LL-37–dependent increase in cell stiffness that prevents epithelial invasion by bacteria.

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Deficiency of antibacterial peptides in patients with morbus Kostmann: an observation study

Cited by 452 publications

References 27 publications

Cathelicidin Antimicrobial Peptides Block Dendritic Cell TLR4 Activation and Allergic Contact Sensitization

Cathelicidin Antimicrobial Peptides Block Dendritic Cell TLR4 Activation and Allergic Contact Sensitization

Fitness level impacts salivary antimicrobial protein responses to a single bout of cycling exercise

Cathelicidin LL-37 Increases Lung Epithelial Cell Stiffness, Decreases Transepithelial Permeability, and Prevents Epithelial Invasion by Pseudomonas aeruginosa

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