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Journal articles on the topic 'LL37'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 February 2022

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1

Lande, Roberto, Immacolata Pietraforte, Anna Mennella, Raffaella Palazzo, Francesca Romana Spinelli, Konstantinos Giannakakis, Francesca Spadaro, et al. "Complementary Effects of Carbamylated and Citrullinated LL37 in Autoimmunity and Inflammation in Systemic Lupus Erythematosus." International Journal of Molecular Sciences 22, no. 4 (February 6, 2021): 1650. http://dx.doi.org/10.3390/ijms22041650.

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LL37 acts as T-cell/B-cell autoantigen in Systemic lupus erythematosus (SLE) and psoriatic disease. Moreover, when bound to “self” nucleic acids, LL37 acts as “danger signal,” leading to type I interferon (IFN-I)/pro-inflammatory factors production. T-cell epitopes derived from citrullinated-LL37 act as better antigens than unmodified LL37 epitopes in SLE, at least in selected HLA-backgrounds, included the SLE-associated HLA-DRB1*1501/HLA-DRB5*0101 backgrounds. Remarkably, while “fully-citrullinated” LL37 acts as better T-cell-stimulator, it loses DNA-binding ability and the associated “adjuvant-like” properties. Since LL37 undergoes a further irreversible post-translational modification, carbamylation and antibodies to carbamylated self-proteins other than LL37 are present in SLE, here we addressed the involvement of carbamylated-LL37 in autoimmunity and inflammation in SLE. We detected carbamylated-LL37 in SLE-affected tissues. Most importantly, carbamylated-LL37-specific antibodies and CD4 T-cells circulate in SLE and both correlate with disease activity. In contrast to “fully citrullinated-LL37,” “fully carbamylated-LL37” maintains both innate and adaptive immune-cells’ stimulatory abilities: in complex with DNA, carbamylated-LL37 stimulates plasmacytoid dendritic cell IFN-α production and B-cell maturation into plasma cells. Thus, we report a further example of how different post-translational modifications of a self-antigen exert complementary effects that sustain autoimmunity and inflammation, respectively. These data also show that T/B-cell responses to carbamylated-LL37 represent novel SLE disease biomarkers.

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2

Palazzo, Raffaella, Immacolata Pietraforte, Carlo Chizzolini, Roberto Lande, and Loredana Frasca. "RB139, RB140, RB141 and RB142 antibodies recognize human citrullinated LL37 by ELISA." Antibody Reports 3, no. 3 (May 26, 2020): e189. http://dx.doi.org/10.24450/journals/abrep.2020.e189.

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LL37 is a natural antibiotic, active against bacteria and fungi and some viruses. Here we show that three monoclonal antibodies (RB139, RB141, and RB142) are exclusively specific for citrullinated LL37, whereas RB140 recognizes both native LL37 and cit-LL37. None recognizes LL37 modified by carbamylation. These antibodies can represent previously unavailable tools to detect the presence of citrullinated LL37 in body fluids by ELISA in the course of autoimmune and infectious diseases.

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3

Lande, Roberto, Stefano Alivernini, Barbara Tolusso, Francesca Spadaro, Mario Falchi, Raffaella Palazzo, Immacolata Pietraforte, et al. "Monoclonal antibodies RB139 and RB142 recognize citrullinated LL37 by immunofluorescence in histological sections in Systemic lupus erythematosus (SLE) and Rheumatoid arthritis (RA)." Antibody Reports 3, no. 4 (July 27, 2020): e236. http://dx.doi.org/10.24450/journals/abrep.2020.e236.

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LL37 is a natural antibiotic, but is also a molecule with pleiotropic functions as well as an immune-modulator. LL37 is produced by epithelial cells and is present in neutrophils’ granules. LL37 alone, or in complex with DNA, can activate inflammatory pathways in psoriasis, systemic lupus erythematosus (SLE) and rheumatoid arthritis (RA). In this work, we describe the capacity of two recombinant monoclonal antibodies, RB139 and RB142, previously shown to specifically recognize LL37 in its citrullinated form (cit-LL37) by ELISA, to detect LL37 by immunofluorescence in human inflamed tissues derived from SLE and RA patients. Such antibodies represent previously unavailable tools to detect the presence, the citrullinated state and the exact localization of cit-LL37 in human tissues in health and disease.

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4

Lande, Roberto, Stefano Alivernini, Barbara Tolusso, Francesca Spadaro, Mario Falchi, Raffaella Palazzo, Immacolata Pietraforte, et al. "RB137 recognizes LL37 in neutrophil-extracellular trap-like (NET) structures in systemic lupus erythematosus and rheumatoid arthritis inflamed tissues by immunofluorescence in histological sections." Antibody Reports 3, no. 4 (July 27, 2020): e235. http://dx.doi.org/10.24450/journals/abrep.2020.e235.

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Besides being a natural antibiotic, the human cathelicidin LL37, produced by epithelial cells and neutrophils, is an important immune-modulator. LL37 alone, or in complex with DNA, can activate inflammatory pathways in psoriasis, Systemic Lupus Erythematosus (SLE) and Rheumatoid Arthritis (RA). In this work, we describe the capacity of the recombinant monoclonal antibody RB137, previously shown to specifically recognize LL37 in its native form by ELISA, to detect LL37 by immunofluorescence in human tissues derived from SLE and RA patients. In these tissues, LL37 decorates DNA filaments resembling neutrophil-extracellular-trap (NET) structures. This antibody represents a valuable tool to detect the presence, the native state and the exact localization of LL37 in human tissues in health and disease.

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5

Palazzo, Raffaella, Immacolata Pietraforte, Carlo Chizzolini, Roberto Lande, and Loredana Frasca. "RB137 and RB138 antibodies recognize human cathelicidin LL37 by ELISA." Antibody Reports 3, no. 3 (May 26, 2020): e188. http://dx.doi.org/10.24450/journals/abrep.2020.e188.

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LL37 is a cationic antimicrobial peptide (AMP), which can undergo post-translational modifications (PTM), such as citrullination and carbamylation. We demonstrate here that recombinant antibodies RB137 and RB138 are specific for native LL37 and do not recognize modified LL37 (citrullinated and carbamylated). They thus represent tools to assess the presence of native, unmodified LL37 in body fluids by ELISA.

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6

Lande, Roberto, Raffaella Palazzo, Philippe Hammel, Immacolata Pietraforte, Isabelle Surbeck, Michel Gilliet, Carlo Chizzolini, and Loredana Frasca. "Generation of Monoclonal Antibodies Specific for Native LL37 and Citrullinated LL37 That Discriminate the Two LL37 Forms in the Skin and Circulation of Cutaneous/Systemic Lupus Erythematosus and Rheumatoid Arthritis Patients." Antibodies 9, no. 2 (May 11, 2020): 14. http://dx.doi.org/10.3390/antib9020014.

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Human cathelicidin LL37 is a cationic antimicrobial peptide active against bacteria and viruses and exerting immune modulatory functions. LL37 can be also a target of autoreactive B- and T-lymphocytes in autoimmune settings. Irreversible post-translational modifications, such as citrullination and carbamylation, mainly occurring at the level of cationic amino acids arginine and lysine, can affect the inflammatory properties and reduce antibacterial effects. Moreover, these modifications could be implicated in the rupture of immune tolerance to LL37 in chronic conditions such as psoriatic disease and cutaneous lupus (LE)/systemic lupus erythematosus (SLE). Here, we describe the generation and fine specificity of six recombinant antibodies (MRB137–MRB142), produced as a monovalent mouse antibody with the antigen-binding scFv portion fused to a mouse IgG2a Fc, and their ability to recognize either native or citrullinated LL37 (cit-LL37) and not cross-react to carbamylated LL37. By using these antibodies, we detected native LL37 or cit-LL37 in SLE and rheumatoid arthritis (RA) sera, and in LE skin, by ELISA and immunohistochemistry, respectively. Such antibodies represent previously unavailable and useful tools to address relationships between the presence of post-translational modified LL37 and the immune system status (in terms of innate/adaptive responses activation) and the clinical characteristics of patients affected by chronic immune-mediated diseases or infectious diseases.

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7

Ganguly, Dipyaman, Georgios Chamilos, Roberto Lande, Josh Gregorio, Stephan Meller, Valeria Facchinetti, Bernhard Homey, Franck J. Barrat, Tomasz Zal, and Michel Gilliet. "Self-RNA–antimicrobial peptide complexes activate human dendritic cells through TLR7 and TLR8." Journal of Experimental Medicine 206, no. 9 (August 24, 2009): 1983–94. http://dx.doi.org/10.1084/jem.20090480.

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Dendritic cell (DC) responses to extracellular self-DNA and self-RNA are prevented by the endosomal seclusion of nucleic acid–recognizing Toll-like receptors (TLRs). In psoriasis, however, plasmacytoid DCs (pDCs) sense self-DNA that is transported to endosomal TLR9 upon forming a complex with the antimicrobial peptide LL37. Whether LL37 also interacts with extracellular self-RNA and how this may contribute to DC activation in psoriasis is not known. Here, we report that LL37 can bind self-RNA released by dying cells, protect it from extracellular degradation, and transport it into endosomal compartments of DCs. In pDC, self-RNA–LL37 complexes activate TLR7 and, like self-DNA–LL37 complexes, trigger the secretion of IFN-α without inducing maturation or the production of IL-6 and TNF-α. In contrast to self-DNA–LL37 complexes, self-RNA–LL37 complexes also trigger the activation of classical myeloid DCs (mDCs). This occurs through TLR8 and leads to the production of TNF-α and IL-6, and the differentiation of mDCs into mature DCs. We also found that self-RNA–LL37 complexes are present in psoriatic skin lesions and are associated with mature mDCs in vivo. Our results demonstrate that the cationic antimicrobial peptide LL37 converts self-RNA into a trigger of TLR7 and TLR8 in human DCs, and provide new insights into the mechanism that drives the auto-inflammatory responses in psoriasis.

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8

Wu, Fan, and Cheemeng Tan. "Dead bacterial absorption of antimicrobial peptides underlies collective tolerance." Journal of The Royal Society Interface 16, no. 151 (February 2019): 20180701. http://dx.doi.org/10.1098/rsif.2018.0701.

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The collective tolerance towards antimicrobial peptides (APs) is thought to occur primarily through mechanisms associated with live bacterial cells. In contrast to the focus on live cells, we discover that the LL37 antimicrobial peptide kills a subpopulation of Escherichia coli , forming dead cells that absorb the remaining LL37 from the environment. Combining mathematical modelling with population and single-cell experiments, we show that bacteria absorb LL37 at a timing that coincides with the permeabilization of their cytoplasmic membranes. Furthermore, we show that one bacterial strain can absorb LL37 and protect another strain from killing by LL37. Finally, we demonstrate that the absorption of LL37 by dead bacteria can be reduced using a peptide adjuvant. In contrast to the known collective tolerance mechanisms, we show that the absorption of APs by dead bacteria is a dynamic process that leads to emergent population behaviour.

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9

Salamah, Maryam F., Divyashree Ravishankar, Xenia Kodji, Leonardo A. Moraes, Harry F. Williams, Thomas M. Vallance, Dina A. Albadawi, et al. "The endogenous antimicrobial cathelicidin LL37 induces platelet activation and augments thrombus formation." Blood Advances 2, no. 21 (November 9, 2018): 2973–85. http://dx.doi.org/10.1182/bloodadvances.2018021758.

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Abstract Platelet-associated complications including thrombosis, thrombocytopenia, and hemorrhage are commonly observed during various inflammatory diseases such as sepsis, inflammatory bowel disease, and psoriasis. Despite the reported evidence on numerous mechanisms/molecules that may contribute to the dysfunction of platelets, the primary mechanisms that underpin platelet-associated complications during inflammatory diseases are not fully established. Here, we report the discovery of formyl peptide receptor 2, FPR2/ALX, in platelets and its primary role in the development of platelet-associated complications via ligation with its ligand, LL37. LL37 acts as a powerful endogenous antimicrobial peptide, but it also regulates innate immune responses. We demonstrate the impact of LL37 in the modulation of platelet reactivity, hemostasis, and thrombosis. LL37 activates a range of platelet functions, enhances thrombus formation, and shortens the tail bleeding time in mice. By utilizing a pharmacological inhibitor and Fpr2/3 (an ortholog of human FPR2/ALX)–deficient mice, the functional dependence of LL37 on FPR2/ALX was determined. Because the level of LL37 is increased in numerous inflammatory diseases, these results point toward a critical role for LL37 and FPR2/ALX in the development of platelet-related complications in such diseases. Hence, a better understanding of the clinical relevance of LL37 and FPR2/ALX in diverse pathophysiological settings will pave the way for the development of improved therapeutic strategies for a range of thromboinflammatory diseases.

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10

Chang, Hao-Teng, Pei-Wen Tsai, Hsin-Hui Huang, Yu-Shu Liu, Tzu-Shan Chien, and Chung-Yu Lan. "LL37 and hBD-3 elevate the β-1,3-exoglucanase activity of Candida albicans Xog1p, resulting in reduced fungal adhesion to plastic." Biochemical Journal 441, no. 3 (January 16, 2012): 963–70. http://dx.doi.org/10.1042/bj20111454.

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The opportunistic fungus Candida albicans causes oral thrush and vaginal candidiasis, as well as candidaemia in immunocompromised patients including those undergoing cancer chemotherapy, organ transplant and those with AIDS. We previously found that the AMPs (antimicrobial peptides) LL37 and hBD-3 (human β-defensin-3) inhibited C. albicans viability and its adhesion to plastic. For the present study, the mechanism by which LL37 and hBD-3 reduced C. albicans adhesion was investigated. After AMP treatment, C. albicans adhesion to plastic was reduced by up to ~60% and was dose-dependent. Our previous study indicated that LL37 might interact with the cell-wall β-1,3-exoglucanase Xog1p, which is involved in cell-wall β-glucan metabolism, and consequently the binding of LL37 or hBD-3 to Xog1p might cause the decrease in adhesion. For the present study, Xog1p(41–438)-6H, an N-terminally truncated, active, recombinant construct of Xog1p and Xog1p fragments were produced and used in pull-down assays and ELISA in vitro, which demonstrated that all constructs interacted with both AMPs. Enzymatic analyses showed that LL37 and hBD-3 enhanced the β-1,3-exoglucanase activity of Xog1p(41–438)-6H approximately 2-fold. Therefore elevated Xog1p activity might compromise cell-wall integrity and decrease C. albicans adhesion. To test this hypothesis, C. albicans was treated with 1.3 μM Xog1p(41–438)-6H and C. albicans adhesion to plastic decreased 47.7%. Taken together, the evidence suggests that Xog1p is one of the LL37/hBD-3 targets, and elevated β-1,3-exoglucanase activity reduces C. albicans adhesion to plastic.

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11

Bucki, Robert, and Paul A. Janmey. "Interaction of the Gelsolin-Derived Antibacterial PBP 10 Peptide with Lipid Bilayers and Cell Membranes." Antimicrobial Agents and Chemotherapy 50, no. 9 (September 2006): 2932–40. http://dx.doi.org/10.1128/aac.00134-06.

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ABSTRACTPBP 10, an antibacterial, cell membrane-permeant rhodamine B-conjugated peptide derived from the polyphosphoinositide binding site of gelsolin, interacts selectively with both lipopolysaccharides (LPS) and lipoteichoic acid (LTA), the distinct components of gram-negative and gram-positive bacteria, respectively. Isolated LPS and LTA decrease the antimicrobial activities of PBP 10, as well as other antimicrobial peptides, such as cathelicidin-LL37 (LL37) and mellitin. In an effort to elucidate the mechanism of bacterial killing by PBP 10, we compared its effects on artificial lipid bilayers and eukaryotic cell membranes with the actions of the mellitin, magainin II, and LL37 peptides. This study reveals that pore formation is unlikely to be involved in PBP 10-mediated membrane destabilization. We also investigated the effects of these peptides on platelets and red blood cells (RBCs). Comparison of these antimicrobial peptides shows that only mellitin has a toxic effect on platelets and RBCs in a concentration range concomitant with its bactericidal activity. The hemolytic activities of the PBP 10 and LL37 peptides significantly increase when RBCs are osmotically swollen in hypotonic solution, indicating that these antibacterial peptides may take advantage of the more extended form of bacterial membranes in exerting their killing activities. Additionally, we found that LL37 hemolytic activity was much higher when RBCs were induced to expose phosphatidylserine to the external leaflet of their plasma membranes. This finding suggests that asymmetrical distribution of phospholipids in the external membranes of eukaryotic cells may represent an important factor in determining the specificity of antibacterial peptides for targeting bacteria rather than eukaryotic cells.

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12

Liang, Huiyi, Yanzi Yan, Jingjiao Wu, Xiaofei Ge, Lai Wei, Lixin Liu, and Yongming Chen. "Topical nanoparticles interfering with the DNA-LL37 complex to alleviate psoriatic inflammation in mice and monkeys." Science Advances 6, no. 31 (July 2020): eabb5274. http://dx.doi.org/10.1126/sciadv.abb5274.

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Cell-free DNA (cfDNA) released from damaged or dead cells combines with LL37 and is converted into an immune response activator to exacerbate psoriasis. Here, we show that cationic nanoparticles (cNPs) efficiently compete for DNA from the DNA-LL37 immunocomplex and inhibit DNA-LL37-induced cell activation. Using phenotypical images, psoriasis area and severity index scoring, histology, and immunohistochemical analysis, we demonstrate that topical application of cNPs on psoriasiform skin of a mouse model relieves psoriatic symptoms. It is noteworthy that the results were confirmed in a cynomolgus monkey model. Moreover, topically administrated cNPs showed low in vivo toxicity because of their retention in skin. Mechanistic analyses of cytokine expression in the psoriatic site, cfDNA levels in circulation and inflamed skin, skin permeation, and biodistribution of cNPs also matched the therapeutic outcomes. Therefore, we present a previously unidentified strategy of nanomedicine to treat skin inflammatory diseases, which demonstrates great potential for clinical application.

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13

DeLong, Robert K., Jeffrey Comer, Elza Neelima Mathew, and Majid Jaberi-Douraki. "Comparative Molecular Immunological Activity of Physiological Metal Oxide Nanoparticle and its Anticancer Peptide and RNA Complexes." Nanomaterials 9, no. 12 (November 22, 2019): 1670. http://dx.doi.org/10.3390/nano9121670.

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Currently, there is a great interest in nanoparticle-based vaccine delivery. Recent studies suggest that nanoparticles when introduced into the biological milieu are not simply passive carriers but may also contribute immunological activity themselves or of their own accord. For example there is considerable interest in the biomedical applications of one of the physiologically-based inorganic metal oxide nanoparticle, zinc oxide (ZnO). Indeed zinc oxide (ZnO) NP are now recognized as a nanoscale chemotherapeutic or anticancer nanoparticle (ANP) and several recent reports suggest ZnO NP and/or its complexes with drug and RNA induce a potent antitumor response in immuno-competent mouse models. A variety of cell culture studies have shown that ZnO NP can induce cytokines such as IFN-γ, TNF-α, IL-2, and IL-12 which are known to regulate the tumor microenvironment. Much less work has been done on magnesium oxide (MgO), cobalt oxide (Co3O4), or nickel oxide (NiO); however, despite the fact that these physiologically-based metal oxide NP are reported to functionally load and assemble RNA and protein onto their surface and may thus also be of potential interest as nanovaccine platform. Here we initially compared in vitro immunogenicity of ZnO and Co3O4 NP and their effects on cancer-associated or tolerogenic cytokines. Based on these data we moved ZnO NP forward to testing in the ex vivo splenocyte assay relative to MgO and NiO NP and these data showed significant difference for flow cytometry sorted population for ZnO-NP, relative to NiO and MgO. These data suggesting both molecular and cellular immunogenic activity, a double-stranded anticancer RNA (ACR), polyinosinic:poly cytidylic acid (poly I:C) known to bind ZnO NP; when ZnO-poly I:C was injected into B16F10-BALB/C tumor significantly induced, IL-2 and IL-12 as shown by Cohen’s d test. LL37 is an anticancer peptide (ACP) currently in clinical trials as an intratumoral immuno-therapeutic agent against metastatic melanoma. LL37 is known to bind poly I:C where it is thought to compete for receptor binding on the surface of some immune cells, metastatic melanoma and lung cells. Molecular dynamic simulations revealed association of LL37 onto ZnO NP confirmed by gel shift assay. Thus using the well-characterized model human lung cancer model cell line (BEAS-2B), poly I:C RNA, LL37 peptide, or LL37-poly I:C complexes were loaded onto ZnO NP and delivered to BEAS-2B lung cells, and the effect on the main cancer regulating cytokine, IL-6 determined by ELISA. Surprisingly ZnO-LL37, but not ZnO-poly I:C or the more novel tricomplex (ZnO-LL37-poly I:C) significantly suppressed IL-6 by >98–99%. These data support the further evaluation of physiological metal oxide compositions, so-called physiometacomposite (PMC) materials and their formulation with anticancer peptide (ACP) and/or anticancer RNA (ACR) as a potential new class of immuno-therapeutic against melanoma and potentially lung carcinoma or other cancers.

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14

Chamilos, Georgios, Josh Gregorio, Stephan Meller, Roberto Lande, Dimitrios P. Kontoyiannis, Robert L. Modlin, and Michel Gilliet. "Cytosolic sensing of extracellular self-DNA transported into monocytes by the antimicrobial peptide LL37." Blood 120, no. 18 (November 1, 2012): 3699–707. http://dx.doi.org/10.1182/blood-2012-01-401364.

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Abstract The intracellular location of nucleic acid sensors prevents recognition of extracellular self-DNA released by dying cells. However, on forming a complex with the endogenous antimicrobial peptide LL37, extracellular DNA is transported into endosomal compartments of plasmacytoid dendritic cells, leading to activation of Toll-like receptor-9 and induction of type I IFNs. Whether LL37 also transports self-DNA into nonplasmacytoid dendritic cells, leading to type I IFN production via other intracellular DNA receptors is unknown. Here we found that LL37 very efficiently transports self-DNA into monocytes, leading the production of type I IFNs in a Toll-like receptor-independent manner. This type I IFN induction was mediated by double-stranded B form DNA, regardless of its sequence, CpG content, or methylation status, and required signaling through the adaptor protein STING and TBK1 kinase, indicating the involvement of cytosolic DNA sensors. Thus, our study identifies a novel link between the antimicrobial peptides and type I IFN responses involving DNA-dependent activation of cytosolic sensors in monocytes.

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15

Deslouches, Berthony, Kazi Islam, Jodi K. Craigo, Shruti M. Paranjape, Ronald C. Montelaro, and Timothy A. Mietzner. "Activity of the De Novo Engineered Antimicrobial Peptide WLBU2 against Pseudomonas aeruginosa in Human Serum and Whole Blood: Implications for Systemic Applications." Antimicrobial Agents and Chemotherapy 49, no. 8 (August 2005): 3208–16. http://dx.doi.org/10.1128/aac.49.8.3208-3216.2005.

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ABSTRACT Cationic amphipathic peptides have been extensively investigated as a potential source of new antimicrobials that can complement current antibiotic regimens in the face of emerging drug-resistant bacteria. However, the suppression of antimicrobial activity under certain biologically relevant conditions (e.g., serum and physiological salt concentrations) has hampered efforts to develop safe and effective antimicrobial peptides for clinical use. We have analyzed the activity and selectivity of the human peptide LL37 and the de novo engineered antimicrobial peptide WLBU2 in several biologically relevant conditions. The host-derived synthetic peptide LL37 displayed high activity against Pseudomonas aeruginosa but demonstrated staphylococcus-specific sensitivity to NaCl concentrations varying from 50 to 300 mM. Moreover, LL37 potency was variably suppressed in the presence of 1 to 6 mM Mg2+ and Ca2+ ions. In contrast, WLBU2 maintained its activity in NaCl and physiologic serum concentrations of Mg2+ and Ca2+. WLBU2 is able to kill P. aeruginosa (106 CFU/ml) in human serum, with a minimum bactericidal concentration of <9 μM. Conversely, LL37 is inactive in the presence of human serum. Bacterial killing kinetic assays in serum revealed that WLBU2 achieved complete bacterial killing in 20 min. Consistent with these results was the ability of WLBU2 (15 to 20 μM) to eradicate bacteria from ex vivo samples of whole blood. The selectivity of WLBU2 was further demonstrated by its ability to specifically eliminate P. aeruginosa in coculture with human monocytes or skin fibroblasts without detectable adverse effects to the host cells. Finally, WLBU2 displayed potent efficacy against P. aeruginosa in an intraperitoneal infection model using female Swiss Webster mice. These results establish a potential application of WLBU2 in the treatment of bacterial sepsis.

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16

Vignoni, Mariana, Hasitha de Alwis Weerasekera, Madeline J. Simpson, Jaywant Phopase, Thien-Fah Mah, May Griffith, Emilio I. Alarcon, and Juan C. Scaiano. "LL37 peptide@silver nanoparticles: combining the best of the two worlds for skin infection control." Nanoscale 6, no. 11 (2014): 5725–28. http://dx.doi.org/10.1039/c4nr01284d.

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17

Mandic Havelka, A., E. Yektaei-Karin, K. Hultenby, OE Sørensen, J. Lundahl, V. Berggren, and G. Marchini. "Maternal plasma level of antimicrobial peptide LL37 is a major determinant factor of neonatal plasma LL37 level." Acta Paediatrica 99, no. 6 (February 22, 2010): 836–41. http://dx.doi.org/10.1111/j.1651-2227.2010.01726.x.

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18

Jana, Jagannath, Rajiv Kumar Kar, Anirban Ghosh, Atanu Biswas, Surajit Ghosh, Anirban Bhunia, and Subhrangsu Chatterjee. "Human cathelicidin peptide LL37 binds telomeric G-quadruplex." Molecular BioSystems 9, no. 7 (2013): 1833. http://dx.doi.org/10.1039/c3mb70030e.

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19

Smith, Jordan R., Katie E. Barber, Animesh Raut, and Michael J. Rybak. "β-Lactams Enhance Daptomycin Activity against Vancomycin-Resistant Enterococcus faecalis and Enterococcus faecium inIn VitroPharmacokinetic/Pharmacodynamic Models." Antimicrobial Agents and Chemotherapy 59, no. 5 (March 9, 2015): 2842–48. http://dx.doi.org/10.1128/aac.00053-15.

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ABSTRACTEnterococcus faecalisandEnterococcus faeciumare frequently resistant to vancomycin and β-lactams. In enterococcal infections with reduced glycopeptide susceptibility, combination therapy is often administered. Our objective was to conduct pharmacokinetic/pharmacodynamic (PK/PD) models to evaluate β-lactam synergy with daptomycin (DAP) against resistant enterococci. OneE. faecalisstrain (R6981) and twoE. faeciumstrains (R6370 and 8019) were evaluated. DAP MICs were obtained. All strains were evaluated for response to LL37, an antimicrobial peptide, in the presence and absence of ceftaroline (CPT), ertapenem (ERT), and ampicillin (AMP). After 96 h,in vitromodels were run simulating 10 mg DAP/kg body weight/day, 600 mg CPT every 8 h (q8h), 2 g AMP q4h, and 1 g ERT q24h, both alone and in combination against all strains. DAP MICs were 2, 4, and 4 μg/ml for strains R6981, R6370, and 8019, respectively. PK/PD models demonstrated bactericidal activity with DAP-CPT, DAP-AMP, and DAP-ERT combinations against strain 8019 (P< 0.001 and log10CFU/ml reduction of >2 compared to any single agent). Against strains R6981 and R6370, the DAP-AMP combination demonstrated enhancement against R6370 but not R6981, while the combinations of DAP-CPT and DAP-ERT were bactericidal, demonstrated enhancement, and were statistically superior to all other regimens at 96 h (P< 0.001) against both strains. CPT, ERT, and AMP similarly augmented LL37 killing against strain 8019. In strains R6981 and R6370, CPT and ERT aided LL37 more than AMP (P< 0.001). Compared to DAP alone, combination regimens provide better killing and prevent resistance. Clinical research involving DAP combinations is warranted.

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Tao, Renchuan, Richard J. Jurevic, Kimberly K. Coulton, Marjorie T. Tsutsui, Marilyn C. Roberts, Janet R. Kimball, Norma Wells, Jeffery Berndt, and Beverly A. Dale. "Salivary Antimicrobial Peptide Expression and Dental Caries Experience in Children." Antimicrobial Agents and Chemotherapy 49, no. 9 (September 2005): 3883–88. http://dx.doi.org/10.1128/aac.49.9.3883-3888.2005.

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ABSTRACT Dental caries is a major worldwide oral disease problem in children. Although caries are known to be influenced by dietary factors, the disease results from a bacterial infection; thus, caries susceptibility may be affected by host factors such as salivary antimicrobial peptides. This study aimed to determine a possible correlation between caries prevalence in children and salivary concentrations of the antimicrobial peptides human beta-defensin-3 (hBD-3), the cathelicidin LL37, and the alpha-defensins HNP1-3 (a mixture of HNP1, 2, 3). Oral examinations were performed on 149 middle school children, and unstimulated whole saliva was collected for immunoassays of the three peptides and for assay of caries-causing bacteria in saliva. The median salivary levels of hBD-3, LL37, and HNP1-3 were in the microgram/ml range but were highly variable in the population. While levels of LL37 and hBD-3 did not correlate with caries experience, the median HNP1-3 levels were significantly higher in children with no caries than in children with caries. Children with high caries levels did not have high levels of salivary Streptococcus mutans, and the HNP1-3 level was not correlated with salivary S. mutans. By immunohistochemistry we localized HNP1-3 in submandibular salivary duct cells. HNPs are also released by neutrophils into the gingival crevicular fluid. Both sources may account for their presence in saliva. Low salivary levels of HNP1-3 may represent a biological factor that contributes to caries susceptibility. This observation could lead to new ways to screen for caries susceptibility and to new means of assessing the risk for this common oral problem.

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Ramos, Reinaldo, João Pedro Silva, Ana Cristina Rodrigues, Raquel Costa, Luísa Guardão, Fernando Schmitt, Raquel Soares, Manuel Vilanova, Lucília Domingues, and Miguel Gama. "Wound healing activity of the human antimicrobial peptide LL37." Peptides 32, no. 7 (July 2011): 1469–76. http://dx.doi.org/10.1016/j.peptides.2011.06.005.

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22

Girnita, A., H. Zheng, C. Worrall, M. Ståhle, and L. Girnita. "P52 IGF-1R and LL37 – a promoting growth interaction." Growth Hormone & IGF Research 20 (January 2010): S58. http://dx.doi.org/10.1016/s1096-6374(10)70152-0.

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Buznyk, O. "The sustained delivery system of the antiinfection peptide LL37 system — a potentially new treatment method of ocular infections. Report 1. Testing of different nano- and microparticles as carriers of LL37." Oftalmologicheskii Zhurnal 48, no. 2 (April 8, 2014): 17–21. http://dx.doi.org/10.31288/oftalmolzh201421721.

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Lin, Xiaoxuan, Ruoxun Wang, and Sui Mai. "Advances in delivery systems for the therapeutic application of LL37." Journal of Drug Delivery Science and Technology 60 (December 2020): 102016. http://dx.doi.org/10.1016/j.jddst.2020.102016.

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Pasyechnikova, N., S. Yakymenko, O. Buznyk, M. Islam, and M. Griffith. "Collagen-Based Corneal Substitutes with Incorporated Anti-infective Peptide LL37 Sustalined Deivery System." Oftalmologicheskii Zhurnal 53, no. 1 (February 17, 2015): 110–14. http://dx.doi.org/10.31288/oftalmolzh20151110114.

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Islam, M. M., M. Griffith, and O. Buznyk. "Anti-infective peptide LL37 sustained delivery system — a potential novel treatment method of ocular infections. Report 2. Antiviral properties of silica nanoparticle encapsulated LL37." Oftalmologicheskii Zhurnal 49, no. 3 (May 27, 2014): 53–57. http://dx.doi.org/10.31288/oftalmolzh201435357.

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Hitchon, Carol A., Xiaobo Meng, Hani S. El Gabalawy, and Linda Larcombe. "Human host defence peptide LL37 and anti-cyclic citrullinated peptide antibody in early inflammatory arthritis." RMD Open 5, no. 1 (April 2019): e000874. http://dx.doi.org/10.1136/rmdopen-2018-000874.

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ObjectiveAntibodies to citrullinated peptides (anti-CCP) develop in individuals predisposed to rheumatoid arthritis (RA). Neutrophil extracellular traps are a major source of citrullinated antigens and the immunomodulatory host defence peptide LL-37. Vitamin D regulates LL-37 expression. This study assessed the associations of LL-37 and anti-CCP, vitamin D metabolites and vitamin D receptor (VDR) polymorphisms in early inflammatory arthritis (EIA).MethodsSerum LL-37, 25-hydroxy-vitamin D (25OHvitD) and anti-CCP were measured by ELISA in treatment naïve EIA (n = 181). VDR single nucleotide polymorphisms (Fok1, Bsm1, Apa1, Taq1, Cdx-2) and HLADRB1 shared epitope (SE) alleles were detected by DNA amplification. Associations were tested in multivariable models. Median (25%, 75%) or percentiles are reported.ResultsParticipants (70 % female, age 56 [45, 66] years, disease activity score [DAS28ESR3var] 3.7 [2.8, 4.8], 41 % anti-CCP positive, 68 % RA) had low serum 25OHvitD; 20.5 nmol/L (13.9, 29.0). In multivariable models, controlling for age, sex, SE, smoking and vitamin D deficiency, LL37 level (top quartile) associated with anti-CCP seropositivity (OR 22; 95% CI 4 to 104).ConclusionsLevels of circulating LL-37 are associated with anti-CCP seropositivity. LL37 activity may be one mechanism linking infection and toxin exposure to anti-CCP generation.

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Deslouches, Berthony, Jonathan D. Steckbeck, Jodi K. Craigo, Yohei Doi, Jane L. Burns, and Ronald C. Montelaro. "Engineered Cationic Antimicrobial Peptides To Overcome Multidrug Resistance by ESKAPE Pathogens." Antimicrobial Agents and Chemotherapy 59, no. 2 (November 24, 2014): 1329–33. http://dx.doi.org/10.1128/aac.03937-14.

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ABSTRACTMultidrug resistance constitutes a threat to the medical achievements of the last 50 years. In this study, we demonstrated the abilities of twode novoengineered cationic antibiotic peptides (eCAPs), WLBU2 and WR12, to overcome resistance from 142 clinical isolates representing the most common multidrug-resistant (MDR) pathogens and to display a lower propensity to select for resistant bacteriain vitrocompared to that with colistin and LL37. The results warrant an exploration of eCAPs for use in clinical settings.

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Khung, R., H. Shiba, M. Kajiya, M. Kittaka, K. Ouhara, K. Takeda, N. Mizuno, T. Fujita, H. Komatsuzawa, and H. Kurihara. "LL37 induces VEGF expression in dental pulp cells through ERK signalling." International Endodontic Journal 48, no. 7 (September 12, 2014): 673–79. http://dx.doi.org/10.1111/iej.12365.

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Chereddy, Kiran Kumar, Charles-Henry Her, Michela Comune, Claudia Moia, Alessandra Lopes, Paolo E. Porporato, Julie Vanacker, et al. "PLGA nanoparticles loaded with host defense peptide LL37 promote wound healing." Journal of Controlled Release 194 (November 2014): 138–47. http://dx.doi.org/10.1016/j.jconrel.2014.08.016.

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Cassin, Margaret E., Andrew J. Ford, Sophia M. Orbach, Scott E. Saverot, and Padmavathy Rajagopalan. "The design of antimicrobial LL37-modified collagen-hyaluronic acid detachable multilayers." Acta Biomaterialia 40 (August 2016): 119–29. http://dx.doi.org/10.1016/j.actbio.2016.04.027.

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Kim, Soon-ja, Renshu Quan, Sung-Jin Lee, Hak-Kyo Lee, and Joong-Kook Choi. "Antibacterial activity of recombinant hCAP18/LL37 protein secreted from Pichia pastoris." Journal of Microbiology 47, no. 3 (June 2009): 358–62. http://dx.doi.org/10.1007/s12275-009-0131-9.

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Dutta, Jyotibon, Suhas Ramesh, Siduduzo M. Radebe, Anou M. Somboro, Beatriz G. de la Torre, Hendrik G. Kruger, Sabiha Y. Essack, Fernando Albericio, and Thavendran Govender. "Optimized Microwave Assisted Synthesis of LL37, a Cathelicidin Human Antimicrobial Peptide." International Journal of Peptide Research and Therapeutics 21, no. 1 (November 7, 2014): 13–20. http://dx.doi.org/10.1007/s10989-014-9439-3.

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Stephan, Alexander, Marina Batinica, Julia Steiger, Pia Hartmann, Frank Zaucke, Wilhelm Bloch, and Mario Fabri. "LL37:DNA complexes provide antimicrobial activity against intracellular bacteria in human macrophages." Immunology 148, no. 4 (July 18, 2016): 420–32. http://dx.doi.org/10.1111/imm.12620.

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Lu, Yingying, Hong Jiang, Bingjue Li, Luxi Cao, Qixia Shen, Weiwei Yi, Zhenyu Ju, et al. "Telomere dysfunction promotes small vessel vasculitis via the LL37-NETs-dependent mechanism." Annals of Translational Medicine 8, no. 6 (March 2020): 357. http://dx.doi.org/10.21037/atm.2020.02.130.

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Lin, Qiao, Berthony Deslouches, Ronald C. Montelaro, and Y. Peter Di. "Prevention of ESKAPE pathogen biofilm formation by antimicrobial peptides WLBU2 and LL37." International Journal of Antimicrobial Agents 52, no. 5 (November 2018): 667–72. http://dx.doi.org/10.1016/j.ijantimicag.2018.04.019.

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Merkle, Monika, Joachim Pircher, Hanna Mannell, Florian Krötz, Philipp Blüm, Thomas Czermak, Erik Gaitzsch, et al. "LL37 inhibits the inflammatory endothelial response induced by viral or endogenous DNA." Journal of Autoimmunity 65 (December 2015): 19–29. http://dx.doi.org/10.1016/j.jaut.2015.07.015.

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Lai, Yvonne, Sreedevi Adhikarakunnathu, Kanchan Bhardwaj, C. T. Ranjith-Kumar, Yahong Wen, Jarrat L. Jordan, Linda H. Wu, Bogdan Dragnea, Lani San Mateo, and C. Cheng Kao. "LL37 and Cationic Peptides Enhance TLR3 Signaling by Viral Double-stranded RNAs." PLoS ONE 6, no. 10 (October 21, 2011): e26632. http://dx.doi.org/10.1371/journal.pone.0026632.

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Buznyk, A., N. Pasyechnikova, S. Yakymenko, A. Moloda, M. M. Islam, and M. Griffith. "The sustained delivery system of the antiinfection peptide LL37 — a potential new method of treatment of ocular infections. Report 3. Antimicrobial activity of LL37 encapsulated in silica nanoparticle." Oftalmologicheskii Zhurnal 51, no. 5 (April 12, 2014): 4–8. http://dx.doi.org/10.31288/oftalmolzh2014548.

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Buznyk, O., C. J. Lee, M. M. Islam, N. Pasyechnikova, and M. Griffith. "Antiviral properties of collagen-based corneal substitute incorporating sustained delivery system for anti-infective peptide LL37." Oftalmologicheskii Zhurnal 57, no. 5 (September 30, 2015): 42–45. http://dx.doi.org/10.31288/oftalmolzh201554245.

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41

Sakoulas, George, Warren Rose, Poochit Nonejuie, Joshua Olson, Joseph Pogliano, Romney Humphries, and Victor Nizet. "Ceftaroline Restores Daptomycin Activity against Daptomycin-Nonsusceptible Vancomycin-Resistant Enterococcus faecium." Antimicrobial Agents and Chemotherapy 58, no. 3 (December 23, 2013): 1494–500. http://dx.doi.org/10.1128/aac.02274-13.

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ABSTRACTDaptomycin-nonsusceptible vancomycin-resistantEnterococcus faecium(VRE) strains are a formidable emerging threat to patients with comorbidities, leaving few therapeutic options in cases of severe invasive infections. Using a previously characterized isogenic pair of VRE strains from the same patient differing in their daptomycin susceptibilities (Etest MICs of 0.38 mg/liter and 10 mg/liter), we examined the effect of ceftaroline, ceftriaxone, and ampicillin on membrane fluidity and susceptibility of VRE to surface binding and killing by daptomycin and human cathelicidin antimicrobial peptide LL37. Synergy was notedin vitrobetween daptomycin, ampicillin, and ceftaroline for the daptomycin-susceptible VRE strain, but only ceftaroline showed synergy against the daptomycin-nonsusceptible VRE strain (∼2 log10CFU reduction at 24 h). Ceftaroline cotreatment increased daptomycin surface binding with an associated increase in membrane fluidity and an increase in the net negative surface charge of the bacteria as evidenced by increased poly-l-lysine binding. Consistent with the observed biophysical changes, ceftaroline resulted in increased binding and killing of daptomycin-nonsusceptible VRE by human cathelicidin LL37. Using a pair of daptomycin-susceptible/nonsusceptible VRE strains, we noted that VRE is ceftaroline resistant, yet ceftaroline confers significant effects on growth rate as well as biophysical changes on the cell surface of VRE that can potentiate the activity of daptomycin and innate cationic host defense peptides, such as cathelicidin. Although limited to just 2 strains, these finding suggest that additionalin vivoandin vitrostudies need to be done to explore the possibility of using ceftaroline as adjunctive anti-VRE therapy.

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Brogden, K. A., V. C. Kalfa, M. R. Ackermann, D. E. Palmquist, P. B. McCray, and B. F. Tack. "The Ovine Cathelicidin SMAP29 Kills Ovine Respiratory Pathogens In Vitro and in an Ovine Model of Pulmonary Infection." Antimicrobial Agents and Chemotherapy 45, no. 1 (January 1, 2001): 331–34. http://dx.doi.org/10.1128/aac.45.1.331-334.2001.

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ABSTRACT Cathelicidins are antimicrobial peptides from sheep (SMAP29 and SMAP34), rabbits (CAP11 and CAP18), rodents (CRAMP), and humans (FALL39, LL37, and h/CAP18). In a broth microdilution assay against nine ovine pathogens, SMAP29, SMAP34, mouse CRAMP, CAP18, CAP1831, CAP1828, CAP1822, and CAP1821a were the most active, with MICs as low as 0.6 μg/ml. Other cathelicidins were less active. In lambs with pneumonia, 0.5 mg of SMAP29 reduced the concentration of bacteria in both bronchoalveolar lavage fluid and consolidated pulmonary tissues. Hence, the antimicrobial activity of SMAP29 suggests that it has applications in the treatment of respiratory tract infections.

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Frasca, Loredana, and Roberto Lande. "Role of Defensins and Cathelicidin LL37 in Auto-Immune and Auto- Inflammatory Diseases." Current Pharmaceutical Biotechnology 13, no. 10 (July 1, 2012): 1882–97. http://dx.doi.org/10.2174/138920112802273155.

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Zürcher, Christoph, Kay-Sara Sauter, and Matthias Schweizer. "Pestiviral E rns blocks TLR-3-dependent IFN synthesis by LL37 complexed RNA." Veterinary Microbiology 174, no. 3-4 (December 2014): 399–408. http://dx.doi.org/10.1016/j.vetmic.2014.09.028.

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Kittaka, Mizuho, Hideki Shiba, Mikihito Kajiya, Takako Fujita, Tomoyuki Iwata, Khung Rathvisal, Kazuhisa Ouhara, et al. "The antimicrobial peptide LL37 promotes bone regeneration in a rat calvarial bone defect." Peptides 46 (August 2013): 136–42. http://dx.doi.org/10.1016/j.peptides.2013.06.001.

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Steinstraesser, Lars, Andre Ring, Robert Bals, Hans-Ulrich Steinau, and Stefan Langer. "The Human Host Defense Peptide LL37/hCAP Accelerates Angiogenesis in PEGT/PBT Biopolymers." Annals of Plastic Surgery 56, no. 1 (January 2006): 93–98. http://dx.doi.org/10.1097/01.sap.0000190883.30005.91.

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Pouwels, Simon D., Martijn C. Nawijn, Erik Bathoorn, Annelies Riezebos-Brilman, Antoon J. M. van Oosterhout, Huib A. M. Kerstjens, and Irene H. Heijink. "Increased serum levels of LL37, HMGB1 and S100A9 during exacerbation in COPD patients." European Respiratory Journal 45, no. 5 (April 30, 2015): 1482–85. http://dx.doi.org/10.1183/09031936.00158414.

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48

Ferreira, André F., Michela Comune, Akhilesh Rai, Lino Ferreira, and Pedro N. Simões. "Atomistic-Level Investigation of a LL37-Conjugated Gold Nanoparticle By Well-Tempered Metadynamics." Journal of Physical Chemistry B 122, no. 35 (August 14, 2018): 8359–66. http://dx.doi.org/10.1021/acs.jpcb.8b05717.

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Amagai, R., T. Takahashi, T. Fujimura, K. Yamasaki, and S. Aiba. "517 Human cathelicidin LL37 binds to scavenger receptors in inflammatory human skin diseases." Journal of Investigative Dermatology 139, no. 5 (May 2019): S89. http://dx.doi.org/10.1016/j.jid.2019.03.593.

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Hell, Ã, C. G. Giske, A. Nelson, U. RÃ¶mling, and G. Marchini. "Human cathelicidin peptide LL37 inhibits both attachment capability and biofilm formation ofStaphylococcus epidermidis." Letters in Applied Microbiology 50, no. 2 (February 2010): 211–15. http://dx.doi.org/10.1111/j.1472-765x.2009.02778.x.

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