Synthesis and structure–activity relationship of β-defensins, multi-functional peptides of the immune system

Klüver, Enno; Adermann, Knut; Schulz, Axel

doi:10.1002/psc.749

Cited by 92 publications

(84 citation statements)

References 107 publications

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“…Both NOD2 and DEFB1 are involved in the resistance to bacterial pathogens. NOD2 (also called CARD15) is a member of the phylogenetically conserved NACHT-LRR (NLR) family and plays a role in the immune response to intracellular bacteria by recognizing MPD, a peptidoglycan component (43); DEFB1 is an antimicrobial peptide implicated in the resistance of epithelial surfaces to microbial colonization and belongs to the family of defensins, microbicidal and cytotoxic peptides made by neutrophils (53). Despite the great importance of the NOD pathway and the role of defensins in the innate immune response, our interest especially focused on characterizing TLR7 gene regulation in DC, because very little is known about it.…”

Section: Discussionmentioning

confidence: 99%

Sensitization to TLR7 Agonist in IFN-β-Preactivated Dendritic Cells

Severa

Remoli

Giacomini

et al. 2007

The Journal of Immunology

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TLRs interact with a growing list of pathogen-derived products and these interactions drive the activation of innate and adaptive immune responses. Dendritic cells (DC) play a key role in these events expressing a heterogeneous repertoire of TLRs. We have previously demonstrated the production of type I IFNs in DC following bacterial infections and TLR triggering. In this study, we sought to characterize the transcriptome specifically induced in human DC by IFN-β production stimulated upon LPS treatment. To this aim, by using cDNA microarrays, we compared the transcriptome of DC following LPS treatment in the absence or presence of neutralizing anti-type I IFN Abs. Interestingly, we found that the expression of TLR7 was induced during LPS-induced maturation of DC in a type I IFN-dependent manner. The induction of TLR7 in maturing DC was mainly a consequence of the transcriptional activity of IRF-1, whose binding site was located within TLR7 promoter. Moreover, we also demonstrated that “priming” of immature DC, that usually express TLR8 but not TLR7, with exogenous IFN-β induced a functionally active TLR7. In fact, treatment with the TLR7-specific ligand 3M-001 up-regulated the expression of CD83, CD86, and CD38 in IFN-β-primed DC but not in immature DC. Therefore, a robust enhancement in proinflammatory as well as regulatory cytokines was observed. These data suggest that TLR4-mediated type I IFN release activates specific transcription programs in DC amplifying the expression of pathogen sensors to correctly and combinatorially respond to a bacterial as well as viral infection.

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Section: Discussionmentioning

confidence: 99%

Sensitization to TLR7 Agonist in IFN-β-Preactivated Dendritic Cells

Severa

Remoli

Giacomini

et al. 2007

The Journal of Immunology

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“…13 It is therefore difficult to purify this protein from the sperm membrane and luminal contents in mild solutions. Because chemical synthesis of b-defensins is expensive and success is limited, 23 the use of recombinant expression strategies is preferred. 24 Efficient soluble protein expression was important in the recombinant strategy of defensin synthesis, 23 with soluble expression itself being the minimal requirement.…”

Section: Soluble Expression and Antimicrobial Activity Of Recombinantmentioning

confidence: 99%

“…Because chemical synthesis of b-defensins is expensive and success is limited, 23 the use of recombinant expression strategies is preferred. 24 Efficient soluble protein expression was important in the recombinant strategy of defensin synthesis, 23 with soluble expression itself being the minimal requirement. The recombinant construct was confirmed by DNA sequencing covering the whole open-reading frame region and the bilateral sequences.…”

Section: Soluble Expression and Antimicrobial Activity Of Recombinantmentioning

confidence: 99%

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Rat recombinant β-defensin 22 is a heparin-binding protein with antimicrobial activity

Diao¹,

Yu²,

Sun³

et al. 2010

Asian J Androl

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Approximately 40-50 b-defensins are predominantly expressed in the male reproductive system of mammals. This selective expression raises the question as to the roles of these molecules in innate immunity and fertility in the male reproductive tract. Rat b-defensin 22 is an epididymis-specific b-defensin expressed in segments 12-14 of the epididymis. This protein contains both b-defensin and lectin signature sequences, yet its antimicrobial activity and carbohydrate-binding ability have not been shown. We herein demonstrated the antimicrobial activity of recombinant rat b-defensin 22 against Escherichia coli and Candida albicans. Its lectin-like activity was also investigated by demonstrating its binding ability with heparin beads. This heparin-binding activity implies some potential roles for this defensin in determining the fertilisation capabilities of sperm.

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“…Defensins are a large family of cationic antimicrobial peptides that comprise of 30-50 amino acid residues and exist widely in various species of plants and animals (Hancock, 2001;Ganz, 2003;Ganz, 2004;Selsted and Ouellette, 2005;Klüver et al, 2006). They have broad antimicrobial activity against pathogens, including bacteria, viruses, and fungi (Selsted and Ouellette, 2005;Peschel and Sahl, 2006;Yang et al, 2007;Auvynet and Rosenstein, 2009).…”

Section: Introductionmentioning

confidence: 99%

Preparation of polyclonal antibody against porcine beta defensin 2 and identification of its distribution in tissues of pig

Bao¹,

Li²,

Zhang³

et al. 2015

Genet. Mol. Res.

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ABSTRACT. Porcine β-defensin 2 (pBD2) is an antimicrobial peptide in pigs that plays an important role in the immune system by preventing bacterial invasion. To produce an anti-pBD2 antibody, which is not commercially available, we expressed and purified a soluble, his-tagged version of pBD2 (his-pBD2). Purified pBD2 was injected into New Zealand white rabbits to generate polyclonal antiserum. Anti-pBD2 antibodies were purified by ammonium sulfate precipitation, followed by diethylaminoethyl cellulose ionexchange chromatography. The purified polyclonal antibody showed high sensitivity, with a titer as high as 204,800 by enzyme-linked immunosorbent assay, and it also showed high specificity for both his-pBD2 and native pBD2, as assessed by western blotting. Furthermore, immunohistochemistry analysis using the purified antibody revealed that pBD2 protein is distributed in the tongue, liver, kidney, small intestine, and large intestine of pigs. These results indicate that the prepared polyclonal antibody will be a useful tool for further studies of the function and mechanism of pBD2.

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Synthesis and structure–activity relationship of β-defensins, multi-functional peptides of the immune system

Cited by 92 publications

References 107 publications

Sensitization to TLR7 Agonist in IFN-β-Preactivated Dendritic Cells

Sensitization to TLR7 Agonist in IFN-β-Preactivated Dendritic Cells

Rat recombinant β-defensin 22 is a heparin-binding protein with antimicrobial activity

Preparation of polyclonal antibody against porcine beta defensin 2 and identification of its distribution in tissues of pig

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