hBD‐1: a novel β‐defensin from human plasma

Bensch, Klaus W.; Raida, Manfred; Mägert, Hans-Jürgen; Schulz‐Knappe, Peter; Forssmann, Wolf‐Georg

doi:10.1016/0014-5793(95)00687-5

Cited by 514 publications

(340 citation statements)

References 22 publications

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“…5,6 Human bdefensin 1 (DEFB1, hBD-1) was the first characterized human b-defensin identified in hemofiltrate. 7 DEFB1 is constitutively expressed mainly in kidney, keratinocytes, oral cavity, as well as in urogenital tract. 8,9 The in vitro expression of DEFB1 can be upregulated by LPS, IL-1b, interferon-g (IFN-g) and arginine.…”

Section: Introductionmentioning

confidence: 99%

Genomic variations within DEFB1 are associated with the susceptibility to and the fatal outcome of severe sepsis in Chinese Han population

Huang

et al. 2007

Genes Immun

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Sepsis is a systemic inflammatory response syndrome to infection. Human b-defensin 1 (DEFB1) is a multifunctional mediator in infection and inflammation, which has been largely explored in ex vivo studies. The present case-control study was designed to investigate whether DEFB1 genomic variations are associated with the susceptibility to and the outcome of severe sepsis in 211 patients with severe sepsis and 157 ethnic-matched healthy controls. After correcting for multiple testing, the À44G/C was the only polymorphism found to show significant associations with both the susceptibility to and the fatal outcome of severe sepsis (P ¼ 0.0049, odd ratio (OR) 1.971 and P ¼ 0.002, OR 2.406, respectively). Haplotype À20A/À44C/À52G showed a protective role against severe sepsis (P ¼ 0.0066, OR 0.6751), whereas haplotype À20G/À44G/À52G served as a risk factor for the fatal outcome of severe sepsis (P ¼ 0.0052, OR 2.427). These findings provide further evidence that b-defensin 1 may play a role in the pathogenesis of severe sepsis.

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Section: Introductionmentioning

confidence: 99%

Genomic variations within DEFB1 are associated with the susceptibility to and the fatal outcome of severe sepsis in Chinese Han population

Huang

et al. 2007

Genes Immun

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“…3 Based on their size and the spatial position of the six cysteine residues, animal defensins are classified as a-, b-, y-defensins of vertebrates (mammalia and birds) and insect defensins. To date, vertebrate defensins were identified in numerous species: mice, [6][7][8] birds-where they are called gallinacins- 9 rats, 10 cattle, 11,12 goats, 13 sheeps, 14 humans, 8,15,16 and non-human primates [17][18][19][20] (reviewed in Martin et al, 4 Hughes, 21 Schroder, 22 and Lehrer and Ganz 23 ). Interestingly, domestic cattle (Bos taurus) was shown to share a broad spectrum of different b-defensins, for example, tap (tracheal antimicrobial peptide), lap (lingual antimicrobial peptide), bnbd (bovine neutrophil peptide), nbd12 (neutrophil beta defensin 12), and ebd (enteric beta defensin).…”

Section: Introductionmentioning

confidence: 99%

Variability and evolution of bovine β-defensin genes

Luenser

Ludwig

2004

Genes Immun

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Defensins comprise an important family of antimicrobial peptides. Among vertebrates numerous defensin genes have been detected, but their evolutionary background is still discussed. We investigated the molecular evolution of bovine defensins via screening of different bovine species including the extinct ancestor of domestic cattle (Bos primigenius) for b-defensin encoding genes. We detected a large variability of new defensin encoding sequences similar to previously published bovine neutrophil b-defensin (bnbd), neutrophil b-defensin 12 (nbd12), enteric b-defensin (ebd), lingual antimicrobial peptide (lap), and tracheal antimicrobial peptide (tap). Our data suggest that variants of the same so-called subfamily (tap, lap, ebd, and nbd12) each share a common ancestry independent of their species origin, implicating several duplication events of tap, lap, ebd, and nbd12 before the different bovine lineages diverged. Variants of bovine neutrophil b-defensins bnbd5 and bnbd9 were detected exclusively in domestic cattle and aurochs. Values of synonymous and nonsynonymous substitutions demonstrated lap, bnbd5, bnbd9 and nbd12 evolving under positive selection, whereas amino-acid altering substitutions among variants of ebd and tap are purified. Comparison of the amino-acid sequences with available structures of human and murine defensins suggested conservation of the typical secondary elements of defensins in the absence of high sequence similarity.

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“…They are composed of 29-42 amino acids and contain three disulphide bonds, formed by three pairs of cysteine residues [1][2][3][4]. Defensins have been isolated from various tissue sources, such as mammalian trachea, intestine, tongue and skin, and human plasma, oral mucosa, salivary glands, saliva and ocular surface [5][6][7][8][9][10][11][12][13]. Defensins are involved in the oxygenindependent mechanism of the host immune response [14].…”

Section: Introductionmentioning

confidence: 99%

Large-scale synthesis and functional elements for the antimicrobial activity of defensins

Raj

Antonyraj

Karunakaran

2000

Biochemical Journal

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Human neutrophil defensins, and their analogues incorporating anionic, hydrophobic or cationic residues at the N- and C-termini, were synthesized by solid-phase procedures. The synthetic defensins were examined for their microbicidal activity against Candida albicans, two Gram-negative bacteria (Actinobacillus actinomycetemcomitans and Porphyromonas gingivalis) and two Gram-positive bacteria (Streptococcus gordonii and Streptococcus mutans). The human neutrophil peptide 1 (HNP1) and HNP2 were found to be potent candidacidal agents. HNP3, which differs by one amino acid at the N-terminus of its sequence, was totally inactive. The Gram-negative bacteria A. actinomycetemcomitans and P. gingivalis and the Gram-positive bacteria S. gordonii and S. mutans were insensitive to human defensins. However, the insertion of two basic residues, such as arginine, at both the N-terminus and the C-terminus of HNP2 significantly enhanced antifungal and antibacterial activity. The addition of anionic residues, such as aspartic acid, at the N- and C-termini rendered the molecule totally inactive. The presence of two hydrophobic amino acids, such as valine, at the N-terminus of HNP2 and of two basic arginine residues at its C-terminus resulted in molecules that were optimally active against these oral pathogens. The results suggest that the N- and C-terminal residues in defensin peptides are the crucial functional elements that determine their microbicidal potency. The three-dimensional structure of all defensins constitutes the same amphiphilic β-sheet structure, with the polar face formed by the N- and C-terminal residues playing an important role in defining microbicidal potency and the antimicrobial spectrum. The enhanced microbicidal activity observed for defensin peptides with two basic residues at both the N- and C-termini could be due to optimization of the amphiphilicity of the structure, which could facilitate specific interactions with the microbial membranes.

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hBD‐1: a novel β‐defensin from human plasma

Cited by 514 publications

References 22 publications

Genomic variations within DEFB1 are associated with the susceptibility to and the fatal outcome of severe sepsis in Chinese Han population

Genomic variations within DEFB1 are associated with the susceptibility to and the fatal outcome of severe sepsis in Chinese Han population

Variability and evolution of bovine β-defensin genes

Large-scale synthesis and functional elements for the antimicrobial activity of defensins

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