Literature DB >> 7768155

Antimicrobial peptides as agents of mucosal immunity.

C L Bevins1.   

Abstract

Mucosal surfaces are continually exposed to a wide range of potentially pathogenic organisms, yet the incidence of infectious disease resulting from these encounters is relatively low. This suggests the presence of highly effective defence mechanisms in these tissues. Antimicrobial peptides have recently been discovered in mucosal tissues and may play a significant role in host defence. Several mucosal peptides (andropin, magainin, tracheal antimicrobial peptide, enteric defensins and PR-39) all fulfil minimal criteria for a role in mucosal host defence, including potent in vitro antimicrobial activity and accumulation at the mucosal surface. Most of these mucosal peptides are encoded by members of large gene families that contain members found in other biological contexts more classically associated with antimicrobial defence. The abundance, activity and evolutionary history of several epithelial peptides suggest that antimicrobial peptides play a key role in host defence at mucosal surfaces.

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Year:  1994        PMID: 7768155     DOI: 10.1002/9780470514658.ch15

Source DB:  PubMed          Journal:  Ciba Found Symp        ISSN: 0300-5208


  14 in total

Review 1.  Peptide antibiotics.

Authors:  R E Hancock; D S Chapple
Journal:  Antimicrob Agents Chemother       Date:  1999-06       Impact factor: 5.191

2.  Enteric beta-defensin: molecular cloning and characterization of a gene with inducible intestinal epithelial cell expression associated with Cryptosporidium parvum infection.

Authors:  A P Tarver; D P Clark; G Diamond; J P Russell; H Erdjument-Bromage; P Tempst; K S Cohen; D E Jones; R W Sweeney; M Wines; S Hwang; C L Bevins
Journal:  Infect Immun       Date:  1998-03       Impact factor: 3.441

3.  Bactericidal activity of a synthetic peptide (CG 117-136) of human lysosomal cathepsin G is dependent on arginine content.

Authors:  W M Shafer; F Hubalek; M Huang; J Pohl
Journal:  Infect Immun       Date:  1996-11       Impact factor: 3.441

4.  Isolation, antimicrobial activities, and primary structures of hamster neutrophil defensins.

Authors:  P Mak; K Wójcik; I B Thogersen; A Dubin
Journal:  Infect Immun       Date:  1996-11       Impact factor: 3.441

5.  Identification and genetic characterization of PmrA-regulated genes and genes involved in polymyxin B resistance in Salmonella enterica serovar typhimurium.

Authors:  Rita Tamayo; Sara S Ryan; Andrea J McCoy; John S Gunn
Journal:  Infect Immun       Date:  2002-12       Impact factor: 3.441

6.  Characterization of a fish antimicrobial peptide: gene expression, subcellular localization, and spectrum of activity.

Authors:  A M Cole; R O Darouiche; D Legarda; N Connell; G Diamond
Journal:  Antimicrob Agents Chemother       Date:  2000-08       Impact factor: 5.191

7.  Constitutive mutations of the Salmonella enterica serovar Typhimurium transcriptional virulence regulator phoP.

Authors:  J S Gunn; R K Ernst; A J McCoy; S I Miller
Journal:  Infect Immun       Date:  2000-06       Impact factor: 3.441

8.  Anti-microbial properties of histone H2A from skin secretions of rainbow trout, Oncorhynchus mykiss.

Authors:  Jorge M O Fernandes; Graham D Kemp; M Gerard Molle; Valerie J Smith
Journal:  Biochem J       Date:  2002-12-01       Impact factor: 3.857

9.  Expression of the peptide antibiotic human beta-defensin 1 in cultured gingival epithelial cells and gingival tissue.

Authors:  S Krisanaprakornkit; A Weinberg; C N Perez; B A Dale
Journal:  Infect Immun       Date:  1998-09       Impact factor: 3.441

10.  The major cold shock gene, cspA, is involved in the susceptibility of Staphylococcus aureus to an antimicrobial peptide of human cathepsin G.

Authors:  Samuel Katzif; Damien Danavall; Samera Bowers; Jacqueline T Balthazar; William M Shafer
Journal:  Infect Immun       Date:  2003-08       Impact factor: 3.441

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