Literature DB >> 8268005

Iron uptake mechanisms of pathogenic bacteria.

K G Wooldridge1, P H Williams.   

Abstract

Most of the iron in a mammalian body is complexed with various proteins. Moreover, in response to infection, iron availability is reduced in both extracellular and intracellular compartments. Bacteria need iron for growth and successful bacterial pathogens have therefore evolved to compete successfully for iron in the highly iron-stressed environment of the host's tissues and body fluids. Several strategies have been identified among pathogenic bacteria, including reduction of ferric to ferrous iron, occupation of intracellular niches, utilisation of host iron compounds, and production of siderophores. While direct evidence that high affinity mechanisms for iron acquisition function as bacterial virulence determinants has been provided in only a small number of cases, it is likely that many if not all such systems play a central role in the pathogenesis of infection.

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Year:  1993        PMID: 8268005     DOI: 10.1111/j.1574-6976.1993.tb00026.x

Source DB:  PubMed          Journal:  FEMS Microbiol Rev        ISSN: 0168-6445            Impact factor:   16.408


  116 in total

Review 1.  Probiotic bacteria as biological control agents in aquaculture.

Authors:  L Verschuere; G Rombaut; P Sorgeloos; W Verstraete
Journal:  Microbiol Mol Biol Rev       Date:  2000-12       Impact factor: 11.056

2.  Pathogenic neisseriae can use hemoglobin, transferrin, and lactoferrin independently of the tonB locus.

Authors:  P J Desai; E Garges; C A Genco
Journal:  J Bacteriol       Date:  2000-10       Impact factor: 3.490

3.  The mammalian neuroendocrine hormone norepinephrine supplies iron for bacterial growth in the presence of transferrin or lactoferrin.

Authors:  P P Freestone; M Lyte; C P Neal; A F Maggs; R D Haigh; P H Williams
Journal:  J Bacteriol       Date:  2000-11       Impact factor: 3.490

4.  The siderophore 2,3-dihydroxybenzoic acid is not required for virulence of Brucella abortus in BALB/c mice.

Authors:  B H Bellaire; P H Elzer; C L Baldwin; R M Roop
Journal:  Infect Immun       Date:  1999-05       Impact factor: 3.441

5.  Survey of ferroxidase expression and siderophore production in clinical isolates of Pseudomonas aeruginosa.

Authors:  Wilhelmina M Huston; Adam J Potter; Michael P Jennings; Jordi Rello; Alan R Hauser; Alastair G McEwan
Journal:  J Clin Microbiol       Date:  2004-06       Impact factor: 5.948

6.  Chemical scaffolds with structural similarities to siderophores of nonribosomal peptide-polyketide origin as novel antimicrobials against Mycobacterium tuberculosis and Yersinia pestis.

Authors:  Julian A Ferreras; Akash Gupta; Neal D Amin; Arijit Basu; Barij N Sinha; Stefan Worgall; Venkatesan Jayaprakash; Luis E N Quadri
Journal:  Bioorg Med Chem Lett       Date:  2011-08-26       Impact factor: 2.823

7.  Expression and characterization of an iron-regulated hemin-binding protein, HbpA, from Leptospira interrogans serovar Lai.

Authors:  Swapna Asuthkar; Sridhar Velineni; Johannes Stadlmann; Friedrich Altmann; Manjula Sritharan
Journal:  Infect Immun       Date:  2007-06-18       Impact factor: 3.441

8.  SirR, a novel iron-dependent repressor in Staphylococcus epidermidis.

Authors:  P J Hill; A Cockayne; P Landers; J A Morrissey; C M Sims; P Williams
Journal:  Infect Immun       Date:  1998-09       Impact factor: 3.441

Review 9.  Beyond iron: non-classical biological functions of bacterial siderophores.

Authors:  Timothy C Johnstone; Elizabeth M Nolan
Journal:  Dalton Trans       Date:  2015-04-14       Impact factor: 4.390

10.  Binding and accumulation of hemin in Neisseria gonorrhoeae.

Authors:  P J Desai; R Nzeribe; C A Genco
Journal:  Infect Immun       Date:  1995-12       Impact factor: 3.441

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