Literature DB >> 1532495

Transferrins and heme-compounds as iron sources for pathogenic bacteria.

B R Otto1, A M Verweij-van Vught, D M MacLaren.   

Abstract

The low concentration of free iron in body fluids creates bacteriostatic conditions for many microorganisms and is therefore an important defense factor of the body against invading bacteria. Pathogenic bacteria have developed several mechanisms for acquiring iron from the host. Siderophore-mediated iron uptake involves the synthesis of low molecular weight iron chelators called siderophores which compete with the host iron-binding glycoproteins lactoferrin (LF) and transferrin (TF) for iron. Other ways to induce iron uptake, without the mediation of siderophores, are the possession of outer membrane protein receptors that actually recognize the complex of TF or LF with iron, resulting in the internalization of this metal, and the use of heme-compounds released into the circulation after lysis of erythrocytes. In this review, the nonsiderophore-mediated iron-uptake systems used by certain pathogenic bacteria are emphasized. The possible contribution of these iron-uptake systems to the virulence of pathogens is also discussed.

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Year:  1992        PMID: 1532495     DOI: 10.3109/10408419209114559

Source DB:  PubMed          Journal:  Crit Rev Microbiol        ISSN: 1040-841X            Impact factor:   7.624


  153 in total

1.  HmbR, a hemoglobin-binding outer membrane protein of Neisseria meningitidis, undergoes phase variation.

Authors:  A R Richardson; I Stojiljkovic
Journal:  J Bacteriol       Date:  1999-04       Impact factor: 3.490

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.  Quantification of siderophore and hemolysin from Stachybotrys chartarum strains, including a strain isolated from the lung of a child with pulmonary hemorrhage and hemosiderosis.

Authors:  S J Vesper; D G Dearborn; O Elidemir; R A Haugland
Journal:  Appl Environ Microbiol       Date:  2000-06       Impact factor: 4.792

4.  Immunization with recombinant transferrin binding protein B enhances clearance of nontypeable Haemophilus influenzae from the rat lung.

Authors:  D C Webb; A W Cripps
Journal:  Infect Immun       Date:  1999-05       Impact factor: 3.441

5.  PspA protects Streptococcus pneumoniae from killing by apolactoferrin, and antibody to PspA enhances killing of pneumococci by apolactoferrin [corrected].

Authors:  Mirza Shaper; Susan K Hollingshead; William H Benjamin; David E Briles
Journal:  Infect Immun       Date:  2004-09       Impact factor: 3.441

6.  Crystallization and preliminary crystallographic studies of Campylobacter jejuni ChuZ, a member of a novel haem oxygenase family.

Authors:  Rui Zhang; Jinyong Zhang; Honglei Ding; Dongshui Lu; Yonglin Hu; Da Cheng Wang; Quanming Zou
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2011-09-29

7.  Terephthalamide-containing ligands: fast removal of iron from transferrin.

Authors:  Rebecca J Abergel; Kenneth N Raymond
Journal:  J Biol Inorg Chem       Date:  2007-11-08       Impact factor: 3.358

8.  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

9.  Cloning and characterization of tdhA, a locus encoding a TonB-dependent heme receptor from Haemophilus ducreyi.

Authors:  C E Thomas; B Olsen; C Elkins
Journal:  Infect Immun       Date:  1998-09       Impact factor: 3.441

10.  Binding of heme-hemopexin complexes by soluble HxuA protein allows utilization of this complexed heme by Haemophilus influenzae.

Authors:  L D Cope; S E Thomas; Z Hrkal; E J Hansen
Journal:  Infect Immun       Date:  1998-09       Impact factor: 3.441

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