Literature DB >> 3902529

Uptake of iron from hemoglobin and the haptoglobin-hemoglobin complex by hemolytic bacteria.

R T Francis, J W Booth, R R Becker.   

Abstract

The abilities of Staphylococcus aureus and Streptococcus pyogenes to remove iron from mouse 59Fe hemoglobin that was either in free form or complexed with human haptoglobin, were evaluated. 59Fe hemoglobin from the amphibian Taricha granulosa was also used in free form or complexed with the amphibian's hemoglobin-binding proteins. Contrary to what was reported from a study using pathogenic Escherichia coli, haptoglobin failed to exhibit a bacteriostatic influence when complexed with hemoglobin. In our study, more 59Fe was removed by the bacteria from the haptoglobin-hemoglobin complex than from free mouse hemoglobin. The hemoglobin and hemoglobin-plasma protein complexes of Taricha were stripped of 59Fe at similar rates and extents by both bacterial species.

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Year:  1985        PMID: 3902529     DOI: 10.1016/0020-711x(85)90262-9

Source DB:  PubMed          Journal:  Int J Biochem        ISSN: 0020-711X


  28 in total

1.  Characterization of MtsR, a new metal regulator in group A streptococcus, involved in iron acquisition and virulence.

Authors:  Christopher S Bates; Chadia Toukoki; Melody N Neely; Zehava Eichenbaum
Journal:  Infect Immun       Date:  2005-09       Impact factor: 3.441

2.  Iron regulation of Serratia marcescens hemolysin gene expression.

Authors:  K Poole; V Braun
Journal:  Infect Immun       Date:  1988-11       Impact factor: 3.441

3.  Heme transfer from streptococcal cell surface protein Shp to HtsA of transporter HtsABC.

Authors:  Mengyao Liu; Benfang Lei
Journal:  Infect Immun       Date:  2005-08       Impact factor: 3.441

4.  The human protein haptoglobin inhibits IsdH-mediated heme-sequestering by Staphylococcus aureus.

Authors:  Jakob H Mikkelsen; Kasper Runager; Christian B F Andersen
Journal:  J Biol Chem       Date:  2019-12-09       Impact factor: 5.157

5.  Effects of serum carrier proteins on the growth of pathogenic neisseriae with heme-bound iron.

Authors:  D W Dyer; E P West; P F Sparling
Journal:  Infect Immun       Date:  1987-09       Impact factor: 3.441

6.  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

7.  Study of streptococcal hemoprotein receptor (Shr) in iron acquisition and virulence of M1T1 group A streptococcus.

Authors:  Samira Dahesh; Victor Nizet; Jason N Cole
Journal:  Virulence       Date:  2012-10-17       Impact factor: 5.882

8.  Analysis of haptoglobin and hemoglobin-haptoglobin interactions with the Neisseria meningitidis TonB-dependent receptor HpuAB by flow cytometry.

Authors:  Kyle H Rohde; David W Dyer
Journal:  Infect Immun       Date:  2004-05       Impact factor: 3.441

9.  Identification and characterization of HtsA, a second heme-binding protein made by Streptococcus pyogenes.

Authors:  Benfang Lei; Mengyao Liu; Jovanka M Voyich; Christopher I Prater; Subbarao V Kala; Frank R DeLeo; James M Musser
Journal:  Infect Immun       Date:  2003-10       Impact factor: 3.441

10.  Bis-methionyl coordination in the crystal structure of the heme-binding domain of the streptococcal cell surface protein Shp.

Authors:  Roman Aranda; Chad E Worley; Mengyao Liu; Eduard Bitto; M Susan Cates; John S Olson; Benfang Lei; George N Phillips
Journal:  J Mol Biol       Date:  2007-08-31       Impact factor: 5.469

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