Literature DB >> 21258843

Mechanisms of iron import in anthrax.

Erin Sarah Honsa1, Anthony William Maresso.   

Abstract

During an infection, bacterial pathogens must acquire iron from the host to survive. However, free iron is sequestered in host proteins, which presents a barrier to iron-dependent bacterial replication. In response, pathogens have developed mechanisms to acquire iron from the host during infection. Interestingly, a significant portion of the iron pool is sequestered within heme, which is further bound to host proteins such as hemoglobin. The copious amount of heme-iron makes hemoglobin an ideal molecule for targeted iron uptake during infection. While the study of heme acquisition is well represented in Gram-negative bacteria, the systems and mechanism of heme uptake in Gram-positive bacteria has only recently been investigated. Bacillus anthracis, the causative agent of anthrax disease, represents an excellent model organism to study iron acquisition processes owing to a multifaceted lifecycle consisting of intra- and extracellular phases and a tremendous replicative potential upon infection. This review provides an in depth description of the current knowledge of B. anthracis iron acquisition and applies these findings to a general understanding of how pathogenic Gram-positive bacteria transport this critical nutrient during infection.

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Year:  2011        PMID: 21258843     DOI: 10.1007/s10534-011-9413-x

Source DB:  PubMed          Journal:  Biometals        ISSN: 0966-0844            Impact factor:   2.949


  28 in total

1.  Characterization of heme ligation properties of Rv0203, a secreted heme binding protein involved in Mycobacterium tuberculosis heme uptake.

Authors:  Cedric P Owens; Jing Du; John H Dawson; Celia W Goulding
Journal:  Biochemistry       Date:  2012-02-08       Impact factor: 3.162

2.  Corynebacterium diphtheriae Iron-Regulated Surface Protein HbpA Is Involved in the Utilization of the Hemoglobin-Haptoglobin Complex as an Iron Source.

Authors:  Lindsey R Lyman; Eric D Peng; Michael P Schmitt
Journal:  J Bacteriol       Date:  2018-03-12       Impact factor: 3.490

3.  Heme Binding by Corynebacterium diphtheriae HmuT: Function and Heme Environment.

Authors:  Elizabeth B Draganova; Neval Akbas; Seth A Adrian; Gudrun S Lukat-Rodgers; Daniel P Collins; John H Dawson; Courtni E Allen; Michael P Schmitt; Kenton R Rodgers; Dabney W Dixon
Journal:  Biochemistry       Date:  2015-10-26       Impact factor: 3.162

4.  Characterization of the second conserved domain in the heme uptake protein HtaA from Corynebacterium diphtheriae.

Authors:  Rizvan C Uluisik; Neval Akbas; Gudrun S Lukat-Rodgers; Seth A Adrian; Courtni E Allen; Michael P Schmitt; Kenton R Rodgers; Dabney W Dixon
Journal:  J Inorg Biochem       Date:  2016-11-23       Impact factor: 4.155

5.  Progress toward the Development of a NEAT Protein Vaccine for Anthrax Disease.

Authors:  Miriam A Balderas; Chinh T Q Nguyen; Austen Terwilliger; Wendy A Keitel; Angelina Iniguez; Rodrigo Torres; Frederico Palacios; Celia W Goulding; Anthony W Maresso
Journal:  Infect Immun       Date:  2016-11-18       Impact factor: 3.441

6.  The five near-iron transporter (NEAT) domain anthrax hemophore, IsdX2, scavenges heme from hemoglobin and transfers heme to the surface protein IsdC.

Authors:  Erin Sarah Honsa; Marian Fabian; Ana Maria Cardenas; John S Olson; Anthony William Maresso
Journal:  J Biol Chem       Date:  2011-08-01       Impact factor: 5.157

Review 7.  Heme uptake in bacterial pathogens.

Authors:  Heidi Contreras; Nicholas Chim; Alfredo Credali; Celia W Goulding
Journal:  Curr Opin Chem Biol       Date:  2014-01-04       Impact factor: 8.822

8.  Corynebacterium diphtheriae HmuT: dissecting the roles of conserved residues in heme pocket stabilization.

Authors:  Elizabeth B Draganova; Seth A Adrian; Gudrun S Lukat-Rodgers; Cyrianne S Keutcha; Michael P Schmitt; Kenton R Rodgers; Dabney W Dixon
Journal:  J Biol Inorg Chem       Date:  2016-08-25       Impact factor: 3.358

9.  Spectroscopic evidence for a 5-coordinate oxygenic ligated high spin ferric heme moiety in the Neisseria meningitidis hemoglobin binding receptor.

Authors:  David Z Mokry; Angela Nadia-Albete; Michael K Johnson; Gudrun S Lukat-Rodgers; Kenton R Rodgers; William N Lanzilotta
Journal:  Biochim Biophys Acta       Date:  2014-06-23

10.  Heme-bound SiaA from Streptococcus pyogenes: Effects of mutations and oxidation state on protein stability.

Authors:  Neval Akbas; Elizabeth B Draganova; Darci R Block; Brian R Sook; Yau Fong Chan; Joy Zhuo; Zehava Eichenbaum; Kenton R Rodgers; Dabney W Dixon
Journal:  J Inorg Biochem       Date:  2015-11-14       Impact factor: 4.155

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