NDLI: Metal selectivity by the virulence-associated yersiniabactin metallophore system

Please wait, while we are loading the content...

The capability of Pseudomonas aeruginosa to recruit zinc under conditions of limited metal availability is affected by inactivation of the ZnuABC transporter

Contrasting regulation of macrophage iron homeostasis in response to infection with Listeria monocytogenes depending on localization of bacteria

Back cover

Metallomics Vol - 7 Issue - 5

Metallomics Vol - 7 Issue - 4

Metallomics Vol - 7 Issue - 3

Metallomics Vol - 7 Issue - 2

Metal selectivity by the virulence-associated yersiniabactin metallophore system

Content Provider	Royal Society of Chemistry (RSC)
Author	Hung, Chia S. Henderson, Jeffrey P. Giblin, Daryl E. Koh, Eun-Ik Crowley, Jan R. Parker, Kaveri S.
Copyright Year	2015
Abstract	Uropathogenic Escherichia coli secrete siderophores during human infections. Although siderophores are classically defined by their ability to bind iron(III) ions, the virulence-associated siderophore yersiniabactin was recently found to bind divalent copper ions during urinary tract infections. Here we use a mass spectrometric approach to determine the extent of non-iron(III) metal interactions by yersiniabactin and its TonB-dependent outer membrane importer FyuA. In addition to copper, iron and gallium ions, yersiniabactin was also observed to form stable nickel, cobalt, and chromium ion complexes. In E. coli, copper(II) and all other non-iron(III) yersiniabactin complexes were imported by FyuA in a TonB-dependent manner. Among metal–yersiniabactin complexes, copper(II) yersiniabactin is predicted to be structurally distinctive and was the only complex not to competitively inhibit iron(III) yersiniabactin import. These results are consistent with yersiniabactin as part of a metallophore system able to prioritize iron(III) complex uptake in high copper environments.
Starting Page	1011
Ending Page	1022
Page Count	12
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	7
Issue Number	6
Journal	Metallomics
DOI	10.1039/c4mt00341a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Ferric Gallium Siderophore Urinary system Escherichia coli Chromium Ion Nickel Yersiniabactin Copper Cobalt
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Metal selectivity by the virulence-associated yersiniabactin metallophore system

YbtT is a low-specificity type II thioesterase that maintains production of the metallophore yersiniabactin in pathogenic enterobacteria

Back to the metal age: battle for metals at the host–pathogen interface during urinary tract infection

Uropathogenic enterobacteria use the yersiniabactin metallophore system to acquire nickel

The Porphyromonas gingivalis HmuY haemophore binds gallium(iii), zinc(ii), cobalt(iii), manganese(iii), nickel(ii), and copper(ii) protoporphyrin IX but in a manner different to iron(iii) protoporphyrin IX

The role of transition metal transporters for iron, zinc, manganese, and copper in the pathogenesis of Yersinia pestis

The RcnRA (YohLM) system of Escherichia coli: A connection between nickel, cobalt and iron homeostasis

Transition metals in plant photosynthesis

Roles of Escherichia coli ZinT in cobalt, mercury and cadmium resistance and structural insights into the metal binding mechanism

Metal selectivity by the virulence-associated yersiniabactin metallophore system

Similar Documents

Metal selectivity by the virulence-associated yersiniabactin metallophore system

YbtT is a low-specificity type II thioesterase that maintains production of the metallophore yersiniabactin in pathogenic enterobacteria

Back to the metal age: battle for metals at the host–pathogen interface during urinary tract infection

Uropathogenic enterobacteria use the yersiniabactin metallophore system to acquire nickel

The Porphyromonas gingivalis HmuY haemophore binds gallium(iii), zinc(ii), cobalt(iii), manganese(iii), nickel(ii), and copper(ii) protoporphyrin IX but in a manner different to iron(iii) protoporphyrin IX

The role of transition metal transporters for iron, zinc, manganese, and copper in the pathogenesis of Yersinia pestis

The RcnRA (YohLM) system of Escherichia coli: A connection between nickel, cobalt and iron homeostasis

Transition metals in plant photosynthesis

Roles of Escherichia coli ZinT in cobalt, mercury and cadmium resistance and structural insights into the metal binding mechanism

Metal selectivity by the virulence-associated yersiniabactin metallophore system