Metal binding specificity of the MntABC permease of Neisseria gonorrhoeae and its influence on bacterial growth and interaction with cervical epithelial cells

Lim, Karen H. L., Jones, Christopher E., vanden Hoven, Rachel N., Edwards, Jennifer L., Falsetta, Megan L., Apicella, Michael A., Jennings, Michael P. and McEwan, Alastair G. (2008) Metal binding specificity of the MntABC permease of Neisseria gonorrhoeae and its influence on bacterial growth and interaction with cervical epithelial cells. Infection and Immunity, 76 8: 3569-3576. doi:10.1128/IAI.01725-07

Attached Files (Some files may be inaccessible until you login with your UQ eSpace credentials)
Name Description MIMEType Size Downloads
UQ172371_OA.pdf Full text (open access) application/pdf 582.23KB 0

Author Lim, Karen H. L.
Jones, Christopher E.
vanden Hoven, Rachel N.
Edwards, Jennifer L.
Falsetta, Megan L.
Apicella, Michael A.
Jennings, Michael P.
McEwan, Alastair G.
Title Metal binding specificity of the MntABC permease of Neisseria gonorrhoeae and its influence on bacterial growth and interaction with cervical epithelial cells
Formatted title
Metal binding specificity of the MntABC permease of Neisseria gonorrhoeae and its influence on bacterial growth and interaction with cervical epithelial cells
Journal name Infection and Immunity   Check publisher's open access policy
ISSN 1098-5522
1070-6313
Publication date 2008-08-01
Sub-type Article (original research)
DOI 10.1128/IAI.01725-07
Open Access Status File (Publisher version)
Volume 76
Issue 8
Start page 3569
End page 3576
Total pages 8
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Language eng
Abstract mntABC from Neisseria gonorrhoeae encodes an ABC permease which includes a periplasmic divalent cation binding receptor protein of the cluster IX family, encoded by mntC. Analysis of an mntC mutant showed that growth of N. gonorrhoeae could be stimulated by addition of either manganese(II) or zinc(II) ions, suggesting that the MntABC system could transport both ions. In contrast, growth of the mntAB mutant in liquid culture was possible only when the medium was supplemented with an antioxidant such as mannitol, consistent with the view that ion transport via MntABC is essential for protection of N. gonorrhoeae against oxidative stress. Using recombinant MntC, we determined that MntC binds Zn2+ and Mn2+ with almost equal affinity (dissociation constant of ~0.1 µM). Competition assays with the metallochromic zinc indicator 4-(2-pyridylazo)resorcinol showed that MntC binds Mn2+ and Zn2+ at the same binding site. Analysis of the N. gonorrhoeae genome showed that MntC is the only Mn/Zn metal binding receptor protein cluster IX in this bacterium, in contrast to the situation in many other bacteria which have systems with dedicated Mn and Zn binding proteins as part of distinctive ABC cassette permeases. Both the mntC and mntAB mutants had reduced intracellular survival in a human cervical epithelial cell model and showed reduced ability to form a biofilm. These data suggest that the MntABC transporter is of importance for survival of Neisseria gonorrhoeae in the human host.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2009 Higher Education Research Data Collection
School of Chemistry and Molecular Biosciences
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 39 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 37 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Sat, 28 Mar 2009, 01:20:00 EST by Jennifer Falknau on behalf of School of Chemistry & Molecular Biosciences