Jump to main content
Jump to site search

Issue 30, 2019
Previous Article Next Article

Antimicrobial silver targets glyceraldehyde-3-phosphate dehydrogenase in glycolysis of E. coli

Author affiliations

Abstract

Silver has long been used as an antibacterial agent, yet its molecular targets remain largely unknown. Using a custom-designed coupling of gel electrophoresis with inductively coupled plasma mass spectrometry (GE-ICP-MS), we identified six silver-binding proteins in E. coli. The majority of the identified proteins are associated with the central carbon metabolism of E. coli. Among them, we unveil that GAPDH, an essential enzyme in glycolysis, serves as a vital target of Ag+ in E. coli for the first time. We demonstrate that silver inhibits the enzymatic function of GAPDH through targeting Cys149 in its catalytic site. The X-ray structure reveals that Ag+ coordinates to Cys149 and His176 with a quasi-linear geometry (S–Ag–N angle of 157°). And unexpectedly, two Ag+ ions coordinate to Cys288 in the non-catalytic site with weak argentophilic interaction (Ag⋯Ag distance of 2.9 Å). This is the first report on antimicrobial Ag+ targeting a key enzyme in the glycolytic pathway of E. coli. The findings expand our knowledge on the mode of action and bio-coordination chemistry of silver, particularly silver-targeting residues in proteins at the atomic level.

Graphical abstract: Antimicrobial silver targets glyceraldehyde-3-phosphate dehydrogenase in glycolysis of E. coli

Back to tab navigation

Supplementary files

Article information


Submitted
24 Apr 2019
Accepted
14 Jun 2019
First published
24 Jun 2019

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2019,10, 7193-7199
Article type
Edge Article

Antimicrobial silver targets glyceraldehyde-3-phosphate dehydrogenase in glycolysis of E. coli

H. Wang, M. Wang, X. Yang, X. Xu, Q. Hao, A. Yan, M. Hu, R. Lobinski, H. Li and H. Sun, Chem. Sci., 2019, 10, 7193
DOI: 10.1039/C9SC02032B

This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material and it is not used for commercial purposes.

Reproduced material should be attributed as follows:

  • For reproduction of material from NJC:
    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
  • For reproduction of material from PCCP:
    [Original citation] - Published by the PCCP Owner Societies.
  • For reproduction of material from PPS:
    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
  • For reproduction of material from all other RSC journals:
    [Original citation] - Published by The Royal Society of Chemistry.

Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.


Social activity

Search articles by author

Spotlight

Advertisements