Oral Presentation BacPath 13: Molecular Analysis of Bacterial Pathogens Conference 2015

Cadmium-induced mismetallation causes dysregulation of transition metal-ion homeostasis in Streptococcus pneumoniae (#34)

Stephanie Begg 1 , Bart Eijkelkamp 1 , Zhenyao Luo 2 , Rafael Counago 2 , Jacqueline Morey 1 , Megan Maher 3 , Cheryl-lynn Ong 2 , Alastair McEwan 2 , Bostjan Kobe 2 , Megan O'Mara 2 , James Paton 1 , Christopher McDevitt 1
  1. Research Centre for Infectious Diseases, University of Adelaide, Adelaide, SA, Australia
  2. School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, QLD, Australia
  3. La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC, Australia

Streptococcus pneumoniae (the pneumococcus) is the world’s foremost bacterial pathogen, responsible for more than one million deaths each year. As a host-adapted pathogen, S. pneumoniae is able to colonise multiple anatomical niches, all of which have distinct extracellular environments. Adaptation to fluctuating metal-ion concentrations at the host-pathogen interface is essential for successful colonisation and presents a major challenge for invasive bacterial pathogens. S. pneumoniae addresses this by using a combination of metal homeostatic mechanisms to tightly regulate intracellular metal concentrations. However, the molecular details of how this is achieved remains poorly understood.

Recently we showed that selective metal-ion uptake was dependent upon essential protein-metal interactions that were dictated by a complex interplay of metal-ion coordination chemistry at the metal-binding site (Couñago, Ween, Begg et al 2014. Nature Chemical Biology). However, our work also revealed that the intrinsic flexibility within protein structures permitted non-physiological ions, such as cadmium, to subvert these selectivity determinants, resulting in non-cognate interactions (mismetallation). Here we show that although PsaA, the manganese-binding protein of S. pneumoniae, has evolved to optimally bind and release manganese, imperfect steric selection of metal-ions also make it permissive for the acquisition of cadmium. Here, we combined transcriptional analyses, whole cell metal-ion determination, scanning electron microscopy, and high-resolution structural data, to show that the inability of the pneumococcus to regulate cadmium uptake resulted in a dramatic decrease in the cellular accumulation of manganese and zinc ions. This was due to mismetallation of the proteins involved in metal-ion uptake and efflux, as well as other metal-responsive transcriptional regulators. This resulted in a global dysregulation of pneumococcal metal homeostasis (Begg et al 2015. Nature Communications). Collectively, our work provides new insights into fundamental aspects of bacterial metal-ion homeostasis and also reveals how chemically similar metal-ions can disturb the molecular determinants responsible for metal-ion selection.