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Papers In Press, published online ahead of print October 31, 2005
Research Center for Infectious Diseases, University of Würzburg, Würzburg 97070
Corresponding Author: s.hammerschmidt{at}mail.uni-wuerzburg.de
Streptococcus pneumoniae expresses two surface-exposed lipoproteins, PpmA and SlrA, which share homology with distinct families of peptidyl-prolyl isomerases (PPIases). In this study, we demonstrated for the first time that the lipoprotein cyclophilin, SlrA, can catalyse the cis-trans isomerisation of proline containing tetrapeptides and that SlrA contributes to pneumococcal colonisation. The substrate specificity of SlrA is typical for prokaryotic and eukaryotic cyclophilins, with Suc-Ala-Ala-Pro-Phe-pNA being the most rapidly catalysed substrate. In a mouse pneumonia model the slrA knockout D39slrA did not cause significant differences in the survival times of mice compared to the isogenic wild-type strain. In contrast, a detailed analysis of bacterial outgrowth over time in the nasopharynx, airways, lungs, blood, and spleen, showed a rapid elimination of slrA mutants from the upper airways but did not reveal significant differences in the lungs, blood and spleen. These results suggested that SlrA is involved in colonisation but does not contribute significantly to invasive pneumococcal disease. In cell culture infection experiments, the absence of SlrA impaired adherence to pneumococcal disease specific epithelial and endothelial non-professional cell lines. Adherence of the slrA mutant could not be restored by exogenously added SlrA. Strikingly, deficiency in SlrA did not reduce binding activity to host target proteins, but resulted in enhanced uptake by professional phagocytes. In conclusion, SlrA is a functional, cyclophilin-type PPIase and contributes to pneumococcal virulence in the first stage of infection, namely, colonisation of the upper airways, most likely by modulating the biological function of important virulence proteins.
J. Biol. Chem, 10.1074/jbc.M510014200
Submitted on September 12, 2005
Accepted on October 31, 2005
The streptococcal lipoprotein rotamase A (SlrA) is a functional peptidyl-prolyl isomerase involved in pneumococcal colonisation
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