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International Journal of Microbiology
Volume 2014 (2014), Article ID 918143, 9 pages
http://dx.doi.org/10.1155/2014/918143
Research Article

The TIR Domain Containing Locus of Enterococcus faecalis Is Predominant among Urinary Tract Infection Isolates and Downregulates Host Inflammatory Response

1Institute of Medical Microbiology, Justus Liebig University, Schubertstraße 81, 35392 Giessen, Germany
2Iztacala Superior Studies Faculty, National Autonomous University of Mexico, Avenida de los Barrios 1, Los Reyes Iztacala, 54090 Tlalnepantla, MEX, Mexico

Received 3 April 2014; Revised 11 June 2014; Accepted 30 June 2014; Published 24 July 2014

Academic Editor: Michael McClelland

Copyright © 2014 Thomas Daniel Kraemer et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Supplementary Material

Supplementary Figure 1: The primary sequence of TcpF-TIR exhibits common TIR domain motifs. Primary sequence alignment of human Tcps involved in TLR2 signaling and bacterial Tcps of Paracoccus denitrificans (PdTIR), Escherichia coli (TcpC-TIR) and Enterococcus faecalis (TcpF-TIR). The regions corresponding to the conserved TIR motifs, boxes 1,2 and 3 are indicated by red, blue and yellow rectangles, respectively. Secondary structure elements of TLR1-TIR (PDB: 1FYV) are shown above the alignment. The alignment was generated using ClustalOmega.

Supplementary Figure 2: In silico structure prediction of TcpF-TIR reveals structural similarity to TLR1-TIR. (A) Predicted tertiary-structure of TcpF-TIR (residues 7-128). According to previous studies α- helices are labeled as α(A-B) and β-pleated sheets as β(A-B). (B) Superposition of TcpF-TIR and TLR1-TIR (PDB: 1FYV). TcpF-TIR is colored in magenta and TLR1-TIR in green. Secondary structure elements of TcpF-TIR are labeled as previously described. The BB-loop refers to the connecting loop between the second β-pleated sheet (βB) and the second α-helix (αB). (C) Structural alignment of the BB-loops of TcpF-TIR and TLR1-TIR. TcpF-TIR is colored in magenta and TLR1-TIR in green. Residue positions refer to sequences of TcpF and TLR1.Protein tertiary-structure prediction based on homology detection was performed using HHpred by the Max-Planck Institute for Developmental Biology. Structural alignment was generated using TM-align by Zhang-Lab and illustration was composed using pymol (Schroedinger). (D) Superposition of TcpF-TIR (magenta) and its Ala41Thr (blue) mutant. (E) Superposition of TcpF-TIR (magenta) and its Gln76Lys (blue) mutant.

  1. Supplementary Material