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. 2017 Jan 30;8:15. doi: 10.3389/fendo.2017.00015

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Copyright © 2017 N’Diaye, Gannesen, Borrel, Maillot, Enault, Racine, Plakunov, Chevalier, Lesouhaitier and Feuilloley.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Bacterial substance P (SP) and calcitonin gene-related peptide (CGRP) sensors. The thermo unstable ribosomal elongation factor EfTu identified as SP sensor is a 395 amino acids protein (43 kDa) characterized by three principal domains (A). Domain I is essentially organized in alpha helix whereas II and III form beta strands. No signal sequence or transmembrane domain signature is present. EfTu is not showing significant sequence or structural similarities with the NK1 SP human receptor (B). The Staphylococcus epidermidis chaperone DnaK identified as CGRP sensor is a 609 amino acids protein (70 kDa) (C). This protein is showing limited similarity with the human CGRP receptor component protein (CGRP-RCP) but higher similarity with an invertebrate (Ciona intestinalis) CGRP-RCP (124 amino acids) where DnaK was found covering 45% of its sequence with 40% identity (D). Sequence similarities were investigated by BlastP (https://blast.ncbi.nlm). 3D structures were calculated by RaptorX (31) and visualized using Python Molecular Viewer V1.5.6.