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Background  The response of the NarQP two-component signal transduction system regulon in response to the presence of nitrate for the bovine pathogen  Mannheimia haemolytica  A1 was investigated by proteomic analysis. Total proteins from a  narP  mutant and the parent SH1217 grown with or without NaNO 3  supplement were examined by ISO-DALT 2D electrophoresis and liquid chromatography-mass spectrometry.    Results  Seventeen proteins were differentially expressed in the parent strain SH1217 in response to the addition of NaNO 3  to the growth media. These responses were absent in the  narP  mutant, indicating that the altered production of these proteins is mediated by NarP  Mh  . Interestingly, NarP  Mh   mediated the increased production of some proteins which are not generally associated with nitrate respiration, such as the iron transporters FbpA and YfeA. The increased production of proteins such as superoxide dismutase, SodA, and GAPDH were also observed. The increased production of these iron-regulated proteins by NarP  Mh   is thought to enhance the swift establishment of the nitrate respiration mechanism of  M. haemolytica  during pathogenesis.    Conclusion  The data suggested NarP  Mh   acts as an important regulator which regulates the expression of a small set of proteins in response to nitrate availability. This may contribute to the prevalence of  M. haemolytica  A1 in its host during pathogenesis of BPP, through enhancing the effectiveness of nitrate respiration either directly or indirectly.

A proteomic analysis of the regulon of the NarP two-component regulatory system response regulator in the bovine pathogen Mannheimia haemolytica A1