a proteomic analysis of the regulon of the narp two-component regulatory system response regulator in the bovine pathogen mannheimia haemolytica a1蛋白质组学分析的调节子narp双组分监管系统响应监管机构在牛病原体mannheimia haemolytica a1.pdfVIP
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a proteomic analysis of the regulon of the narp two-component regulatory system response regulator in the bovine pathogen mannheimia haemolytica a1蛋白质组学分析的调节子narp双组分监管系统响应监管机构在牛病原体mannheimia haemolytica a1
Inamoto and Lo BMC Research Notes 2011, 4:510
/1756-0500/4/510
RESEARCH ARTICLE Open Access
A proteomic analysis of the regulon of the NarP
two-component regulatory system response
regulator in the bovine pathogen Mannheimia
haemolytica A1
*
Ichiro Inamoto and Reggie Lo YC Lo
Abstract
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 NaNO3 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 NaNO3 to the growth media. These responses were absent in the narP mutant, indicating that the altered
production of these proteins is mediated by NarPMh. Interestingly, NarPMh 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 NarPMh is thought to enhance the swift
establishment of the nitrate respiration mechanism of M. haemolytica during pathogenesis.
Conclusion: The data suggested NarPMh 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
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