The 'art' genes encode specific arginine uptake proteins, and are repressed by the repressible promoters of ArgR, affecting transcription of artJ [1,2]. Cpb0502, the arginine-binding periplasmic protein 2 precursor from Chlamydophila pneumoniae TW-183 strains, is responsible for arginine transport. As C. pneumoniae is difficult to isolate and culture, there have been many studies of better ways to detect it. A microimmunofluorescence assay (MIF) is still considered to be the 'gold standard' for detecting C. pneumoniae. Although MIF has its own limitations, a number of immunogenic antigens have been shown to be C. pneumoniae specific by this test. Here, we report Cpb0502 as a specific immunogenic antigen against C. pneumoniae as it was detected only in human infection sera of C. pneumoniae but not in Legionella pneumophila and Mycoplasma pneumoniae infection sera, showing high specificity and sensitivity by MIF, western blot and ELISA analysis. And also the crystal structure of Cpb0502 was determined to be a dimer at 2.07. å, revealing a similar backbone structure to a histidine kinase receptor, HK29S. Therefore we may suggest that Cpb0502 is a candidate immunogenic antigen for better diagnosis of C. pneumoniae.
|Number of pages
|Biochemical and biophysical research communications
|Published - 2012 Feb 17
Bibliographical noteFunding Information:
We thank KJ Kim for his assistance in collecting the data at beamlines 4A and 6C of the Pohang Light Source, Korea. This work was supported by grants from the National R&D Program for the Functional Proteomics Center, 21C Frontier Program and in part by Global Frontier Program of a National Research Foundation of Korea (NRF) grant funded by the Korean Government.
- Arginine periplasmic binding protein 2
- Chlamydophila pneumoniae
- Immunogenic antigen
- Serological test
- Structural analysis
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology