Title Proteomic Analysis of Protein Expression in Streptococcus pneumoniae in Response to Temperature Shift
Author Myoung-Ro Lee1, Song-Mee Bae2, Tong-Soo Kim1, and Kwang-Jun Lee*1,2
Address 1Lab. of Pathogenic Proteomics, Center for Immunology and Pathology, National Institute of Health, Korea Center for Diseases control and Prevention, 5 Nokbun-Dong, Eunpyung-Ku, Seoul 122-701, Republic of Korea, 2Division of Bacterial Respiratory Infections, Center for Infectious Disease, National Institute of Health, Korea Center for Diseases control and Prevention, 5 Nokbun-Dong, Eunpyung-Ku, Seoul 122-701, Republic of Korea
Bibliography Journal of Microbiology, 44(4),p.375-382, 2006,
DOI
Key Words heat shock, two-dimensional gel electrophoresis, Streptococcus pneumoniae
Abstract From its initial colonization to causation of disease, Streptococcus pneumoniae has evolved strategies to cope with a number of stressful in vivo environmental conditions. In order to analyze a global view of this organism’s response to heat shock, we established a 2-D electrophoresis proteome map of the S. pneumoniae D39 soluble proteins under in vitro culture conditions and performed the comparative proteome analysis to a 37 to 42°C temperature up-shift in S. pneumoniae. When the temperature of an exponentially growing S. pneumoniae D39 culture was raised to 42°C, the expression level of 25 proteins showed changes when compared to the control. Among these 25 proteins, 12 were identified by MALDI-TOF and LC-coupled ESI MS/MS. The identified proteins were shown to be involved in the general stress response, energy metabolism, nucleotide biosynthesis pathways, and purine metabolism. These results provide clues for understanding the mechanism of adaptation to heat shock by S. pneumoniae and may facilitate the assessment <br>of a possible role for these proteins in the physiology and pathogenesis of this pathogen.
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