Heat-shock response in Brucella abortus
Abstract number: P964
Amir Mozaffari N., Rajabnia R.
Objectives: Heat shock proteins are highly conserved molecules and serve a variety of functions in bacterial cells including protein folding and transport. They mainly serve to protect cells from various forms of stresses including heat shocks. In reference to the potent antigenicity of hsp and its activation of macrophages, the differences in virulence of Brucella cells may be originated from differences in patterns of response to heat shocks induced by the high degrees of fever that is usually manifested in brucellosis.
Methods: Five B. abortus strains, isolated from human and cows, were subjected to 39, 40, and 42 Celsius degrees heat treatments. The bacterial whole cell proteins were extracted and resolved by SDS-PAGE electrophoresis. Western blottings were used to detect antibody production against the extracted bacterial proteins especially hsp60 in both control and patient sera.
Results: SDS-PAGE gels revealed protein bands mainly in the range of 10100 KDa. The amounts of a 60 KDa protein band (hsp60) was significantly enhanced following heat shocks in relation to the unheated bacterial cells. The heat shock response points to a significant higher production of a 60 KDa protein (hsp60). The sera from brucellosis patients reacted with several of these cell derived protein bands in western blots, none of which were reactive with sera from healthy individuals. The western blot protein bands showed striking differences.
Conclusion: The results of this study point to the immunogenic properties of Brucella heat shock proteins, especially the overwhelming response towards hsp60. Therefore, hsp60 can be an appropriate antigenic candidate for engineering subunit vaccine against Brucella, as well as for ELISA test development.
|Session name:||18th European Congress of Clinical Microbiology and Infectious Diseases|
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