Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/14841
Title: Immunomodulatory roles of heat shock proteins
Authors: NG KIAN HONG
Keywords: Heat shock protein; cross-presentation; LPS contamination; intranasal immunization; regulatory cells; Drosophila Expression System
Issue Date: 7-Jun-2005
Source: NG KIAN HONG (2005-06-07). Immunomodulatory roles of heat shock proteins. ScholarBank@NUS Repository.
Abstract: Heat shock proteins (HSPs) are evolutionary conserved proteins that play essential roles in protein folding, trafficking and degradation. Recently, their immunological roles have been reported and reviewed. In our present studies, we sought to understand the immunomodulatory roles of Burkholderia pseudomallei Hsp70, Hsp60 and Mycobacterium bovis Hsp65 collectively. We found that these HSPs could promote cross-presentation of exogenous ovalbumin on the dendritic cells, DC2.4 to a T cell hybridoma, B3Z. This process was found to be independent of LPS contamination and CD54 expression. In addition, our results suggest that the effect of HSPs on enhancement of cross-presentation involves the initial steps of antigen processing. Furthermore, our data strongly suggest that LPS contamination in the HSP preparations have been contributing to the release of TNF-alpha and activation of NF-kappaB in DC. In a mouse model of intranasal immunization, we are able to detect HSP-specific IgG and IgA in the serum and nasal wash, respectively in the mice after intranasal immunization. Surprisingly, HSP-immunization is also shown to induce regulatory cells secreting IL-10. Finally, we report the successful cloning and expression of human Hsp72, B. pseudomallei Hsp70 and Hsp60 in the endotoxin-free Drosophila Expression System (DES).
URI: http://scholarbank.nus.edu.sg/handle/10635/14841
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