| Autor: |
Schumann, Gisbert, Schleier, Susanne, Rosenkrands, Ida, Nehmann, Nina, Hälbich, Steffi, Zipfel, Peter, Jonge, Marien, Cole, Stewart, Munder, Thomas, Möllmann, Ute |
| Zdroj: |
Central European Journal of Biology; Jun2006, Vol. 1 Issue 2, p183-202, 20p |
| Abstrakt: |
In order to study the function of the Mycobacterium tuberculosis protein ESAT-6 in the infection process, we searched for host proteins that interact with this secreted mycobacterial protein. Using a yeast two-hybrid system we identified the rat syntenin-1 protein as a candidate to interact with ESAT-6. This interaction was confirmed in vitro by protein overlay and by surface plasmon resonance using recombinant ESAT-6 and human syntenin-1, and by co-purification analysis of the mycobacterial expressed ESAT-6 and macrophage derived syntenin-1. The interaction domains were localized by two-hybrid studies using truncated derivatives of both proteins and by peptide spot analysis. Two domains of each protein mediate the ESAT-6/syntenin-1 interaction. The C-terminus of ESAT-6 binds to the PDZ-domains of syntenin-1 and the N-terminus of ESAT-6 binds to the N-terminus of syntenin-1. Thus, the host protein syntenin-1 represents a possible cellular receptor for the mycobacterial protein ESAT-6. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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