Molecular basis of PE and PPE protein-protein interactions in Mycobacterium tuberculosis
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AbstractTuberculosis is an infectious disease with global significance, millions of people are infected with Mycobacterium tuberculosis every year. About 10% of the coding sequence of Mycobacterium tuberculosis corresponds to the PE/PPE protein family members, which has been shown to be important for infection, antigenic variation, immune evasion, virulence and host signal transduction. However, a major obstacle to understand the structure-function of these PE or PPE proteins relies on purification of soluble protein samples as many of these PE/PPE proteins require a cognate protein partner to enhance proper folding and stability. To date, only the crystal structure of PE25/PPE41 complex has been determined. In this study, potential PE-PPE pairs were identified by yeast two-hybrid screen, and validated by pull-down assays. The confirmed pairs were further subjected to large-scale co-expression and purification. In the process of exploration and optimization of PE-PPE purification, the minimal regions required for molecular interaction of PE-PPE pair were identified using limited proteolysis analysis combined with mass spectrometry and pull down assay, At present, crystallization studies of the purified complex are underway and functional analysis will be performed in the future. Structural and functional information obtained from this PE-PPE pair will provide insight to elucidate the pathogenesis of Mtb and to design novel intervention against TB.
All Author(s) ListCHEN, Xin; AU Wing Ngor Shannon
Name of ConferenceNew Approaches and Concepts in Microbiology
Start Date of Conference27/06/2017
End Date of Conference30/06/2017
Place of ConferenceHeidelberg
Country/Region of ConferenceGermany
LanguagesEnglish-United States

Last updated on 2018-18-01 at 08:22