CFP10 discriminates between nonacetylated and acetylated ESAT‐6 of Mycobacterium tuberculosis by differential interaction

Proteomics - Tập 4 Số 10 - Trang 2954-2960 - 2004
Limei Meng Okkels1,2, Eva‐Christina Müller3, Monika Schmid2, Ida Rosenkrands1, Stefan H. E. Kaufmann4, Peter Andersen1, Peter R. Jungblut2
1Department of Infectious Disease Immunology, Statens Serum Institut, Copenhagen, Denmark
2Max-Planck-Institute for Infection Biology, Core Facility Protein Analysis, Berlin, Germany
3Max Delbrück Center for Molecular Medicine, Neuroproteomics, Berlin, Germany
4Max Planck Institute for Infection Biology, Department of Immunology, Berlin, Germany

Tóm tắt

Abstract

ESAT‐6 (the 6 kDa early secreted antigenic target) protein species in short‐term culture filtrate of Mycobacterium tuberculosis were separated in a 4–5 narrow range pI gradient two‐dimensional gel electrophoresis (2‐DE). Eight ESAT‐6 protein species were analyzed in detail by peptide mass fingerprinting matrix‐assisted laser desorption/ionization‐mass spectrometry as well as by electrospray ionization‐tandem mass spectrometry. An N‐terminal Thr acetylation was identified in four species and a C‐terminal truncation was identified in two species. In 2‐DE blot overlay assays, the recombinant 10 kDa culture filtrate protein (CFP10) discriminated N‐terminal acetylated and nonacetylated ESAT‐6 by differential interaction, whereas removal of the C‐terminal 11 residues of ESAT‐6 had no effects thereon. This example shows that the access to the protein species level can be a prerequisite to understand regulation of protein‐protein interaction.

Từ khóa


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Proteomics

Tập 4 Số 10

2954-2960

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