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

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.

journal_name

Proteomics

journal_title

Proteomics

authors

Okkels LM,Müller EC,Schmid M,Rosenkrands I,Kaufmann SH,Andersen P,Jungblut PR

doi

10.1002/pmic.200400906

subject

Has Abstract

pub_date

2004-10-01 00:00:00

pages

2954-60

issue

10

eissn

1615-9853

issn

1615-9861

journal_volume

4

pub_type

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