Characterisation of complex formation between members of the Mycobacterium tuberculosis complex CFP-10/ESAT-6 protein family: Towards an understanding of the rules governing complex formation and thereby functional flexibility

Kirsty L. Lightbody, Philip S. Renshaw, Michelle L. Collins, Rebecca L. Wright, Debbie M. Hunt, Stephen V. Gordon, R. Glyn Hewinson, Roger S. Buxton, Richard A. Williamson, Mark D. Carr

Research output: Contribution to journalArticlepeer-review

41 Citations (SciVal)

Abstract

We have previously shown that the secreted M. tuberculosis complex proteins CFP-10 and ESAT-6 form a tight, 1:1 complex, which may represent their functional form. In the work reported here a combination of yeast two-hybrid and biochemical analysis has been used to characterise complex formation between two other pairs of CFP-10/ESAT-6 family proteins (Rv0287/Rv0288 and Rv3019c/Rv3020c) and to determine whether complexes can be formed between non-genome paired members of the family. The results clearly demonstrate that Rv0287/Rv0288 and Rv3019c/3020c form tight complexes, as initially observed for CFP-10/ESAT-6. The closely related Rv0287/Rv0288 and Rv3019c/Rv3020c proteins are also able to form non-genome paired complexes (Rv0287/Rv3019c and Rv0288/Rv3020c), but are not capable of binding to the more distantly related CFP-10/ESAT-6 proteins.

Original languageEnglish
Pages (from-to)255-262
Number of pages8
JournalFEMS Microbiology Letters
Volume238
Issue number1
Early online date29 Jul 2004
DOIs
Publication statusPublished - 01 Sept 2004

Keywords

  • CFP-10
  • ESAT-6
  • ESAT-6 family members
  • Protein-protein interaction
  • Tuberculosis

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