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The M. tuberculosis antigen 85 complex and mycolyltransferase activity

L Kremer1, W N Maughan, R A Wilson

  • 1Department of Microbiology & Immunology, University of Newcastle upon Tyne, UK.

Letters in Applied Microbiology
|April 10, 2002
PubMed
Abstract

Insights

Mycobacterium tuberculosis antigen 85 complex (Ag85) proteins FbpA, FbpB, and FbpC2 have mycolyltransferase activity. FbpC1, a related protein, was investigated and found to lack this activity, suggesting its function remains unknown.

Area of Science:

  • Microbiology
  • Biochemistry
  • Tuberculosis research

Background:

  • The antigen 85 complex (Ag85) in Mycobacterium tuberculosis includes FbpA, FbpB, and FbpC2, crucial for pathogenesis and mycolyltransferase activity.
  • A newly identified protein, FbpC1, shares similarity with the Ag85 complex.

Purpose of the Study:

  • To investigate whether FbpC1 possesses mycolyltransferase activity, a hallmark of the Ag85 complex.
  • To determine the specific proteins within the Ag85 complex responsible for mycolyltransferase activity.

Main Methods:

  • Heterologous expression of FbpA, FbpC1, and FbpC2 in Escherichia coli.
  • Purification of recombinant proteins under non-denaturing conditions.
  • In vitro mycolyltransferase assay to assess enzyme activity.

Main Results:

  • Recombinant FbpC1 did not exhibit in vitro mycolyltransferase activity.
  • FbpC1 was not recognized by monoclonal antibodies specific to the native Ag85 complex.
  • FbpA and FbpC2 demonstrated mycolyltransferase activity, consistent with known functions.

Conclusions:

  • Mycolyltransferase activity is confined to FbpA, FbpB, and FbpC2 within the Ag85 family.
  • The specific biological role of FbpC1 in Mycobacterium tuberculosis requires further investigation.

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