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Chlamydia trachomatis Mip-like protein.

A G Lundemose1, D A Rouch, S Birkelund

  • 1Institute of Medical Microbiology, University of Aarhus, Denmark.

Molecular Microbiology
|September 1, 1992
PubMed
Summary
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Chlamydia trachomatis possesses a Mip-like protein conserved across serovars. Antibodies targeting its N-terminal fragment inhibit chlamydial infectivity, indicating accessible epitopes on infectious elementary bodies.

Area of Science:

  • Microbiology
  • Immunology
  • Molecular Biology

Background:

  • Chlamydia trachomatis is a significant human pathogen.
  • A Mip-like protein in C. trachomatis shares homology with Legionella pneumophila Mip.
  • This protein resembles eukaryotic and prokaryotic FK506-binding proteins.

Purpose of the Study:

  • To present the full sequence of the C. trachomatis Mip-like protein.
  • To investigate the conservation of the chlamydial Mip-like gene.
  • To determine the surface exposure of Mip-like protein epitopes and their role in infectivity.

Main Methods:

  • DNA sequencing of the Mip-like gene from C. trachomatis serovar L2.
  • Polymerase chain reaction (PCR) to detect the gene in other serovars.

Related Experiment Videos

  • Antibody production and immunofluorescence/immuno-gold electron microscopy to assess epitope accessibility.
  • Complement-dependent infectivity inhibition assays.

    • Main Results:

    • The complete Mip-like sequence of C. trachomatis serovar L2 was determined.
    • The chlamydial mip-like gene is highly conserved across major C. trachomatis biovars.
    • Antibodies against the recombinant Mip-like protein did not detect surface-exposed epitopes on elementary bodies or reticulate bodies.
    • Antibodies against the N-terminal fragment inhibited up to 91% of cell culture infectivity.

    Conclusions:

    • The C. trachomatis Mip-like protein is conserved and shares similarities with known FK506-binding proteins.
    • Antibody-accessible epitopes are present on the N-terminus of the Mip-like protein on infectious elementary bodies.
    • These findings suggest a potential role for the N-terminal region in chlamydial infectivity and host interaction.