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Characterization of I/F1 glycoprotein as a receptor for Mycoplasma pneumoniae

U R Hengge1, M Kirschfink, A L König

  • 1Institute of Immunology, University of Heidelberg, Germany.

Infection and Immunity
|January 1, 1992
PubMed

Insights

Mycoplasma pneumoniae infections involve cold agglutinins that bind to I/Fl glycoprotein on red blood cells. This study identifies I/Fl antigens as the receptors for M. pneumoniae, crucial for understanding infection mechanisms.

Area of Science:

  • Microbiology
  • Immunology
  • Glycobiology

Background:

  • Mycoplasma infections are associated with cold agglutinins, specifically anti-I and anti-Fl.
  • These cold agglutinins suggest a potential interaction between Mycoplasma and erythrocyte surface antigens.

Purpose of the Study:

  • To isolate and characterize the erythrocyte receptor for Mycoplasma pneumoniae.
  • To investigate the role of I/Fl glycoprotein in M. pneumoniae binding.

Main Methods:

  • Isolation of I/Fl glycoprotein from human erythrocyte membranes.
  • Dot blot analysis and hemagglutination assays using sialidase-treated I/Fl glycoprotein and erythrocytes.
  • Hemagglutination inhibition assays to determine receptor structural properties.

Main Results:

  • Mycoplasma pneumoniae demonstrated dose-dependent binding to purified I/Fl glycoprotein.
  • Binding was dependent on sialylated carbohydrate determinants, as evidenced by decreased mycoplasma attachment to sialidase-treated targets.
  • Glycophorins were ruled out as receptors, while I/Fl antigens were confirmed as the binding sites.

Conclusions:

  • The I/Fl antigens on human erythrocyte membranes serve as receptors for Mycoplasma pneumoniae.
  • Understanding this interaction is key to elucidating the pathogenesis of Mycoplasma infections.

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