Chlamydia trachomatis and Chlamydia pneumoniae bind specifically to phosphatidylethanolamine in HeLa cells and to GalNAc beta 1-4Gal beta 1-4GLC sequences-found in asialo-GM1 and asial-GM2

Biochem Biophys Res Commun. 1991 Mar 29;175(3):1082-9. doi: 10.1016/0006-291x(91)91676-4.


To examine the possible role of lipids as adhesion receptors for infection, Chlamydia trachomatis and Chlamydia pneumoniae were labeled with 125I and layered on thin-layer chromatograms (tlc) of separated lipids isolated from target cells, and bound bacteria were detected by autoradiography. Elementary bodies from both species bound specifically and with high affinity to one lipid in HeLa 229 cells. Purification of this receptor by column chromatography on DEAE Sepharose followed by continuous preparative tlc, and structural analysis by 500-MHz 1H-NMR spectroscopy and fast atom bombardment mass spectrometry confirmed the HeLa cell chlamydial receptor to be phosphatidylethanolamine (PE). The chlamydiae also bound strongly to purified asialo-GM1 and asialo-GM2, but not to other neutral or acidic lipids tested. The relative binding of chlamydiae to human PE and asialo-GM1 was modified in the presence divalent cations, suggesting that chlamydiae have two interrelated receptor binding sites.

MeSH terms

  • Bacterial Adhesion* / physiology*
  • Bacterial Proteins*
  • Carbohydrate Sequence
  • Cell Line
  • Chlamydia / physiology*
  • Chlamydia trachomatis / physiology*
  • Female
  • G(M1) Ganglioside*
  • Gangliosides
  • Glycolipids / physiology*
  • Glycosphingolipids / physiology*
  • HeLa Cells / physiology
  • Humans
  • Kinetics
  • Molecular Sequence Data
  • Vagina


  • Bacterial Proteins
  • Gangliosides
  • Glycolipids
  • Glycosphingolipids
  • ganglio-N-triaosylceramide
  • G(M1) Ganglioside
  • asialo GM1 ganglioside