Infection with Chlamydia trachomatis alters the tyrosine phosphorylation and/or localization of several host cell proteins including cortactin

Infect Immun. 1997 Dec;65(12):5301-8. doi: 10.1128/iai.65.12.5301-5308.1997.


Infection of epithelial cells by two biovars of Chlamydia trachomatis results in the tyrosine phosphorylation of several host proteins. The most prominent change in host protein tyrosine phosphorylation involves a complex of proteins with molecular masses of 75 to 85 kDa (pp75/85) and 100 kDa (pp100). The C. trachomatis-induced tyrosine phosphorylation of pp75/85 and pp100 is observed in several cell lines, including epithelial cells, fibroblasts, and macrophages. Subcellular fractionation and detergent solubility properties of pp75/85 are consistent with its association with the cytoskeleton. Phosphoamino acid analysis demonstrates that the pp75/85 complex is phosphorylated on both tyrosine and serine residues. Immunofluorescence studies of chlamydia-infected cells by using fluorescein isothiocyanate-phalloidin and antibodies to phosphotyrosine and cortactin demonstrate that tyrosine-phosphorylated proteins, as well as cortactin, are localized to the chlamydial vacuole and that this process is facilitated by actin.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Biological Transport
  • Chlamydia Infections / metabolism*
  • Chlamydia trachomatis*
  • Cortactin
  • HeLa Cells
  • Humans
  • Mice
  • Microfilament Proteins / metabolism*
  • Phosphorylation
  • Proteins / metabolism
  • Tyrosine / metabolism


  • CTTN protein, human
  • Cortactin
  • Cttn protein, mouse
  • Microfilament Proteins
  • Proteins
  • Tyrosine