A chlamydial type III translocated protein is tyrosine-phosphorylated at the site of entry and associated with recruitment of actin

D. R. Clifton, K. A. Fields, S. S. Grieshaber, C. A. Dooley, E. R. Fischer, D. J. Mead, R. A. Carabeo, T. Hackstadt

Research output: Contribution to journalArticle

276 Citations (Scopus)

Abstract

The obligate intracellular bacterium Chlamydia trachomatis rapidly induces its own entry into host cells. Initial attachment is mediated by electrostatic interactions to heparan sulfate moieties on the host cell, followed by irreversible binding to an unknown secondary receptor. This secondary binding leads to the recruitment of actin to the site of attachment, formation of an actin-rich, pedestal-like structure, and finally internalization of the bacteria. How chlamydial induce this process is unknown. We have identified a high-molecular-mass tyrosine-phosphorylated protein that is rapidly phosphorylated on attachment to the host cell. Immunoelectron microscopy studies revealed that this tyrosine-phosphorylated protein is localized to the cytoplasmic face of the plasma membrane at the site of attachment of surface-associated chlamydiae. The phosphoprotein was isolated by immunoprecipitation with the antiphosphotyrosine antibody 4G10 and identified as the chlamydial protein CT456, a hypothetical protein with unknown function. The chlamydial protein (Tarp) appears to be translocated into the host cell by type III secretion because it is exported in a Yersinia heterologous expression assay. Phosphotyrosine signaling across the plasma membrane preceded the recruitment of actin to the site of chlamydial attachment and may represent the initial signal transduced from pathogen to the host cell. These results suggest that C. trachomatis internalization is mediated by a chlamydial type III-secreted effector protein.

Original languageEnglish
Pages (from-to)10166-10171
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume101
Issue number27
DOIs
StatePublished - Jul 6 2004

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Tyrosine
Actins
Proteins
Chlamydia trachomatis
Cell Membrane
Bacteria
Yersinia
Phosphotyrosine
Heparitin Sulfate
Immunoelectron Microscopy
Chlamydia
Phosphoproteins
Static Electricity
Immunoprecipitation
Antibodies

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

A chlamydial type III translocated protein is tyrosine-phosphorylated at the site of entry and associated with recruitment of actin. / Clifton, D. R.; Fields, K. A.; Grieshaber, S. S.; Dooley, C. A.; Fischer, E. R.; Mead, D. J.; Carabeo, R. A.; Hackstadt, T.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 101, No. 27, 06.07.2004, p. 10166-10171.

Research output: Contribution to journalArticle

Clifton, D. R. ; Fields, K. A. ; Grieshaber, S. S. ; Dooley, C. A. ; Fischer, E. R. ; Mead, D. J. ; Carabeo, R. A. ; Hackstadt, T. / A chlamydial type III translocated protein is tyrosine-phosphorylated at the site of entry and associated with recruitment of actin. In: Proceedings of the National Academy of Sciences of the United States of America. 2004 ; Vol. 101, No. 27. pp. 10166-10171.
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