Chlamydia trachomatis induces remodeling of the actin cytoskeleton during attachment and entry into HeLa cells

Reynaldo A Carabeo, Scott S Grieshaber, Elizabeth Fischer, Ted Hackstadt

Research output: Contribution to journalArticle

120 Citations (Scopus)

Abstract

To elucidate the host cell machinery utilized by Chlamydia trachomatis to invade epithelial cells, we examined the role of the actin cytoskeleton in the internalization of chlamydial elementary bodies (EBs). Treatment of HeLa cells with cytochalasin D markedly inhibited the internalization of C. trachomatis serovar L2 and D EBs. Association of EBs with HeLa cells induced localized actin polymerization at the site of attachment, as visualized by either phalloidin staining of fixed cells or the active recruitment of GFP-actin in viable infected cells. The recruitment of actin to the specific site of attachment was accompanied by dramatic changes in the morphology of cell surface microvilli. Ultrastructural studies revealed a transient microvillar hypertrophy that was dependent upon C. trachomatis attachment, mediated by structural components on the EBs, and cytochalasin D sensitive. In addition, a mutant CHO cell line that does not support entry of C. trachomatis serovar L2 did not display such microvillar hypertrophy following exposure to L2 EBs, which is in contrast to infection with serovar D, to which it is susceptible. We propose that C. trachomatis entry is facilitated by an active actin remodeling process that is induced by the attachment of this pathogen, resulting in distinct microvillar reorganization throughout the cell surface and the formation of a pedestal-like structure at the immediate site of attachment and entry.
Original languageEnglish
Pages (from-to)3793-803
Number of pages11
JournalInfection and Immunity
Volume70
Issue number7
Publication statusPublished - Jul 2002

Fingerprint

Chlamydia trachomatis
Actin Cytoskeleton
HeLa Cells
Actins
Cytochalasin D
Hypertrophy
Phalloidine
CHO Cells
Microvilli
Polymerization
Epithelial Cells
Staining and Labeling
Cell Line
Infection
Serogroup

Keywords

  • Animals
  • HeLa Cells
  • Green Fluorescent Proteins
  • Humans
  • Chlamydia trachomatis
  • Recombinant Fusion Proteins
  • Cytochalasin D
  • Phosphatidylinositol 3-Kinases
  • Cytoskeleton
  • Luminescent Proteins
  • Actins
  • CHO Cells
  • Microvilli
  • Cricetinae

Cite this

Carabeo, R. A., Grieshaber, S. S., Fischer, E., & Hackstadt, T. (2002). Chlamydia trachomatis induces remodeling of the actin cytoskeleton during attachment and entry into HeLa cells. Infection and Immunity, 70(7), 3793-803.

Chlamydia trachomatis induces remodeling of the actin cytoskeleton during attachment and entry into HeLa cells. / Carabeo, Reynaldo A; Grieshaber, Scott S; Fischer, Elizabeth; Hackstadt, Ted.

In: Infection and Immunity, Vol. 70, No. 7, 07.2002, p. 3793-803.

Research output: Contribution to journalArticle

Carabeo, RA, Grieshaber, SS, Fischer, E & Hackstadt, T 2002, 'Chlamydia trachomatis induces remodeling of the actin cytoskeleton during attachment and entry into HeLa cells', Infection and Immunity, vol. 70, no. 7, pp. 3793-803.
Carabeo, Reynaldo A ; Grieshaber, Scott S ; Fischer, Elizabeth ; Hackstadt, Ted. / Chlamydia trachomatis induces remodeling of the actin cytoskeleton during attachment and entry into HeLa cells. In: Infection and Immunity. 2002 ; Vol. 70, No. 7. pp. 3793-803.
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N2 - To elucidate the host cell machinery utilized by Chlamydia trachomatis to invade epithelial cells, we examined the role of the actin cytoskeleton in the internalization of chlamydial elementary bodies (EBs). Treatment of HeLa cells with cytochalasin D markedly inhibited the internalization of C. trachomatis serovar L2 and D EBs. Association of EBs with HeLa cells induced localized actin polymerization at the site of attachment, as visualized by either phalloidin staining of fixed cells or the active recruitment of GFP-actin in viable infected cells. The recruitment of actin to the specific site of attachment was accompanied by dramatic changes in the morphology of cell surface microvilli. Ultrastructural studies revealed a transient microvillar hypertrophy that was dependent upon C. trachomatis attachment, mediated by structural components on the EBs, and cytochalasin D sensitive. In addition, a mutant CHO cell line that does not support entry of C. trachomatis serovar L2 did not display such microvillar hypertrophy following exposure to L2 EBs, which is in contrast to infection with serovar D, to which it is susceptible. We propose that C. trachomatis entry is facilitated by an active actin remodeling process that is induced by the attachment of this pathogen, resulting in distinct microvillar reorganization throughout the cell surface and the formation of a pedestal-like structure at the immediate site of attachment and entry.

AB - To elucidate the host cell machinery utilized by Chlamydia trachomatis to invade epithelial cells, we examined the role of the actin cytoskeleton in the internalization of chlamydial elementary bodies (EBs). Treatment of HeLa cells with cytochalasin D markedly inhibited the internalization of C. trachomatis serovar L2 and D EBs. Association of EBs with HeLa cells induced localized actin polymerization at the site of attachment, as visualized by either phalloidin staining of fixed cells or the active recruitment of GFP-actin in viable infected cells. The recruitment of actin to the specific site of attachment was accompanied by dramatic changes in the morphology of cell surface microvilli. Ultrastructural studies revealed a transient microvillar hypertrophy that was dependent upon C. trachomatis attachment, mediated by structural components on the EBs, and cytochalasin D sensitive. In addition, a mutant CHO cell line that does not support entry of C. trachomatis serovar L2 did not display such microvillar hypertrophy following exposure to L2 EBs, which is in contrast to infection with serovar D, to which it is susceptible. We propose that C. trachomatis entry is facilitated by an active actin remodeling process that is induced by the attachment of this pathogen, resulting in distinct microvillar reorganization throughout the cell surface and the formation of a pedestal-like structure at the immediate site of attachment and entry.

KW - Animals

KW - HeLa Cells

KW - Green Fluorescent Proteins

KW - Humans

KW - Chlamydia trachomatis

KW - Recombinant Fusion Proteins

KW - Cytochalasin D

KW - Phosphatidylinositol 3-Kinases

KW - Cytoskeleton

KW - Luminescent Proteins

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KW - CHO Cells

KW - Microvilli

KW - Cricetinae

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