Rac interacts with Abi-1 and WAVE2 to promote an Arp2/3-dependent actin recruitment during chlamydial invasion

Rey A Carabeo, Cheryl A Dooley, Scott S Grieshaber, Ted Hackstadt

Research output: Contribution to journalArticlepeer-review

54 Citations (Scopus)


Chlamydiae are Gram-negative obligate intracellular pathogens to which access to an intracellular environment is fundamental to their development. Chlamydial attachment to host cells induces the activation of the Rac GTPase, which is required for the localization of WAVE2 at the sites of chlamydial entry. Co-immunoprecipitation experiments demonstrated that Chlamydia trachomatis infection promoted the interaction of Rac with WAVE2 and Abi-1, but not with IRSp53. siRNA depletion of WAVE2 and Abi-1 abrogated chlamydia-induced actin recruitment and significantly reduced the uptake of the pathogen by the depleted cells. Chlamydia invasion also requires the Arp2/3 complex as demonstrated by its localization to the sites of chlamydial attachment and the reduced efficiency of chlamydial invasion in cells overexpressing the VCA domain of the neural Wiskott-Aldrich syndrome protein. Thus, C. trachomatis activates Rac and promotes its interaction with WAVE2 and Abi-1 to activate the Arp2/3 complex resulting in the induction of actin cytoskeletal rearrangements that are required for invasion.
Original languageEnglish
Pages (from-to)2278-2288
Number of pages11
JournalCellular Microbiology
Issue number9
Early online date22 Apr 2007
Publication statusPublished - Sept 2007


  • Animals
  • COS Cells
  • Enzyme Activation
  • HeLa Cells
  • Wiskott-Aldrich Syndrome Protein Family
  • Humans
  • Chlamydia trachomatis
  • Recombinant Fusion Proteins
  • RNA, Small Interfering
  • Actin-Related Protein 2-3 Complex
  • Adaptor Proteins, Signal Transducing
  • Cercopithecus aethiops
  • Chlamydia Infections
  • Actins
  • Cytoskeletal Proteins
  • rac GTP-Binding Proteins


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