The RickA protein of Rickettsia conorii activates the Arp2/3 complex

Edith Gouin, Coumaran Egile, Pierre Dehoux, Véronique Villiers, Josephine Adams, Frank Gertler, Rong Li and Pascale Cossart ()
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Edith Gouin: Unité des Interactions Bactéries-Cellules, Institut Pasteur
Coumaran Egile: Harvard Medical School
Pierre Dehoux: Unité des Interactions Bactéries-Cellules, Institut Pasteur
Véronique Villiers: Unité des Interactions Bactéries-Cellules, Institut Pasteur
Josephine Adams: Cleveland Clinic Foundation
Frank Gertler: Massachusetts Institute of Technology
Rong Li: Harvard Medical School
Pascale Cossart: Unité des Interactions Bactéries-Cellules, Institut Pasteur

Nature, 2004, vol. 427, issue 6973, 457-461

Abstract: Abstract Actin polymerization, the main driving force for cell locomotion, is also used by the bacteria Listeria and Shigella and vaccinia virus for intracellular and intercellular movements1,2. Seminal studies have shown the key function of the Arp2/3 complex in nucleating actin and generating a branched array of actin filaments during membrane extension and pathogen movement3. Arp2/3 requires activation by proteins such as the WASP-family proteins or ActA of Listeria. We previously reported that actin tails of Rickettsia conorii, another intracellular bacterium, unlike those of Listeria, Shigella or vaccinia, are made of long unbranched actin filaments apparently devoid of Arp2/3 (ref. 4). Here we identify a R. conorii surface protein, RickA, that activates Arp2/3 in vitro, although less efficiently than ActA. In infected cells, Arp2/3 is detected on the rickettsial surface but not in actin tails. When expressed in mammalian cells and targeted to the membrane, RickA induces filopodia. Thus RickA-induced actin polymerization, by generating long actin filaments reminiscent of those present in filopodia, has potential as a tool for studying filopodia formation.

Date: 2004
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DOI: 10.1038/nature02318

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