A Plasmodium falciparum novel gene encoding a coronin‐like protein which associates with actin filaments

FEBS Letters

Tardieux, Isabelle¹  Liu, Xuan²  Dehoux, Pierre³  Parzy, Daniel⁴  Langsley, Gordon⁵  Poupel, Olivier¹ 

[1] Laboratoire de Biochimie et Biologie Moléculaire des Insectes, Institut Pasteur, 28 rue du Dr Roux, 75724 Paris Cedex 15, France;Laboratory of Parasitic Diseases, NIAID, NIH, Bethesda, MD 20892, USA;Unité des Interactions Bactéries Cellules, Institut Pasteur, Paris, France;Institut de Médecine Tropicale du Service de Santé des Armées, Le Pharo, 13998 Marseille, France;Unité de Parasitologie Expérimentale, URA CNRS 1960, Département d'Immunologie, Institut Pasteur, Paris, France

关键词: Actin dynamic;    Coronin;    WD motif;    Apicomplexa;   

DOI  :  10.1016/S0014-5793(98)01557-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Plasmodium falciparum, the major causative agent of human malaria, is an Apicomplexa protozoan parasite which invades in its intermediate host hepatocytes and erythrocytes. The driving force underlying internalization into the host cell is thought to involve both polymerization of parasite actin, as entry is inhibited by the cytochalasins, and an actin motor-associated protein. In the related Apicomplexa parasite, Toxoplasma gondii, the involvement of parasite actin during both processes of motility and host cell entry has been genetically established. In a search for molecules that can regulate actin dynamics within Apicomplexa parasites, we have identified a P. falciparum homologue of the actin associated protein called coronin originally described in the amoeba Dictyostelium discoideum. The single copy gene displays a strong homology with the amoeba sequence and with the bovine and human coronin homologues recently cloned. This homology lies not only within the N-terminus containing the five WD repeats that characterize coronin but also extends in the C-terminal part. Furthermore, using an affinity-purified mouse monoclonal antibody against D. discoideum coronin, we have detected in extracts of P. falciparum young and mature schizonts a 42-kDa polypeptide which binds this antibody and is present in a Triton insoluble fraction that also contains parasite actin filaments. In addition, the recombinant protein encoded by the homologue nucleotidic sequence of P. falciparum coronin is indeed recognized by the antibody against D. discoideum coronin. Finally, the cross-reactive polypeptide displays the ability to cosediment with exogenous F-actin, a property which fits with its involvement in actin dynamics.

【 授权许可】

Unknown