title: Actin polymerization mediated by Babesia gibsoni aldolase is required for parasite invasion.
abstract: Host cell invasion by apicomplexan parasites driven by gliding motility and empowered by actin-based movement is essential for parasite survival and pathogenicity. The parasites share a conserved invasion process: actin-based motility led by the coordination of adhesin-cytoskeleton via aldolase. A number of studies of host cell invasion in the Plasmodium species and Toxoplasma gondii have been performed. However, the mechanisms of host cell invasion by Babesia species have not yet been studied. Here, we show that Babesia gibsoni aldolase (BgALD) forms a complex with B. gibsoni thrombospondin-related anonymous protein (BgTRAP) and B. gibsoni actin (BgACT), depending on tryptophan-734 (W-734) in BgTRAP. In addition, actin polymerization is mediated by BgALD. Moreover, cytochalasin D, which disrupts actin polymerization, suppressed B. gibsoni parasite growth and inhibited the host cell invasion by parasites, indicating that actin dynamics are essential for erythrocyte invasion by B. gibsoni. This study is the first molecular approach to determine the invasion mechanisms of Babesia species.
authors.affiliation: National Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Hokkaido 080-8555, Japan.
authors.forename: Youn-Kyoung
authors.initials: YK
authors.lastname: Goo
authors.forename: Akio
authors.initials: A
authors.lastname: Ueno
authors.forename: Mohamad Alaa
authors.initials: MA
authors.lastname: Terkawi
authors.forename: G Oluga
authors.initials: GO
authors.lastname: Aboge
authors.forename: Yamagishi
authors.initials: Y
authors.lastname: Junya
authors.forename: Makoto
authors.initials: M
authors.lastname: Igarashi
authors.forename: Jung-Yeon
authors.initials: JY
authors.lastname: Kim
authors.forename: Yeon-Chul
authors.initials: YC
authors.lastname: Hong
authors.forename: Dong-Il
authors.initials: DI
authors.lastname: Chung
authors.forename: Yoshifumi
authors.initials: Y
authors.lastname: Nishikawa
authors.forename: Xuenan
authors.initials: X
authors.lastname: Xuan
mesh_terms: D000199:Actins / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D001403:Babesia / Q000187:drug effects / Q000201:enzymology* / Q000502:physiology*; D015638:Cytochalasin D / Q000494:pharmacology; D018076:DNA, Complementary / Q000302:isolation & purification; D016054:DNA, Protozoan / Q000302:isolation & purification; D004912:Erythrocytes / Q000469:parasitology*; D005260:Female; D005634:Fructose-Bisphosphate Aldolase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D051379:Mice; D008813:Mice, Inbred ICR; D019384:Nucleic Acid Synthesis Inhibitors / Q000494:pharmacology; D016366:Open Reading Frames / Q000235:genetics; D058105:Polymerization; D015800:Protozoan Proteins / Q000378:metabolism
chemical_list: D000199:Actins; D018076:DNA, Complementary; D016054:DNA, Protozoan; D019384:Nucleic Acid Synthesis Inhibitors; D015800:Protozoan Proteins; C069428:thrombospondin-related adhesive protein, protozoan; D015638:Cytochalasin D; D005634:Fructose-Bisphosphate Aldolase
keywords: Aldolase; Babesia gibsoni; Erythrocyte invasion