TY - JOUR
T1 - Actin polymerization mediated by Babesia gibsoni aldolase is required for parasite invasion
AU - Goo, Youn Kyoung
AU - Ueno, Akio
AU - Terkawi, Mohamad Alaa
AU - Oluga Aboge, G.
AU - Junya, Yamagishi
AU - Igarashi, Makoto
AU - Kim, Jung Yeon
AU - Hong, Yeon Chul
AU - Chung, Dong Il
AU - Nishikawa, Yoshifumi
AU - Xuan, Xuenan
PY - 2013/9
Y1 - 2013/9
N2 - 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.
AB - 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.
KW - Aldolase
KW - Babesia gibsoni
KW - Erythrocyte invasion
UR - http://www.scopus.com/inward/record.url?scp=84880313015&partnerID=8YFLogxK
U2 - 10.1016/j.exppara.2013.06.002
DO - 10.1016/j.exppara.2013.06.002
M3 - Article
C2 - 23792005
AN - SCOPUS:84880313015
SN - 0014-4894
VL - 135
SP - 42
EP - 49
JO - Experimental Parasitology
JF - Experimental Parasitology
IS - 1
ER -