Epidermal growth factor-like motifs 1 and 2 of Plasmodium vivax merozoite surface protein 1 are critical domains in erythrocyte invasion.
Plasmodium vivax merozoite surface protein 1 (PvMSP1) is believed to be important in erythrocyte invasion. However, the detailed mechanism of PvMSP1-mediated invasion has been unclear. We demonstrate that the C-terminal 19 kDa domain (PvMSP119) of PvMSP1, the 42-kDa fragment of PvMSP1 is further cleaved to a 33 kDa N-terminal polypeptide and a 19 kDa C-terminal fragment in a secondary processing step, is a critical domain in the binding between parasite ligand and erythrocyte receptor. Also, its cytoadherence was successfully blocked by naturally acquired immunity, was partially sensitive to neuraminidase and trypsin. When expressed separately epidermal growth factor (EGF)-like motifs 1 and 2, subunits of the PvMSP119, mediated 64% and 66% of the erythrocyte-binding activity, respectively, relative to their expression together as a single intact ligand domain. These results suggest that the EGF-like motifs 1 and 2 of PvMSP119 function as a core-binding portion in the attachment of PvMSP1 to erythrocytes.
Han
Hye-Jin
HJ
Department of Microbiology, Inje University College of Medicine, Busan 614-735, South Korea.
Park
Sae-Gwang
SG
Kim
So-Hee
SH
Hwang
Seung-Young
SY
Han
Jin
J
Traicoff
June
J
Kho
Weon-Gyu
WG
Chung
Joon-Yong
JY
D000818:Animals; D001483:Base Sequence; D019556:COS Cells; D017931:DNA Primers; D004815:Epidermal Growth Factor / Q000502:physiology*; D004912:Erythrocytes / Q000469:parasitology*; D020066:Merozoite Surface Protein 1 / Q000737:chemistry / Q000378:metabolism*; D010966:Plasmodium vivax / Q000378:metabolism*
D017931:DNA Primers; D020066:Merozoite Surface Protein 1; D004815:Epidermal Growth Factor