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The Plasmodium knowlesi MAHRP2 ortholog localizes to structures connecting Sinton Mulligan's clefts in the infected erythrocyte |
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| Authors: | Kwame Kumi Asare Miako Sakaguchi Amuza Byaruhanga Lucky Masahito Asada Shinya Miyazaki Yuko Katakai Satoru Kawai Chihong Song Kazuyoshi Murata Kazuhide Yahata Osamu Kaneko |
| Institution: | 1. Program for Nurturing Global Leaders in Tropical and Emerging Infectious Diseases, Graduate School of Biomedical Sciences, Nagasaki University, 1-12-4 Sakamoto, Nagasaki 852-8523, Japan;2. Department of Protozoology, Institute of Tropical Medicine (NEKKEN), Nagasaki University, 1-12-4 Sakamoto, Nagasaki 852-8523, Japan;3. Central Laboratory, Institute of Tropical Medicine (NEKKEN), Nagasaki University, 1-12-4 Sakamoto, Nagasaki 852-8523, Japan;4. The Corporation for Production and Research of Laboratory Primates, 1-1 Hachimandai, Tsukuba, Ibaraki 305-0843, Japan;5. Department of Tropical Medicine and Parasitology, Dokkyo Medical University, 880 Kitakobayashi, Mibu-machi, Tochigi 321-0293, Japan;6. National Institute for Physiological Sciences, 38 Nishigonaka Myodaiji, Okazaki, Aichi 444-8585, Japan |
| Abstract: | During development within the host erythrocyte malaria parasites generate nascent membranous structures which serve as a pathway for parasite protein transport to modify the host cell. The molecular basis of such membranous structures is not well understood, particularly for malaria parasites other than Plasmodium falciparum. To characterize the structural basis of protein trafficking in the Plasmodium knowlesi-infected erythrocyte, we identified a P. knowlesi ortholog of MAHRP2, a marker of the tether structure that connects membranous structures in the P. falciparum-infected erythrocyte. We show that PkMAHRP2 localizes on amorphous structures that connect Sinton Mulligan's clefts (SMC) to each other and to the erythrocyte membrane. Three dimensional reconstruction of the P. knowlesi-infected erythrocyte revealed that the SMC is a plate-like structure with swollen ends, reminiscent of the morphology of the Golgi apparatus. The PkMAHRP2-localized amorphous structures are possibly functionally equivalent to P. falciparum tether structure. These findings suggest a conservation in the ultrastructure of protein trafficking between P. falciparum and P. knowlesi. |
| Keywords: | Corresponding author at: Department of Protozoology Institute of Tropical Medicine (NEKKEN) Nagasaki University 1-12-4 Sakamoto Nagasaki 852-8523 Japan |
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