Adhesion protein complexes of malaria gametocytes assemble following parasite transmission to the mosquito

被引:27
|
作者
Simon, Nina [1 ,2 ]
Kuehn, Andrea [1 ,3 ]
Williamson, Kim C. [4 ]
Pradel, Gabriele [5 ]
机构
[1] Univ Wurzburg, Res Ctr Infect Dis, D-97080 Wurzburg, Germany
[2] Univ Erlangen Nurnberg, Inst Med Biotechnol, D-91052 Erlangen, Germany
[3] Univ Barcelona, Hosp Clin, Barcelona Ctr Int Hlth Res CRESIB, ISGlobal, Barcelona, Spain
[4] Loyola Univ, Dept Biol, Chicago, IL 60626 USA
[5] Rhein Westfal TH Aachen, Div Cellular & Appl Infect Biol, D-52074 Aachen, Germany
关键词
Multi-protein complex; Plasmodium falciparum; PfCCp protein; Pfs230; Gametogenesis; Transmission; PLASMODIUM-FALCIPARUM; EXPRESSION; MEMBRANE; SURFACE; PFS230; COMPARTMENT; ANTIGENS;
D O I
10.1016/j.parint.2015.09.007
中图分类号
R38 [医学寄生虫学]; Q [生物科学];
学科分类号
07 ; 0710 ; 09 ; 100103 ;
摘要
During differentiation in the human, the gametocytes of the malaria parasite Plasmodium falciparum display a remarkable number of adhesive proteins on their plasma membrane. These include the PfCCp protein family of six secreted proteins that assemble to multimeric protein complexes (MPCs) within the gametocyte parasitophorous vacuole. We now show that the PfCCp-based MPCs are linked to the gametocyte plasma membrane via interactions with Pfs230, a binding-partner of the GPI-anchored Pfs48/45. Upon onset of gametogenesis, which takes place after gametocyte uptake by blood-feeding mosquitoes, GPI-anchored Pfs25 joins the MPC, providing an additional link of its components to the plasma membrane. Gametogenesis also initiates cleavage of Pfs230 at its N-terminal site, resulting in its increased interaction with the MPC. Either lack of Pfs230 or impaired Pfs230 processing causes proteolysis of the PfCCp proteins and release from the MPC Our data point to MPC assembly as a crucial step for sexual reproduction. (C) 2015 Elsevier Ireland Ltd. All rights reserved.
引用
收藏
页码:27 / 30
页数:4
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