TY - JOUR
T1 - Adhesion protein complexes of malaria gametocytes assemble following parasite transmission to the mosquito
AU - Simon, Nina
AU - Kuehn, Andrea
AU - Williamson, Kim C.
AU - Pradel, Gabriele
N1 - Publisher Copyright:
© 2015 Elsevier Ireland Ltd.
PY - 2016/2/1
Y1 - 2016/2/1
N2 - 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 interactionswith 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.
AB - 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 interactionswith 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.
KW - Gametogenesis
KW - Multi-protein complex
KW - PfCCp protein
KW - Pfs230
KW - Plasmodium falciparum
KW - Transmission
UR - http://www.scopus.com/inward/record.url?scp=84943763409&partnerID=8YFLogxK
U2 - 10.1016/j.parint.2015.09.007
DO - 10.1016/j.parint.2015.09.007
M3 - Article
C2 - 26408859
AN - SCOPUS:84943763409
SN - 1383-5769
VL - 65
SP - 27
EP - 30
JO - Parasitology International
JF - Parasitology International
IS - 1
ER -