The Plasmodium knowlesi MAHRP2 ortholog localizes to structures connecting Sinton Mulligan's clefts in the infected erythrocyte

Parasitol Int. 2018 Aug;67(4):481-492. doi: 10.1016/j.parint.2018.04.005. Epub 2018 Apr 17.

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.

MeSH terms

  • Erythrocytes / chemistry
  • Erythrocytes / parasitology*
  • Host-Parasite Interactions
  • Membrane Proteins / analysis
  • Plasmodium falciparum / chemistry
  • Plasmodium falciparum / metabolism
  • Plasmodium knowlesi / chemistry
  • Plasmodium knowlesi / genetics
  • Plasmodium knowlesi / metabolism*
  • Protein Transport
  • Protozoan Proteins / chemistry*
  • Protozoan Proteins / genetics*
  • Protozoan Proteins / metabolism

Substances

  • Membrane Proteins
  • Protozoan Proteins