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MESA  -  Mature parasite-infected erythrocyte...

Plasmodium falciparum 3D7

 
 
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High impact information on PFMESA

  • Colocalization studies of the protein pairs of mature parasite-infected erythrocyte surface antigen (MESA) (parasite)/protein4.1(host) and P. falciparum histidine rich protein (PfHRP1) (parasite)/protein4.1(host) showed good real-space correlation for the MESA/protein4.1 pair, but relatively poor correlation for the PfHRP1/protein4.1 pair [1].
  • One of these transported proteins, MESA (mature parasite-infected erythrocyte surface antigen), is anchored to the red cell membrane by noncovalent interaction with erythrocyte protein 4 [2].
  • Loss of parasite proteins ring-infected erythrocyte surface antigen (RESA), knob-associated histidine-rich protein (KAHRP) or Plasmodium falciparum erythrocyte membrane protein 3 (PfEMP3) had a significant effect on the ability of PRBCs to adhere, whereas loss of mature parasite-infected erythrocyte surface antigen (MESA) had no effect [3].
  • The mature-parasite-infected erythrocyte surface antigen (MESA, also known as PfEMP-2 and pp300) of Plasmodium falciparum is a phosphoprotein of approx. 250-300 kDa that is exported from the parasite to the erythrocyte membrane skeleton where it binds to protein 4 [4].
  • 1. Determination of the primary sequence of MESA reveals that it is encoded by 2 exons, a structure common to other exported proteins of P. falciparum [4].
 

Biological context of PFMESA

  • In contrast, parasites from the same clone that were cultured without this selection lost the knobbed and cytoadherent phenotypes, but continued to express MESA [5].
  • Intraerythrocytic Plasmodium falciparum parasites at the trophozoite and schizont stages synthesize a greater than 200-kDa protein, the mature erythrocyte surface antigen (MESA), that is localized at the membrane of infected red blood cells and manifests size polymorphism and antigenic diversity among parasite isolates [5].
  • Our results show that neither MESA nor protein 4.1 is required for phosphorylation of its binding partner [6].
  • Their chromosomal locations have been identified such as KAHRP on chromosome 2 and MESA/PFEMP-2 on chromosomes 5 and 6 [7].
 

Anatomical context of PFMESA

 

Other interactions of PFMESA

References

  1. Membrane specific mapping and colocalization of malarial and host skeletal proteins in the Plasmodium falciparum infected erythrocyte by dual-color near-field scanning optical microscopy. Enderle, T., Ha, T., Ogletree, D.F., Chemla, D.S., Magowan, C., Weiss, S. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  2. Defining the minimal domain of the Plasmodium falciparum protein MESA involved in the interaction with the red cell membrane skeletal protein 4.1. Bennett, B.J., Mohandas, N., Coppel, R.L. J. Biol. Chem. (1997) [Pubmed]
  3. Assignment of functional roles to parasite proteins in malaria-infected red blood cells by competitive flow-based adhesion assay. Cooke, B.M., Glenister, F.K., Mohandas, N., Coppel, R.L. Br. J. Haematol. (2002) [Pubmed]
  4. Repeat structures in a Plasmodium falciparum protein (MESA) that binds human erythrocyte protein 4.1. Coppel, R.L. Mol. Biochem. Parasitol. (1992) [Pubmed]
  5. The mature erythrocyte surface antigen of Plasmodium falciparum is not required for knobs or cytoadherence. Petersen, C., Nelson, R., Magowan, C., Wollish, W., Jensen, J., Leech, J. Mol. Biochem. Parasitol. (1989) [Pubmed]
  6. Plasmodium falciparum: influence of malarial and host erythrocyte skeletal protein interactions on phosphorylation in infected erythrocytes. Magowan, C., Liang, J., Yeung, J., Takakuwa, Y., Coppel, R.L., Mohandas, N. Exp. Parasitol. (1998) [Pubmed]
  7. Knobs, knob proteins and cytoadherence in falciparum malaria. Sharma, Y.D. Int. J. Biochem. (1991) [Pubmed]
  8. Transcription status of vaccine candidate genes of Plasmodium falciparum during the hepatic phase of its life cycle. Bodescot, M., Silvie, O., Siau, A., Refour, P., Pino, P., Franetich, J.F., Hannoun, L., Sauerwein, R., Mazier, D. Parasitol. Res. (2004) [Pubmed]
  9. The mature-parasite-infected erythrocyte surface antigen (MESA) of Plasmodium falciparum associates with the erythrocyte membrane skeletal protein, band 4.1. Lustigman, S., Anders, R.F., Brown, G.V., Coppel, R.L. Mol. Biochem. Parasitol. (1990) [Pubmed]
 
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