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Gene Review

PFC0595c  -  serine/threonine protein phosphatase,...

Plasmodium falciparum 3D7

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Disease relevance of MAL3P5.5

  • Immunogenicity of the Plasmodium falciparum serine repeat antigen (p126) expressed by vaccinia virus [1].
  • The crystal structure reveals a tetramer with a sulphate ion bound in the cofactor-binding site such that the side chains of the catalytic triad of serine, tyrosine and lysine are aligned in an active conformation, as previously observed in the Escherichia coli OAR-NADP+ complex [2].

High impact information on MAL3P5.5

  • The P.falciparum transit peptide is exceptional compared with other known plastid transit peptides in not requiring serine or threonine residues [3].
  • In addition to its synthesis from choline, phosphatidylcholine is synthesized from serine via an unknown pathway [4].
  • Serine, which is actively transported by Plasmodium from human serum and readily available in the parasite, is subsequently converted into phosphoethanolamine [4].
  • The process of human erythrocyte invasion by Plasmodium falciparum parasites involves a calcium-dependent serine protease with properties consistent with a subtilisin-like activity [5].
  • Instead of the known serine-to-asparagine change at position 108 that is important in pyrimethamine resistance, a serine-to-threonine change at the same position is found in cycloguanil-resistant isolates along with an alanine-to-valine change at position 16 [6].

Chemical compound and disease context of MAL3P5.5

  • Based on investigations on several blood stage antigens from Plasmodium falciparum we have expressed a hybrid protein in E. coli containing 262 amino acids of the serine-stretch protein SERP and 189 amino acids of the histidine alanine rich protein HRPII [7].

Biological context of MAL3P5.5


Anatomical context of MAL3P5.5

  • A subset of serine protease inhibitors blocks the processing and shedding of both AMA-1 and TRAP and inhibits sporozoite infectivity, suggesting that interfering with sporozoite proteolytic processing may constitute a valuable strategy to prevent hepatocyte infection [13].
  • As SERA-5 and some other serine-repeat antigens localise to the parasitophorous vacuole in mature parasites, they may play a role in erythrocyte rupture [14].
  • In the present work, we intend to determine the capacity of human lymphocytes to recognize subfragments of the serine-stretch protein SERP, a blood-stage antigen from Plasmodium falciparum [15].
  • We have previously identified a Plasmodium falciparum protein belonging to the superfamily of subtilisin-like serine proteases, which is expressed in a subset of secretory organelles in free merozoites [16].
  • Inhibition studies using synthetic peptides derived from the presumed band 3 enzymatic cleavage sites and the observed uptake of fluorescent phospholipids following gp76 treatment, suggest that band 3 degradation by this serine protease participates in the formation of the parasitophorous vacuole by restructuring the red cell cytoskeleton [17].

Associations of MAL3P5.5 with chemical compounds

  • The unusual concentration of 27 serines in the COOH-terminal portion of the protein shares homology with a similar polyserine repeat of the serine repeat antigen (SERA protein) of Plasmodium falciparum [9].
  • The synthesis of this phospholipid occurs via two routes, the CDP-choline pathway, which uses host choline as a precursor, and the plant-like serine decarboxylase-phosphoethanolamine methyltransferase (SDPM) pathway, which uses host serine as a precursor [18].
  • An apparent plateau was then reached for all metabolites except intracellular serine and Etn [19].
  • No concomitant inhibition of PtdSer or PtdCho labelling from serine occurred, even when PtdEtn formation was decreased by 95% [19].
  • In addition, the 120-kDa serine repeat antigen known as SERA, which was determined to be present on the merozoite, bound to phosphatidylserine vesicles and much less to vesicles of other phospholipids [20].

Physical interactions of MAL3P5.5

  • Secondary processing of the Plasmodium falciparum merozoite surface protein-1 (MSP1) by a calcium-dependent membrane-bound serine protease: shedding of MSP133 as a noncovalently associated complex with other fragments of the MSP1 [21].

Other interactions of MAL3P5.5

  • Remarkably, this cleavage is mediated by the same membrane-bound parasite serine protease as that responsible for shedding of the merozoite surface protein-1 (MSP-1) complex, an abundant, glycosylphosphatidylinositol-anchored multiprotein complex [10].

Analytical, diagnostic and therapeutic context of MAL3P5.5


  1. Immunogenicity of the Plasmodium falciparum serine repeat antigen (p126) expressed by vaccinia virus. Tine, J.A., Conseil, V., Delplace, P., De Taisne, C., Camus, D., Paoletti, E. Infect. Immun. (1993) [Pubmed]
  2. Kinetic, inhibition and structural studies on 3-oxoacyl-ACP reductase from Plasmodium falciparum, a key enzyme in fatty acid biosynthesis. Wickramasinghe, S.R., Inglis, K.A., Urch, J.E., Müller, S., van Aalten, D.M., Fairlamb, A.H. Biochem. J. (2006) [Pubmed]
  3. Protein trafficking to the plastid of Plasmodium falciparum is via the secretory pathway. Waller, R.F., Reed, M.B., Cowman, A.F., McFadden, G.I. EMBO J. (2000) [Pubmed]
  4. A pathway for phosphatidylcholine biosynthesis in Plasmodium falciparum involving phosphoethanolamine methylation. Pessi, G., Kociubinski, G., Mamoun, C.B. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  5. Plasmodium falciparum subtilisin-like protease 2, a merozoite candidate for the merozoite surface protein 1-42 maturase. Barale, J.C., Blisnick, T., Fujioka, H., Alzari, P.M., Aikawa, M., Braun-Breton, C., Langsley, G. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  6. Amino acids in the dihydrofolate reductase-thymidylate synthase gene of Plasmodium falciparum involved in cycloguanil resistance differ from those involved in pyrimethamine resistance. Foote, S.J., Galatis, D., Cowman, A.F. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  7. A recombinant hybrid protein as antigen for an anti-blood stage malaria vaccine. Knapp, B., Hundt, E., Enders, B., Küpper, H.A. Behring Inst. Mitt. (1991) [Pubmed]
  8. Maturation and specificity of Plasmodium falciparum subtilisin-like protease-1, a malaria merozoite subtilisin-like serine protease. Sajid, M., Withers-Martinez, C., Blackman, M.J. J. Biol. Chem. (2000) [Pubmed]
  9. Isolation and deduced amino acid sequence of the gene encoding gp115, a yeast glycophospholipid-anchored protein containing a serine-rich region. Vai, M., Gatti, E., Lacanà, E., Popolo, L., Alberghina, L. J. Biol. Chem. (1991) [Pubmed]
  10. A single malaria merozoite serine protease mediates shedding of multiple surface proteins by juxtamembrane cleavage. Howell, S.A., Well, I., Fleck, S.L., Kettleborough, C., Collins, C.R., Blackman, M.J. J. Biol. Chem. (2003) [Pubmed]
  11. A Conserved Subtilisin Protease Identified in Babesia divergens Merozoites. Montero, E., Gonzalez, L.M., Rodriguez, M., Oksov, Y., Blackman, M.J., Lobo, C.A. J. Biol. Chem. (2006) [Pubmed]
  12. In vivo evidence for the specificity of Plasmodium falciparum phosphoethanolamine methyltransferase and its coupling to the Kennedy pathway. Pessi, G., Choi, J.Y., Reynolds, J.M., Voelker, D.R., Mamoun, C.B. J. Biol. Chem. (2005) [Pubmed]
  13. A role for apical membrane antigen 1 during invasion of hepatocytes by Plasmodium falciparum sporozoites. Silvie, O., Franetich, J.F., Charrin, S., Mueller, M.S., Siau, A., Bodescot, M., Rubinstein, E., Hannoun, L., Charoenvit, Y., Kocken, C.H., Thomas, A.W., Van Gemert, G.J., Sauerwein, R.W., Blackman, M.J., Anders, R.F., Pluschke, G., Mazier, D. J. Biol. Chem. (2004) [Pubmed]
  14. Cysteine proteases of malaria parasites. Rosenthal, P.J. Int. J. Parasitol. (2004) [Pubmed]
  15. Responses of T cells from sensitized donors to recombinant and synthetic peptides corresponding to sequences of the Plasmodium falciparum SERP antigen. Roussilhon, C., Hundt, E., Agrapart, M., Stüber, W., Knapp, B., Dubois, P., Ballet, J.J. Immunol. Lett. (1990) [Pubmed]
  16. PfSUB-2: a second subtilisin-like protein in Plasmodium falciparum merozoites. Hackett, F., Sajid, M., Withers-Martinez, C., Grainger, M., Blackman, M.J. Mol. Biochem. Parasitol. (1999) [Pubmed]
  17. A role for erythrocyte band 3 degradation by the parasite gp76 serine protease in the formation of the parasitophorous vacuole during invasion of erythrocytes by Plasmodium falciparum. Roggwiller, E., Bétoulle, M.E., Blisnick, T., Braun Breton, C. Mol. Biochem. Parasitol. (1996) [Pubmed]
  18. Localization of the phosphoethanolamine methyltransferase of the human malaria parasite Plasmodium falciparum to the Golgi apparatus. Witola, W.H., Pessi, G., El Bissati, K., Reynolds, J.M., Mamoun, C.B. J. Biol. Chem. (2006) [Pubmed]
  19. Phospholipid metabolism of serine in Plasmodium-infected erythrocytes involves phosphatidylserine and direct serine decarboxylation. Elabbadi, N., Ancelin, M.L., Vial, H.J. Biochem. J. (1997) [Pubmed]
  20. Preferential binding of Plasmodium falciparum SERA and rhoptry proteins to erythrocyte membrane inner leaflet phospholipids. Perkins, M.E., Ziefer, A. Infect. Immun. (1994) [Pubmed]
  21. Secondary processing of the Plasmodium falciparum merozoite surface protein-1 (MSP1) by a calcium-dependent membrane-bound serine protease: shedding of MSP133 as a noncovalently associated complex with other fragments of the MSP1. Blackman, M.J., Holder, A.A. Mol. Biochem. Parasitol. (1992) [Pubmed]
  22. Immune responses induced by gene gun or intramuscular injection of DNA vaccines that express immunogenic regions of the serine repeat antigen from Plasmodium falciparum. Belperron, A.A., Feltquate, D., Fox, B.A., Horii, T., Bzik, D.J. Infect. Immun. (1999) [Pubmed]
  23. Molecular cloning, genomic structure and localization in a blood stage antigen of Plasmodium falciparum characterized by a serine stretch. Knapp, B., Hundt, E., Nau, U., Küpper, H.A. Mol. Biochem. Parasitol. (1989) [Pubmed]
  24. Molecular analysis of DHFR and DHPS genes in P. falciparum clinical isolates from the Haut--Ogooué region in Gabon. Mawili-Mboumba, D.P., Ekala, M.T., Lekoulou, F., Ntoumi, F. Acta Trop. (2001) [Pubmed]
  25. Different mutation patterns of atovaquone resistance to Plasmodium falciparum in vitro and in vivo: rapid detection of codon 268 polymorphisms in the cytochrome b as potential in vivo resistance marker. Schwöbel, B., Alifrangis, M., Salanti, A., Jelinek, T. Malar. J. (2003) [Pubmed]
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