Computational Studies on Calpain from Plasmodium falciparum

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Computational Studies on Calpain from Plasmodium falciparum

T.K. Bhatt

Author Affiliations

¹ Department of Biotechnology, Central University of Rajasthan, Kishangarh, INDIA

Res. J. Recent Sci., Volume 1, Issue (9), Pages 79-82, September,2 (2012)

Abstract

Malaria is one of the most devastating diseases prevalent in the world. It is caused by the parasite Plasmodium falciparum. Many species of Plasmodium are shown to infect human host. The increased resistant in malaria parasite against drugs remain the major concern. Hence identification of new and effective drug targets against Plasmodium is a regular process. In the same line, proteases are the major group of the proteins in the parasite which plays crucial role in various processes like migration, evasion and cell cycle etc. Therefore, in this study, we have performed structural studies on cysteine proteases called ‘calpain’ from malaria parasite (Pfcalpain). In addition, phylogenetic analysis was also performed on Pfcalpain. We believe that these results will help in understanding various biological processes of parasite and will be instrumental in discovering effective chemotherapy against malaria.

References

Wu Y., Wang X., Liu X. and Wang Y., Data-mining approaches reveal hidden families of proteases in the genome of malaria parasite, Genome Res., 13, 601–616 (2003)
Shenai B.R., Sijwali P.S., Singh A. and Rosenthal P.J., Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum, J Biol Chem., 275, 29000–29010 (2000)
Rosenthal P.J., Cysteine proteases of malaria parasites, Int J Parasitol., 34, 1489–1499 (2004)
Klemba M., Gluzman I. and Goldberg D.E., A Plasmodium falciparum dipeptidyl minopeptidase 1 participates in vacuolar hemoglobin degradation, J Biol Chem., 279, 43000–43007 (2004)
Sijwali P.S. and Rosenthal P.J., Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparum, Proc Natl Acad Sci U S A., 101, 4384–4389 (2004)
Hadley T., Aikawa M. and Miller L.H., Plasmodium knowlesi: Studies on invasion of rhesus erythrocytes by merozoites in the presence of protease inhibitors, Exp Parasitol., 55, 306–311 (1983)
Croall D.E. and Ersfeld K., The calpains: Modular designs and functional diversity, Genome Biol., , 218 (2007)
Ilario R. et al., A calpain unique to alveolates is essential in Plasmodium falciparum and its knockdown reveals an involvement in pre-S-phase development, Proc Natl Acad Sci U S A., 106, 1554–1559 (2004)
Lovell S.C., Davis I.W., Arendall W.B. , de Bakker P.I., Word J.M., Prisant M.G., Richardson J.S. and Richardson D.C., Structure validation by Calpha geometry: phi,psi and Cbeta deviation, Proteins., 15;50(3), 437-50 (2000)
Dundas J., et. Al., CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues, Nucleic Acids Res., 34, 116–118 (2006)
Bhatt T.K., In-Silico Structure Determination of Protein Falstatin from Malaria Parasite Plasmodium Falciparum, Res. J. Recent Sci.,1(4), 68-71 (2012)
Pettersen E.F., Goddard T.D., Huang C.C., Couch G.S., Greenblatt D.M., Meng E.C. and Ferrin TE, UCSF Chimera - A Visualization System for Exploratory Research and Analysis, J Comput Chem., 25,1605-1612, (2004)

[ref1] Wu Y., Wang X., Liu X. and Wang Y., Data-mining approaches reveal hidden families of proteases in the genome of malaria parasite, Genome Res., 13, 601–616 (2003)

[ref2] Shenai B.R., Sijwali P.S., Singh A. and Rosenthal P.J., Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum, J Biol Chem., 275, 29000–29010 (2000)

[ref3] Rosenthal P.J., Cysteine proteases of malaria parasites, Int J Parasitol., 34, 1489–1499 (2004)

[ref4] Klemba M., Gluzman I. and Goldberg D.E., A Plasmodium falciparum dipeptidyl minopeptidase 1 participates in vacuolar hemoglobin degradation, J Biol Chem., 279, 43000–43007 (2004)

[ref5] Sijwali P.S. and Rosenthal P.J., Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparum, Proc Natl Acad Sci U S A., 101, 4384–4389 (2004)

[ref6] Hadley T., Aikawa M. and Miller L.H., Plasmodium knowlesi: Studies on invasion of rhesus erythrocytes by merozoites in the presence of protease inhibitors, Exp Parasitol., 55, 306–311 (1983)

[ref7] Croall D.E. and Ersfeld K., The calpains: Modular designs and functional diversity, Genome Biol., , 218 (2007)

[ref8] Ilario R. et al., A calpain unique to alveolates is essential in Plasmodium falciparum and its knockdown reveals an involvement in pre-S-phase development, Proc Natl Acad Sci U S A., 106, 1554–1559 (2004)

[ref9] Lovell S.C., Davis I.W., Arendall W.B. , de Bakker P.I., Word J.M., Prisant M.G., Richardson J.S. and Richardson D.C., Structure validation by Calpha geometry: phi,psi and Cbeta deviation, Proteins., 15;50(3), 437-50 (2000)

[ref10] Dundas J., et. Al., CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues, Nucleic Acids Res., 34, 116–118 (2006)

[ref11] Bhatt T.K., In-Silico Structure Determination of Protein Falstatin from Malaria Parasite Plasmodium Falciparum, Res. J. Recent Sci.,1(4), 68-71 (2012)

[ref12] Pettersen E.F., Goddard T.D., Huang C.C., Couch G.S., Greenblatt D.M., Meng E.C. and Ferrin TE, UCSF Chimera - A Visualization System for Exploratory Research and Analysis, J Comput Chem., 25,1605-1612, (2004)