The Ionic and Hydrophobic Interactions Are Required for the Auto Activation of Cysteine Proteases of Plasmodium falciparum

PLoS ONE

Volumn 7, Issue 10, 2012, Pages

  Sundararaj, Srinivasan ^a   Singh, Deepak ^a   Saxena, Ajay K ^b   Vashisht, Kapil ^a   Sijwali, Puran S ^c   Dixit, Rajnikant ^a   Pandey, Kailash C ^a  

^a NATIONAL INSTITUTE OF MALARIA RESEARCH   (India)

^b JAWAHARLAL NEHRU UNIVERSITY   (India)

^c CENTRE FOR CELLULAR AND MOLECULAR BIOLOGY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CYSTEINE PROTEINASE; FALCIPAIN 2; FALCIPAIN 3; GLUTAMINE; LYSINE; PHENYLALANINE; TRYPTOPHAN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACTERIUM MUTANT; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ANALYSIS; ESCHERICHIA COLI; HYDROPHOBICITY; MOLECULAR CLONING; MOLECULAR INTERACTION; MUTAGENESIS; NONHUMAN; PLASMODIUM FALCIPARUM; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN REFOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SALT BRIDGE; TRANSACTIVATION; WILD TYPE;

AMINO ACID SEQUENCE; CYSTEINE ENDOPEPTIDASES; ENZYME ACTIVATION; HEMOGLOBINS; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MALARIA, FALCIPARUM; PLASMODIUM FALCIPARUM; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84867602273     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0047227     Document Type: Article

References (35)

1. WHO World Malaria Report (2008).
2. Fidock DA, (2010) Drug discovery; Priming the antimalarial pipeline. Nature 465: 297-298.
3. Wongsrichanalai C, Meshnick SR, (2008) Declining artesunate-mefloquine efficacy against falciparum malaria on the Cambodia-Thailand border. Emerg Infect Dis 14: 716-719.
4. Dondorp AM, Nosten F, Yi P, Das D, Phyo AP, et al. (2009) Artemisinin resistance in Plasmodium falciparum malaria. N Engl J Med 361: 455-67.
5. Rosenthal PJ, Sijwali PS, Singh A, Shenai BR, (2002) Cysteine proteases of malaria parasites: targets for chemotherapy. Curr Pharm Des 8: 1659-72.
6. Rosenthal PJ, (2004) Cysteine proteases of malaria parasites. Intl J Parasitology 34: 1489-1499.
7. Shenai BR, Sijwali PS, Singh A, Rosenthal PJ, (2000) Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum. J Biol Chem 37: 29000-29010.
8. Sijwali PS, Shenai BR, Gut J, Singh A, Rosenthal PJ, (2001) Expression and characterization of the Plasmodium falciparum haemoglobinase falcipain-3. Biochem J 360: 481-489.
9. Sijwali PS, Shenai BR, Rosenthal PJ, (2002) Folding of the Plasmodium falciparum cysteine protease falcipain-2 is mediated by a chaperone-like peptide and not the prodomain. J Biol Chem 277: 14910-14915.
10. Sijwali PS, Rosenthal PJ, (2004) Gene disruption confirms a critical role for the cysteine protease falcipain-2 in haemoglobin hydrolysis by Plasmodium falciparum. Proc Natl Acad Sci USA 13: 4384-4389.
11. Sijwali PS, Koo J, Singh N, Rosenthal PJ, (2006) Gene disruptions demonstrate independent roles for the four falcipain cysteine proteases of Plasmodium falciparum. Mol Biochem Parasitol 150: 96-106.
12. Pandey KC, Sijwali PS, Singh A, Na BK, Rosenthal PJ, (2004) Independent intramolecular mediators of folding, activity, and inhibition for the Plasmodium falciparum cysteine protease falcipain-2. J Biol Chem 5: 3484-3491.
13. Pandey KC, Wang SX, Sijwali PS, Lau AL, McKerrow JH, et al. (2005) The Plasmodium falciparum cysteine protease falcipain-2 captures its substrate, haemoglobin, via a unique motif. Proc Natl Acad Sci USA 102: 9138-9143.
14. Pandey KC, Dixit R, (2011) Structure-Function of Falcipains; Malarial Cysteine Proteases. Invited review in Journal of Tropical Medicine 10.1155/2012/345195.
15. Subramanian S, Sijwali PS, Rosenthal PJ, (2007) Falcipain cysteine proteases require bipartite motifs for trafficking to the Plasmodium falciparum food vacuole. J Biol Chem 282: 24961-24969.
16. Pandey KC, Barkan DT, Sali A, Rosenthal PJ, (2009) Regulatory elements within the prodomain of Falcipain-2, a cysteine protease of the malaria parasite Plasmodium falciparum. PLoS One 4e: 5694.
17. Subramanian S, Hardt M, Choe Y, Niles RK, Johansen EB, et al. (2009) Haemoglobin cleavage site-specificity of the Plasmodium falciparum cysteine proteases falcipain-2 and falcipain-3. PLoS One 4e: 5156.
18. Nishimura Y, Amano J, Sato H, Tsuji H, Kato K, (1988) Biosynthesis of lysosomal Cathepsins B and H in cultured rat hepatocytes. Arch Biochem & Biophys 262: 159-170.
19. Kominami E, Tsukahara T, Hara K, Katunuma N, (1988) Biosynthesis and processing of lysosomal cysteine proteases in rat macrophages. FEBS Lett 231: 225-228.
20. Rojman J, Stojan J, Kuhelji R, Turk V, Turk B, (1999) Autocatalytic Processing of human procathepsin B is a bimolecular process. FEBS Lett 459: 358-362.
21. Dahl EL, Rosenthal PJ, (2005) Biosynthesis, localization, and processing of falcipain cysteine proteases of Plasmodium falciparum. Mol Biochem Parasitol 139: 205-212.
22. Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR, (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77: 51-59.
23. Shen MY, Sali A, (2006) Statistical potential for assessment and prediction of protein structures. Protein Sci 15: 2507-2524.
24. Eramian D, Eswar N, Shen MY, Sali A, (2008) How well can the accuracy of comparative protein structure models be predicted? Protein Science 17: 1881-93.
25. Fiser A, Do RK, Sali A, (2000) Modeling of loops in protein structures. Protein Science 9: 1753-1773.
26. Wang SX, Pandey KC, Somoza JR, Sijwali PS, Kortemme T, et al. (2006) Structural basis for unique mechanisms of folding and haemoglobin binding by a malarial protease. Proc Natl Acad Sci USA 31: 11503-11518.
27. Pandey KC, Singh N, Arastu Kapur S, Bogyo M, Rosenthal PJ, (2006) Falstatin, a cysteine protease inhibitor of Plasmodium falciparum, facilitates erythrocyte invasion. PLoS Pathogen 11: e117.
28. Cygler M, Sivaraman J, Grochulski P, Coulombe R, Storer AC, et al. (1996) Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion. Structure 4: 405-416.
29. Turk D, Podobnik M, Kuhelj R, Dolinar M, Turk V, (1996) Crystal structures of human procathepsin B at 3.2 and 3.3 angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide. FEBS Lett 384: 211-214.
30. Groves MR, Coulombe R, Jenkins J, Cygler M, (1998) Structural basis for specificity of papain -like cysteine protease proregions toward their congate enzymes. Proteins 32: 504-514.
31. Laurent-Matha V, Derocq D, Prebois C, Katunuma N, Liaudet-Coopman E, (2006) Processing of human cathepsin D is independent of its catalytic function and auto-activation: involvement of cathepsins L and B. J Biochem 139: 363-371.
32. Podobnik M, Kuhelj R, Turk V, Turk D, (1997) Crystal structure of the wild-type human procathepsin B at 2.5 A resolution reveals the native active site of a papain-like cysteine protease zymogen. J Mol Biol 271: 774-788.
33. Jerala R, Zerovnik E, Kidric J, Turk V, (1998) pH-induced conformational transitions of the propeptide of human cathepsin L. A role for a molten globule state in zymogen activation. J Biol Chem 273: 11498-11504.
34. Ménard R, Carmona E, Takebe S, Dufour E, Plouffe C, et al. (1998) Autocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro. J Biol Chem 273: 4478-4484.
35. Fox T, de Miguel E, Mort JS, Storer AC, (1992) Potent slow-binding inhibition of cathepsin B by its propeptide. Biochemistry 31: 12571-12576.