Molecular characterization of a novel cathepsin B from striped murrel channa striatus: Bioinformatics analysis, gene expression, synthesis of peptide and antimicrobial property

Turkish Journal of Fisheries and Aquatic Sciences

Volumn 14, Issue 2, 2014, Pages 379-389

  Arockiaraj, Jesu ^a   Kumaresan, Venkatesh ^a   Chaurasia, Mukesh Kumar ^a   Bhatt, Prasanth ^a   Palanisamy, Rajesh ^a   Pasupuleti, Mukesh ^b   Gnanam, Annie J ^c   Kasi, Marimuthu ^d  

^a SRM INSTITUTE OF SCIENCE AND TECHNOLOGY   (India)

^b CENTRAL DRUG RESEARCH INSTITUTE   (India)

^c UNIVERSITY OF TEXAS AT AUSTIN   (United States)

^d AIMST UNIVERSITY   (Malaysia)

Author keywords

Antimicrobial peptide; Bacteria; Cathepsin B; Fungus; Murrel

Indexed keywords

CHANNA MARULIUS MARULIUS; CHANNA STRIATA; FUNGI;

EID: 84907816992     PISSN: 13032712     EISSN: None     Source Type: Journal    
DOI: 10.4194/1303-2712-v14_2_08     Document Type: Article

References (58)

1. Abirami, A., Venkatesh, K., Akila, S., Rajesh, P., Nagaram, P., Prasanth, B., Arpita, R., Thirumalai, M.K., Gnanam, A.J., Mukesh, P., Kasi, M. and Arockiaraj, J. 2013. Fish lily type lectin-1 contains β-prism 2 architecture: Immunological characterization. Molecular Immunology, 56: 497-506. doi: 10.1016/j.molimm.2013.06.020.
2. Adeni, A., Huet, G., Zerimech, F., Hecquet, B., Balduyck, M. and Peyrata, J.P. 1995. Cathepsin B, L, and D activities in colorectal carcinomas: relationship with clinico-pathological parameters. Cancer Letters, 96: 267-275. doi: 10.1016/0304-3835(95)03930-U.
3. Aoki, H., Ahsan, M.N. and Watabe, S. 2003. Molecular cloning and characterization of cathepsin B from the hepatopancreas of northern shrimp Pandalus borealis. Comparitive Biochemistry Physiology, Part B, 134: 681-694. doi: 10.1016/S1096-4959(03)00023-X.
4. Aoki, T., Nakano, T. and Ueno, R. 1997. Purification and some properties of a latent form cathepsin L from mackerel whitemuscle. Fish Sciences, 63: 824-829.
5. Aoki, T. and Ueno, R. 1997. Involvement of cathepsins B and L in the post-mortem autolysis of mackerel muscle. Food Research International, 30: 585-591. doi: 10.1016/S0963-9969(98)00014-3.
6. Aranishi, F. 1999. Lysis of pathogenic bacteria by epidermal cathepsins L and B in the Japanese eel. Fish Physiology and Biochemistry, 20: 37-41. doi: 10.1023/A:1007763711158.
7. Arockiaraj, J., Annie, J.G., Dhanaraj, M., Ranganath, G., James, M., Arun, S., Saravanan, M., Kasi, M. and Subha, B. 2013. Crustin, a WAP domain containing antimicrobial peptide from freshwater prawn M. rosenbergii: Immune characterization. Fish and Shellfish Immunology, 34: 109-118. doi: 10.1016/j.fsi.2012.10.009.
8. Arockiaraj, J., Annie, J.G., Dhanaraj, M., Thirumalai, M.K., Mukesh, P., Milton, J. and Kasi, M. 2013c. Macrobrachium rosenbergii cathepsin L: Molecular characterization and gene expression in response to viral and bacterial infections. Microbiology Research, 168: 569-579. doi: 10.1016/j.micres.2013.04.007.
9. Arockiaraj, J., Puganeshwaran, V., Sarasvathi, E., Arun, S., Rofina, Y.O. and Subha, B. 2012. Molecular functions of chaperonin gene, containing tailless complex polypeptide 1 from Macrobrachium rosenbergii. Gene, 508: 241-249. doi: 10.1016/j.gene.2012.07.050.
10. Arockiaraj, J., Puganeshwaran, V., Sarasvathi, E., Arun, S., Tahereh, A., Rofina, Y.O. and Subha, B. 2011b. Gene profiling and characterization of arginine kinase-1 (MrAK-1) from freshwater giant prawn (Macrobrachium rosenbergii). Fish and ShellfishImmunology, 31: 81-89. doi: 10.1016/j.fsi.2011.04.004.
11. Arockiaraj, J., Sarasvathi, E., Puganeshwaran, V., Arunsingh, S.V., Othman, R.Y. and Subha, B. 2012. Immunological role of thiol-dependent peroxiredoxin gene in Macrobrachium rosenbergii. Fish and Shellfish Immunology, 33: 121-129. doi: 10.1016/j.fsi.2012.04.010.
12. Arockiaraj, J., Annie, J.G., Dhanaraj, M., Mukesh, P., Milton, J. and Arun, S. 2013a. An upstream initiator caspase 10 of snakehead murrel Channa striatus, containing DED, p20 and p10 subunits: Molecular cloning, gene expression and proteolytic activity. Fish and Shellfish Immunology, 34: 505-513. doi: 10.1016/j.fsi.2012.11.040.
13. Arockiaraj, J., Annie, J.G., Venkatesh, K., Rajesh, P., Prasanth, B., Thirumalai, M.K., Arpita, R., Mukesh, P. and Kasi, M. 2013d. An unconventional antimicrobial protein histone from freshwater prawn Macrobrachium rosenbergii: Analysis of immune properties. Fish and Shellfish Immunology, 35: 1511-1522. doi: 10.1016/j.fsi.2013.08.018.
14. Arockiaraj, J., Sarasvathi, E., Puganeshwaran, V., Arun, S., Rofina, Y.O. and Subha, B. 2011. Effect of infectious hypodermal and hematopoietic necrosis virus (IHHNV) infection on caspase 3c expression and activity in freshwater prawn Macrobrachium rosenbergii. Fish and Shellfish Immunology, 32: 161-169. doi: 10.1016/j.fsi.2011.11.006.
15. Arockiaraj, J., Sarasvathi, E., Puganeshwaran, V., Arun, S., Rofina, Y.O. and Subha, B. 2012a. Molecular cloning, characterization and gene expression of an antioxidant enzyme catalase (MrCat) from Macrobrachium rosenbergii. Fish and Shellfish Immunology, 32: 670-682. doi: 10.1016/j.fsi.2012.01.013.
16. Bhatt, P., Venkatesh, K., Rajesh, P., Mukesh, K.C., Annie, J.G., Mukesh, P. and Arockiaraj, J. 2013. Immunological role of C4 CC chemokine-1 from snakehead murrel Channa striatus. Molecular Immunology, 57: 292-293. doi: 10.1016/j.molimm.2013.10.012.
17. Blomgran, R., Zheng, L. and Stendahl, O. 2007. Cathepsincleaved Bid promotes apoptosis in human neutrophils via oxidative stress-induced lysosomal membrane permeabilization. Journal of Leucine Biology, 81: 1213-1223. doi:10.1189/jlb.0506359.
18. Chwieralski, C.E., Welte, T. and Bühling, F. 2006. Cathepsin-regulated apoptosis. Apoptosis, 11: 143-149. doi: 10.1007/s10495-006-3486-y.
19. Darawiroj, D., Kondo, H., Hirono, I. and Aoki, T. 2008. Immune-related gene expression profiling of yellowtail (Seriola quinqueradiata) kidney cells stimulated with ConA and LPS using microarray analysis. Fish and Shellfish Immunology, 24: 260-266. doi: 10.1016/j.fsi.2007.07.011.
20. Dhanaraj, M., Haniffa, M.A., Ramakrishnan, C.M. and Arunsingh, S.V. 2008. Microbial flora from the epizootic ulcerative syndrome (EUS) infected murrel Channa striatus (Bloch, 1797) in Tirunelveli region. Turkish Journal of Veterinary and Animal Sciences, 32: 221-224.
21. Feng, T., Zhang, H., Liu, H., Zhou, Z., Niu, D., Wong, L., Kucuktas, H., Liu, X., Peatman, E. and Liu, Z. 2011. Molecular characterization and expression analysis of the channel catfish cathepsin D genes. Fish and Shellfish Immunology, 31: 164-169. doi: 10.1016/j.fsi.2011.04.006.
22. Foghsgaard, L., Wissing, D., Mauch, D., Lademann, U., Bastholm, L., Boes, M., Elling, F., Leist, M. and Jaattela, M. 2001. Cathepsin B acts as a dominant execution protease in tumor cell apoptosis induced by tumor necrosis factor. Journal of Cell Biology, 153: 999-1010. doi: 10.1083/jcb.153.5.999.
23. Friedrichs, B., Tepel, C., Reinheckel, T., Deussing, J., von Figura, K., Herzog, V., Peters, C., Saftig, P. and Brix, K. 2003. Thyroid functions of mouse cathepsins B, K, and L. Journal of Clinical Investigation, 111: 1733-1745. doi: 10.1172/JCI200315990.
24. Guicciardi, M.E., Miyoshi, H., Bronk, S.F. and Gores, G.J. 2001. Cathepsin B knockout mice are resistant to tumor necrosis factor-α mediated hepatocyte apoptosis and liver injury: implications for therapeutic applications. American Journal of Pathology, 159: 2045-2054. doi: 10.1016/S0002-9440(10)63056-8.
25. Hiromi, S. and Jimmy, B.F. 2008. Lysine-Enriched Cecropin-Mellitin Antimicrobial Peptides with Enhanced Selectivity. Antimicrobial Agents Chemotherapy, 52: 4463-4465. doi: 10.1128/AAC.00810-08.
26. Holt, O.J., Gallo, F. and Griffiths, G.M. 2006. Regulating secretory lysosomes. J. Biochem., 140: 7-12. doi: 10.1093/jb/mvj126.
27. Illy, C., Quraishi, O., Wang, J., Purisima, E., Vernet, T. and Mort, JS. 1997. Role of the occluding loop in cathepsin B activity. Journal of Biological Chemistry, 272: 1197-1202. doi: 10.1074/jbc.272.2.1197.
28. Itami, T., Takahashi, Y. and Sato, K. 1987. Bacteriolytic activities in the skin mucus of ayu. Nippon Suisan Gakkaishi, 53: 401-406.
29. Jais, A.M.M., Dambisya, Y.M. and Lee, T.L. 1997. Antinociceptive activity of Channa striatus extracts in mice. Journal of Ethnopharmacology, 57: 125-130. doi: 10.1016/S0378-8741(97)00057-3.
30. Jais, A.M.M., Mc Culloch, R. and Croft, K.D. 1994. Fatty acid and amino acid composition of Haruan-Potential for Wound healing. General Pharmacology, 25: 947-950. doi: 10.1016/0306-3623(94)90101-5.
31. Lacaille, F., Kaleta, J. and Brömme, D. 2002. Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design. Chemical Reviews, 102:4459-88. doi: 10.1021/cr0101656.
32. Lilley, J.H. and Roberts, R.J. 1997. Pathogenicity and culture studies comparing the Aphanomyces involved in epizootic ulcerative syndrome (EUS) with other similar fungi. Journal of Fish Diseases, 20: 135-144. doi: 10.1046/j.1365-2761.1997.d01-116.x.
33. Liu, H., Yin, L., Zhang, N., Li, S. and Ma, C. 2008. Isolation of cathepsin B from the muscle of silver carp (Hypophthalmichthys molitrix) and comparison of cathepsins B and L actions on surimi gel softening. Food Chemistry, 110: 310-318. doi:10.1016/j.foodchem.2008.01.068.
34. Livak, K.J. and Schmittgenm, T.D. 2001. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods, 25: 402-408. doi:10.1006/meth.2001.1262.
35. Ma, J., Zhang, D., Jiang, J., Cui, S., Pu, H. and Jiang, S. 2010. Molecular characterization and expression analysis of cathepsin L1 cysteine protease from pearl oyster Pinctada fucata. Fish and Shellfish Immunology, 29: 501-507. doi: 10.1016/j.fsi.2010.05.006.
36. Mann, M. and Aebersold, R. 2003. Mass spectrometry-based proteomics. Nature, 422: 198-207. doi:10.1038/nature01511.
37. Markossian, K.A., Zamyatnin, A.A. and Kurganov, B.I. 2004. Antibacterial proline-rich oligopeptides and their target proteins. Biochemistry (Mosc), 69: 1082-1091. doi: 10.1023/B:BIRY.0000046881.29486.51.
38. Mueller-Steiner, S., Zhou, Y., Arai, H., Roberson, E.D., Sun, B., Chen, J., Wang, X., Yu, G., Esposito, L., Mucke, L. and Gan, L. 2006. Antiamyloidogenic and neuroprotective functions of cathepsin B: Implications for Alzheimer’s disease. Neuron, 51: 703-714. doi:10.1016/j.neuron.2006.07.027.
39. Musil, D., Zucic, D., Turk, D., Engh, R.A., Mayr, I., Huber, R., Popovic, T., Turk, V., Towatari, T. and Katunuma, N. 1991. The refined 2.15 Å X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity. EMBO Journal, 10: 2321-2330.
40. Nguyen, Q., Mort, J.S. and Roughley, P.J. 1990. Cartilage proteoglycan aggregate is degraded more extensively by cathepsin L than by cathepsin B. Biochemistry Journal., 266: 569-573.
41. Otvos, L Jr. 2002. The short proline-rich antibacterial peptide family. Cellular and Molecular Life Sciences, 59: 1138-1150. doi: 10.1007/s00018-002-8493-8.
42. Salvesen, G.S. 2001. A lysosomal protease enters the death scene. Journal of Clinical Investigation, 107: 21-23. doi: 10.1172/JCI11829.
43. Sitaram, N. 2006. Antimicrobial peptides with unusual amino acid compositions and unusual structures. Current Medicinal Chemistry, 13: 679-696. doi: 10.2174/092986706776055689.
44. Somboonwiwat, K., Marcos, M., Tassanakajon, A., Klinbunga, S., Aumelas, A., Romestand, B., Gueguen, Y., Boze, H., Moulin, G. and Bachère, E. 2005. Recombinant expression and anti-microbial activity of anti-lipopolysaccharide factor (ALF) from the black tiger shrimp Penaeus monodon. Developmental and Comparative Immunology, 29: 841-851. doi: 10.1016/j.dci.2005.02.004.
45. Stephens, A., Rojo, L., Araujo-Bernal, S., Garcia-Carreño, F. and Muhlia-Almazan, A. 2012. Cathepsin B from the white shrimp Litopenaeus vannamei: cDNA sequence analysis, tissues-specific expression and biological activity. Comparative Biochemistry and Physiology Part B, 161:32-40. doi: 10.1016/j.cbpb.2011.09.004.
46. Suh, J.Y., Lee, Y.T., Park, C.B, Lee, K.H, Kim, S.C. and Choi, B.S. 1999. Structural and functional implications of a proline residue in the antimicrobial peptide gaegurin. Europena Journal of Biochemistry, 266: 665-674. doi: 10.1046/j.1432-1327.1999.00917.x.
47. Takahashi, Y., Kajiwaki, T., Itami, T. and Konegawa, K. 1987. Enzymatic properties of the bacteriolytic substances in the skin mucus of yellowtail. Nippon Suisan Gakkaishi, 53: 425-431.
48. Thennarasu, S. and Nagaraj, R. 1996. Specific antimicrobial and hemolytic activities of 18-residue peptides derived from the amino terminal region of the toxin pardaxin. Protein Engineering 9: 1219-1224. doi: 10.1093/protein/9.12.1219.
49. Thomssen, C., Schmitt, M., Goretzki, L., Oppelt, P., Pache, L., Dettmar, P., Janicke, F. and Graeff, H. 1995. Prognostic value of the cysteine proteases Cathepsin B and Cathepsin L in human breast cancer. Clinical Cancer Research, 1: 741-746.
50. Torrent, M., Tommaso, P.D., Pulido, D., Nogués, M.V., Notredame, C., Boix, E. and Andreu, D. 2012. AMPA: an automated web server for prediction of protein antimicrobial regions. Bioinformatics, 28: 130-131. doi: 10.1093/bioinformatics/btr604.
51. Trent, M.S., Stead, C.M., Tran, A.X. and Hankins, J.V. 2006. Diversity of endotoxin and its impact on pathogenesis. Journal of Endotoxin Research, 12: 200-223. doi: 10.1177/09680519060120040201.
52. Turk, B., Turk, D. and Turk, V. 2000. Lysosomal cysteine proteases: more than scavengers. Biochemica et Biophysica Acta, 1477: 98-111. doi: 10.1016/S0167-4838(99)00263-0.
53. Turk, V., Turk, B. and Turk, D. 2001. Lysosomal cysteine proteases: facts and opportunities EMBO Journal, 20: 4629-4633. doi: 10.1093/emboj/20.17.4629
54. Uinuk-Ool, T.S., Takezaki, N., Kuroda, N., Figueroa, F., Sato, A., Samonte, I.E., Mayer, W.E. and Klein, J. 2003. Phylogeny of antigen-processing enzymes: cathepsins of a cephalochordate, an agnathan and a bony fish. Scandinavian Journal of Immunology, 58: 436-448. doi: 10.1046/j.1365-3083.2003.01322.x.
55. Vasiljeva, O., Reinheckel, T., Peters, C., Turk, D., Turk, V. and Turk, B. 2007. Emerging roles of cysteine cathepsins in disease and their potential as drug targets. Current Pharmaceutical Design, 13: 387-403. doi: 10.2174/138161207780162962
56. Wang, X., Liu, B., Wang, G., Tang, B. and Xiang, J. 2008. Molecular cloning and functional analysis of cathepsin B in nutrient metabolism during larval development in Meretrix meretrix. Aquaculture, 282: 41-46. doi: 10.1016/j.aquaculture.2008.06.014.
57. Whang, I., De Zoysa, M., Nikapitiya, C., Lee, Y., Kim, Y, Lee, S., et al. 2011. Molecular characterization and expression analysis of Cathepsin B and L cysteine proteases from rock bream (Oplegnathus fasciatus). Fish and Shellfish Immunology, 30: 763-772. doi: 10.1016/j.fsi.2010.12.022.
58. Zhang, F.T., Zhang, Y.B., Chen, Y.D., Zhu, R., Dong, C.W., Li, Y.Y., Zhang, Q.Y. and Gui, J.F 2008. Expressional induction of Paralichthys olivaceus cathepsin B gene in response to virus, poly I:C and lipopolysaccharide. Fish and Shellfish Immunology, 25: 542-549. doi: 10.1016/j.fsi.2008.07.018.