Fasciola hepatica cathepsin L1 from a Turkish isolate is related to Asiatic isolates

• Autorzy: Kuk S , Kaplan M. , Ozdarendeli A. , Tonbak S. , Felek S. , Kalkan A.
• Języki publikacji: EN

Abstrakty

EN

Cathepsin LI (CatLl) is one of the major molecules in the excretory-secretory products of Fasciola hepatica and is secreted by all stages of the developing parasite; it is involved in tissue penetration, immune evasion, feeding and pathogenesis. Our aim in this study was to clone and characterise the F. hepatica CatLl gene from a Turkish isolate. This is the first report of cDNA encoding CatL 1 protein of F. hepatica from a Turkish isolate. Phylogenetic analysis based on the CatLl showed that the Turkish isolate is genetically related to Asiatic isolates. The cathepsin LI gene may be used for DNA vaccination and recombinant protein derived from the gene can be used for serological diagnosis against F. hepatica in Turkey.

Słowa kluczowe

EN

parasitic trematode; Turkish isolate; phylogenetic analysis; cloning; fasciolosis; Fasciola hepatica; sequencing; cathepsin L1

• Wydawca: -
• Czasopismo: Acta Parasitologica
• Rocznik: 2005
• Tom: 50
• Numer: 3
• Opis fizyczny: p.244-248,fig.,ref.

Twórcy

autor

Kuk S

• Firat University, TR23119 Elazig, Turkey

autor

Kaplan M.

autor

Ozdarendeli A.

autor

Tonbak S.

autor

Felek S.

autor

Kalkan A.

Bibliografia

• Andrews S.J. 1999. The life cycle of Fasciola hepatica. In: Fasciolosis (Ed. J.P. Dalton). CAB International, Wallingford, 1-29.
• Carnevale S., Rodriguez M.I., Guarnera E.A., Carmona C., Tanos T., Angel S.O. 2001. Immunodiagnosis of fasciolosis using recombinant procathepsin L cystein proteinase. Diagnostic Microbiology and Infectious Disease, 41, 43-49.
• Cornelissen J.B., Gaasenbeek C.P., Boersma W., Borgsteede F.H., van Miliigen F.J. 1999. Use of a pre-selected epitope of cathepsin-Ll in a highly specific peptide-based immunoassay for the diagnosis of Fasciola hepatica infections in cattle. International Journal for Parasitology, 29, 685-696.
• Cornelissen J.B., Gaasenbeek C.P., Borgsteede F.H., Holland W.G., Harmsen M.M., Boersma W.J. 2001. Early immunodiagnosis of fasciolosis in ruminants using recombinant Fasciola hepatica cathepsin L-like protease. International Journal for Parasitology, 31, 728-737.
• Dalton J.P., Neill S.O., Stack C., Collins P., Walshe A., Sekiya M., Doyle S., Mulcahy G., Hoyle D., Khaznadji E., Moiré N., Brennan G., Mousley A., Kreshchenko N., Maule A.G., Donnelly S.M. 2003. Fasciola hepatica cathepsin L-like proteases: biology, function, and potential in the development of first generation liver fluke vaccines. International Journal for Parasitology, 33, 1173-1181.
• Heussler V.T., Dobbelaere D.A. 1994. Cloning of a protease gene family of Fasciola hepatica by the polymerase chain reaction. Molecular and Biochemical Parasitology, 64, 11-23.
• Irving J.A., Spithill T.W., Pike R.N., Whisstock J.C., Smooker P.M. 2003. The evolution of enzyme specificity in Fasciola spp. Journal of Molecular Evolution, 57, 1-15.
• Jameson B.A., Wolf H. 1988. The antigenic index: a novel algorithm for predicting antigenic determinants. Computer Applications in the Biosciences, 4, 181-186.
• Karrer K.M., Peiffer S.L., DiTomas M.E. 1993. Two distinct gene subfamilies within the family of cysteine protease genes. Proceedings of the National Academy of Sciences of the United States of America, 90, 3063-3067.
• Kreusch S., Fehn M., Maubach G., Nissler K., Rommerskirch W., Schilling K., Weber E., Wenz I., Wiederanders B. 2000. An evolutionarily conserved tripartite tryptophan motif stabilizes the prodomains of cathepsin L-like cysteine proteases. European Journal of Biochemistry, 267, 2965-2972.
• O'Neill S.M., Parkinson M., Strauss W., Angles R., Dalton J.P. 1998. Immunodiagnosis of Fasciola hepatica infection (fascioliasis) in a human population in the Bolivian Altiplano using purified cathepsin L cysteine proteinase. American Journal of Tropical Medicine and Hygiene, 58, 417-423.
• Ozdarendeli A., Kaplan M., Kuk S., Demirdag K., Kalkan A. 2003. In vitro transcription of the Fasciola hepatica cathepsin L1 gene (preliminary study). Acta Parasitologica Turcica, 27, 27-30.
• Panaccio M., Trudgett A. 1999. Molecular biology. In: Fasciolosis (Ed. J.P. Dalton). CAB International, Wallingford, 449-464.
• Roche L., Tort J., Dalton J.P. 1999. The propeptide of Fasciola hepático cathepsin L is a potent and selective inhibitor of the mature enzyme. Molecular and Biochemical Parasitology, 98, 271-277.
• Saitou N., Nei M. 1987. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Molecular Biology and Evolution, 4, 406-425.
• Sambrook J., Fritsch E.F., Maniatis T. 1989. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory Press, New York.
• Tao K., Stearns N.A., Dong J., Wu Q.L., Sahagian G.G. 1994. The proregion of cathepsin L is required for proper folding, stability, and ER exit. Archives of Biochemistry and Biophysics, 311, 19-27.
• Thompson J.D., Higgins D.G., Gibson T.J. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Research, 22, 4673-4680.
• Tort J., Brindley P.J., Knox D., Wolfe K.H., Dalton J.P. 1999. Proteinases and associated genes of parasitic helminths. Advances in Parasitology, 43, 161-266.
• Vernet T., Berti P.J., de Montigny C., Musil R., Tessier D.C., Menard R., Magny M.C., Storer A.C., Thomas D.Y. 1995. Processing of the papain precursor. The ionization state of a conserved amino acid motif within the Pro region participates in the regulation of intramolecular processing. Journal of Biological Chemistry, 270, 10838-10846.
• Wijffels G.L., Panaccio M., Salvatore L., Wilson L., Walker I.D., Spithill T.W. 1994. The secreted cathepsin L-like proteinases of the trematode, Fasciola hepatica, contain 3-hydroxyproline residues. Biochemical Journal, 299, 781-790.
• Yamasaki H., Aoki T. 1993. Cloning and sequence analysis of the major cysteine protease expressed in the trematode parasite Fasciola sp. Biochemistry and Molecular Biology International, 31, 537-542.
• Yamasaki H., Mineki R., Murayama K., Ito A., Aoki T. 2002. Characterisation and expression of the Fasciola gigantica cathepsin L gene. International Journal for Parasitology, 32, 1031-1042.