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Molecular and biochemical characterization of Paragonimus westermani tyrosinase

Published online by Cambridge University Press:  26 January 2015

Y.-A. BAE ,
S.-H. KIM ,
C.-S. AHN ,
J.-G. KIM  and
Y. KONG
Y.-A. BAE
Affiliation:
Department of Microbiology, Gachon University Graduate School of Medicine, Incheon 406-799, Korea
S.-H. KIM
Affiliation:
Department of Microbiology, Gachon University Graduate School of Medicine, Incheon 406-799, Korea
C.-S. AHN
Affiliation:
Department of Molecular Parasitology, Sungkyunkwan University School of Medicine, and Center for Molecular Medicine, Samsung Biomedical Research Institute, Suwon 440-746, Korea
J.-G. KIM
Affiliation:
Department of Molecular Parasitology, Sungkyunkwan University School of Medicine, and Center for Molecular Medicine, Samsung Biomedical Research Institute, Suwon 440-746, Korea
Y. KONG*
Affiliation:
Department of Molecular Parasitology, Sungkyunkwan University School of Medicine, and Center for Molecular Medicine, Samsung Biomedical Research Institute, Suwon 440-746, Korea
*
* Corresponding author. Department of Molecular Parasitology, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea. E-mail: kongy@skku.edu
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Summary

Trematode tyrosinases (TYRs) play a major role in the tanning process during eggshell formation. We investigated the molecular and biochemical features of Paragonimus westermani TYR (PwTYR). The PwTYR cDNA was composed of 1568-bp encompassing a 1422-bp-long open reading frame (474-amino acid polypeptide). A strong phylogenetic relationship with Platyhelminthes and Deuterostomian orthologues was evident. The recombinant PwTYR expressed in prokaryotic cells promptly oxidized diphenol substrates, with a preferential affinity toward ortho-positioned hydroxyl groups. It demonstrated fairly weak activity for monophenol compounds. Diphenol oxidase activity was augmented with an increase of pH from 5·0 to 8·0, while monophenol oxidase activity was highest at an acidic pH and gradually decreased as pH increased. Transcription profile of PwTYR was temporally upregulated along with worm development. PwTYR was specifically localized in vitellocytes and eggs. The results suggested that conversion of tyrosine to L-dihydroxyphenylalanine by PwTYR monophenol oxidase activity might be rate-limiting step during the sclerotization process of P. westermani eggs. The pH-dependent pattern of monophenol and diphenol oxidase activity further proposes that the initial hydroxylation might slowly but steadily progress in acidic secreted vesicles of vitellocytes and the second oxidation process might be rapidly accelerated by neural or weak alkaline pH environments within the ootype.

Keywords

Paragonimus westermanityrosinaserecombinant enzymepH-dependent tyrosinase activityeggshellvitellocyte
Type
Research Article
Information
Parasitology , Volume 142 , Issue 6 , May 2015 , pp. 807 - 815
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Copyright
Copyright © Cambridge University Press 2015 

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References

REFERENCES

Ahn, C. S., Na, B. K., Chung, D. I., Kim, J. G., Kim, J. T. and Kong, Y. (2014). Expression characteristics and specific antibody reactivity of diverse cathepsin F members of Paragonimus westermani . Parasitology International 64, 37–42.Google Scholar
Bae, Y. A., Cai, G. B., Kim, S. H., Sohn, W. M. and Kong, Y. (2013). Expression pattern and substrate specificity of Clonorchis sinensis tyrosinases. International Journal for Parasitology 43, 891–900.CrossRefGoogle ScholarPubMed
Bae, Y. A., Kim, S. H., Cai, G. B., Lee, E. G., Kim, T. S., Agatsuma, T. and Kong, Y. (2007). Differential expression of Paragonimus westermani eggshell proteins during the developmental stages. International Journal for Parasitology 37, 295–305.Google Scholar
Cai, G. B., Bae, Y. A., Zhang, Y., He, Y., Jiang, M. S. and He, L. (2009). Expression and characterization of two tyrosinases from the trematode Schistosoma japonicum . Parasitology Research 104, 601–609.CrossRefGoogle ScholarPubMed
Cho, S. Y., Kong, Y., Yun, D. H., Kang, S. Y., Kim, L. S., Chung, Y. B. and Yang, H. J. (2000). Persisting antibody reaction in paragonimiasis after praziquantel treatment is elicited mainly by egg antigens. Korean Journal of Parasitology 38, 75–84.Google Scholar
Cordingley, J. S. (1987). Trematode eggshells: novel protein biopolymers. Parasitology Today 3, 341–344.Google Scholar
Fitzpatrick, J. M., Hirai, Y., Hirai, H. and Hoffmann, K. F. (2007). Schistosome egg production is dependent upon the activities of two developmentally regulated tyrosinases. FASEB Journal 21, 823–835.Google Scholar
Fitzpatrick, J. M., Johansen, M. V., Johnston, D. A., Dunne, D. W. and Hoffmann, K. F. (2004). Gender-associated gene expression in two related strains of Schistosoma japonicum . Molecular and Biochemical Parasitology 136, 191–209.CrossRefGoogle ScholarPubMed
Fürst, T., Duthaler, U., Sripa, B., Utzinger, J. and Keiser, J. (2012). Trematode infections: liver and lung flukes. Infectious Disease Clinics of North America 26, 399–419.Google Scholar
He, Y., Cai, G., Ni, Y., Li, Y., Zong, H. and He, L. (2012). siRNA-mediated knockdown of two tyrosinase genes from Schistosoma japonicum cultured in vitro . Experimental Parasitology 132, 394–402.Google Scholar
Jaenicke, E. and Decker, H. (2004). Functional changes in the family of type 3 copper proteins during evolution. ChemBioChem 5, 163–169.Google Scholar
Land, E. J., Ramsden, C. A. and Riley, P. A. (2003). Tyrosinase autoactivation and the chemistry of ortho-quinone amines. Accounts of Chemical Research 36, 300–308.Google Scholar
Lane, M. A., Barsanti, M. C., Santos, C. A., Yeung, M., Lubner, S. J. and Weil, G. J. (2009). Human paragonimiasis in North America following ingestion of raw crayfish. Clinical Infectious Diseases 15, e55–e61.Google Scholar
Ma, L. (1963). Trace elements and polyphenol oxidase in Clonorchis sinensis . Journal of Parasitology 49, 197–203.Google Scholar
Mansour, T. E. (1958). Effect of serotonin on phenol oxidase from the liver fluke Fasciola hepatica and from other sources. Biochimica et Biophysica Acta 30, 492–500.Google Scholar
Marles, L. K., Peters, E. M., Tobin, D. J., Hibberts, N. A. and Schallreuter, K. U. (2003). Tyrosine hydroxylase isoenzyme I is present in human melanosomes: a possible novel function in pigmentation. Experimental Dermatology 12, 61–70.CrossRefGoogle Scholar
Nakamura-Uchiyama, F., Mukae, H. and Nawa, Y. (2002). Paragonimiasis: a Japanese perspective. Clinics in Chest Medicine 23, 409–420.Google Scholar
Nellaiappan, K., Devasundari, A. F. and Dhandayuthapani, S. (1989). Properties of phenol oxidase in Fasciola gigantica . Parasitology 99, 403–407.CrossRefGoogle ScholarPubMed
Olivares, C. and Solano, F. (2009). New insights into the active site structure and catalytic mechanism of tyrosinase and its related proteins. Pigment Cell and Melanoma Research 22, 750–760.Google Scholar
Park, H. Y., Russakovsky, V., Ohno, S. and Gilchrest, B. A. (1993). The beta isoform of protein kinase C stimulates human melanogenesis by activating tyrosinase in pigment cells. Journal of Biological Chemistry 268, 11742–11749.Google Scholar
Peñafiel, R., Galindo, J. D., Pedreño, E. and Lozano, J. A. (1982). The process for the activation of frog epidermis pro-tyrosinase. Biochemical Journal 205, 397–404.CrossRefGoogle ScholarPubMed
Ramalingam, K. (1970). Prophenolase and the role of Mehlis’ gland in helminthes. Experientia 26, 828.Google Scholar
Rice-Ficht, A. C., Dusek, K. A., Kochevar, G. J. and Waite, J. H. (1992). Eggshell precursor proteins of Fasciola hepatica, I. Structure and expression of vitelline protein B. Molecular and Biochemical Parasitology 54, 129–141.Google Scholar
Seed, J. L., Boff, M. and Bennett, J. L. (1978). Phenol oxidase activity: induction in female schistosomes by in vitro incubation. Journal of Parasitology 64, 283–289.Google Scholar
Smyth, J. D. and Halton, D. W. (1983). The Physiology of Trematodes. Cambridge University Press, Cambridge, UK.Google Scholar
Threadgold, L. T. (1982). Fasciola hepatica: stereological analysis of vitelline cell development. Experimental Parasitology 54, 352–365.Google Scholar
Wells, K. E. and Cordingley, J. S. (1991). Schistosoma mansoni: eggshell formation is regulated by pH and calcium. Experimental Parasitology 73, 295–310.Google Scholar
Zhang, Y. (2008). I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9, 40.Google Scholar