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A 78 kDa glucose-regulated protein gene of Spirometra erinacei plerocercoid induced by chemical and physiological stresses

Published online by Cambridge University Press:  18 November 2004

D.-H. YUN ,
Y.-A. BAE ,
J.-Y. CHUNG ,
S.-Y. KANG ,
I. KANG ,
W.-M. SOHN ,
S.-H. CHO ,
T.-S. KIM ,
S.-Y. CHO  and
Y. KONG
D.-H. YUN
Affiliation:
Department of Molecular Parasitology and Center for Molecular Medicine, Samsung Biomedical Research Institute and Sungkyunkwan University School of Medicine, Suwon 440-746, Korea Department of Parasitology, College of Medicine, Chung-Ang University, Seoul 156-756, Korea
Y.-A. BAE
Affiliation:
Department of Molecular Parasitology and Center for Molecular Medicine, Samsung Biomedical Research Institute and Sungkyunkwan University School of Medicine, Suwon 440-746, Korea
J.-Y. CHUNG
Affiliation:
Department of Molecular Parasitology and Center for Molecular Medicine, Samsung Biomedical Research Institute and Sungkyunkwan University School of Medicine, Suwon 440-746, Korea PharmacoGenomics Research Center, Inje University, Busan 614-735, Korea
S.-Y. KANG
Affiliation:
Department of Parasitology, College of Medicine, Chung-Ang University, Seoul 156-756, Korea
I. KANG
Affiliation:
Department of Biochemistry and Molecular Biology, School of Medicine, Kyung Hee University, Seoul 130-701, Korea
W.-M. SOHN
Affiliation:
Department of Parasitology, College of Medicine, Gyeongsang National University, Jinju 660-751, Korea
S.-H. CHO
Affiliation:
Department of Parasitology, National Institute of Health, Seoul 122-701, Korea
T.-S. KIM
Affiliation:
Department of Parasitology, National Institute of Health, Seoul 122-701, Korea
S.-Y. CHO
Affiliation:
Department of Molecular Parasitology and Center for Molecular Medicine, Samsung Biomedical Research Institute and Sungkyunkwan University School of Medicine, Suwon 440-746, Korea
Y. KONG
Affiliation:
Department of Molecular Parasitology and Center for Molecular Medicine, Samsung Biomedical Research Institute and Sungkyunkwan University School of Medicine, Suwon 440-746, Korea
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Abstract

To adapt to different environmental conditions between poikilothermic and homeothermic hosts, the plerocercoid of Spirometra erinacei (sparganum) might express a variety of biologically active molecules. We have identified a 78 kDa glucose-regulated protein of the sparganum (SpGrp78) by differential display of mRNA, employing RNAs each from sparganum adjusted at 9 °C and 37 °C. A full-length cDNA of 2148 bp encodes for a protein of 651 amino acids with a predicted molecular mass of 71 610 Da and shares molecular characteristics with heat-shock protein 70, including a putative ATP binding site, signal peptide cleavage site and endoplasmic reticulum retention signal. Phylogenetic analysis revealed that SpGrp78 was mostly related to those of Echinococcus multilocularis and E. granulosus. Expression of SpGrp78 mRNA increased approximately 7-fold by inhibition of glycosylation by tunicamycin, 2-fold by temperature-shift from 9 °C to 37 °C and slightly by pH-shift to 4·0 or 5·5. These results suggested that induction of SpGrp78 mRNA is related to the functional role of SpGrp78 as a molecular chaperone when the parasite adapts to a new host environment.

Keywords

Spirometra erinacei plerocercoid (sparganum)stress proteindifferential display PCRheat-shock proteinglucose-regulated proteinmolecular chaperones
Type
Research Article
Information
Parasitology , Volume 129 , Issue 6 , December 2004 , pp. 713 - 721
Copyright
© 2004 Cambridge University Press

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