A 78 kDa glucose-regulated protein gene of Spirometra erinacei plerocercoid induced by chemical and physiological stresses.
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 degrees C and 37 degrees 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 degrees C to 37 degrees 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.
Yun
D H
DH
Department of Molecular Parasitology and Center for Molecular Medicine, Samsung Biomedical Research Institute and Sungkyunkwan University School of Medicine, Suwon 440-746, Korea.
Bae
Y A
YA
Chung
J Y
JY
Kang
S Y
SY
Kang
I
I
Sohn
W M
WM
Cho
S H
SH
Kim
T S
TS
Cho
S Y
SY
Kong
Y
Y
D000222:Adaptation, Physiological; D000595:Amino Acid Sequence; D000818:Animals; D000091342:Endoplasmic Reticulum Chaperone BiP; D005786:Gene Expression Regulation / Q000187:drug effects / Q000502:physiology; D006360:Heat-Shock Proteins / Q000096:biosynthesis* / Q000502:physiology; D015801:Helminth Proteins / Q000096:biosynthesis* / Q000502:physiology; D006790:Host-Parasite Interactions; D018832:Molecular Chaperones / Q000096:biosynthesis* / Q000502:physiology; D008969:Molecular Sequence Data; D010802:Phylogeny; D012333:RNA, Messenger; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013032:Sparganum / Q000187:drug effects / Q000235:genetics / Q000502:physiology*; D013045:Species Specificity
D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins; D015801:Helminth Proteins; D018832:Molecular Chaperones; D012333:RNA, Messenger