Characterization of partially purified 8 kDa antigenic protein of Clonorchis sinensis.
The 8 kDa antigenic protein of Clonorchis sinensis was partially purified by ammonium sulfate precipitation and subsequently by a column chromatographic steps. The purified protein was separated into 7 and 8 kDa protein bands through SDS-tricine gel electrophoresis, while the protein was found to migrate to a 8 kDa band in 7.5-15% SDS-PAGE. The molecular weight of the antigen was estimated to be 110 kDa by Superose 6 HR 10/30 gel filtration. The purified antigen strongly reacted with the human sera of clonorchiasis. The hyperimmune sera of BALB/c mice immunized against the 8 kDa protein were reacted with both the crude extract and the excretory-secretory product of adult worms, but not with the metacercarial extract. Immunohistochemical staining demonstrated that the protein was distributed to the tegument and subtegumental cells and also to the seminal receptacle. The present findings suggest that the 8 kDa protein is a partition of the multicomplex protein originating from various organs of adult C. sinensis, and that it is composed of several 7 and 8 kDa proteins.
Chung
Young-Bae
YB
Department of Parasitology, Institute of Endemic Diseases, Seoul National University College of Medicine, Seoul 110-799, Korea.
Lee
Mejeong
M
Yang
Hyun-Jong
HJ
Chung
Byung-Suk
BS
Lee
Shun-Yu
SY
Choi
Min-Ho
MH
Hong
Sung-Tae
ST
D000818:Animals; D000947:Antigens, Helminth / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D003003:Clonorchiasis / Q000276:immunology; D003004:Clonorchis sinensis / Q000033:anatomy & histology / Q000276:immunology* / Q000378:metabolism; D015801:Helminth Proteins / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D051379:Mice; D008807:Mice, Inbred BALB C; D008970:Molecular Weight
D000947:Antigens, Helminth; D015801:Helminth Proteins