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Protein composition and antigenicity of the tegument from Paragonimus westermani
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Korean J Parasito > Volume 31(3):1993 > Article

Original Article
Korean J Parasitol. 1993 Sep;31(3):269-276. English.
Published online Mar 20, 1994.  http://dx.doi.org/10.3347/kjp.1993.31.3.269
Copyright © 1993 by The Korean Society for Parasitology
Protein composition and antigenicity of the tegument from Paragonimus westermani
S I Kim,*1 and S Y Cho2
1Department of Parasitology, Chosun University Medical College, Kwangju 501-759, Korea.
Received July 09, 1993; Accepted August 05, 1993.

Abstract

To ascertain that tegument of Paragonimus westermani has specific antigenic proteins, the tegumental fraction was isolated from 10-month-old worms by 0.1% digitonin solution, and subjected to SDS-PAGE and immunoblot. Component proteins of tegumental syncytium comprised of 94, 74 (76-66), 62, 54, 44, 42, 38, 28, 26, 25, 24, 17, 15.5 and 13. 5 kDa proteins. Of them, the 94, 44 and 42 kDa proteins were more specific to tegument, especially the 94 kDa protein was the most prevailing one. In immunoblot, antigens of the 94, 90, 78, 76, 74, 68, 65, 62, 60, 59 and 54 kDa proteins were commonly detected by 7 sera of 10 human paragonimiasis, but none of them reacted with 5 sera of clonorchiasis. In conclusion, the 94 kDa protein was the major tegumental protein, as well as the specific antigen. The 76 and 66 kDa proteins were the minor components of tegument, which were also specific antigens of P. westermani.

Figures


Figs. 1-4
Electron microscopic morphology of P. westermani after and before 0.1% digitonin incubation. 1. Scanning electron microscopy (SEM) of 10-month-old worm after removal of tegument showed many grooves on the surface (× 1,480, 30 kV). 2. SEM of the normal control worm (×1,160, 10kV). 3. Transmission electron microscopy (TEM) of carcass showed no tegumental syncytium (TS) with spine (S) and less dense structures of basal lamina (BL) and muscles (M) (× 4,000, a bar equals 2.5 µm). 4. TEM of normal conrol worm (× 3,500, a bar equals 3 µm).


Fig. 5
Protein composition of tegumental fraction of P. westermani as observed by SDS-PAGE. Electrophoretic profile of trgumental protein extract (PwT) and that of crude worm extract (PwW) were compared. Each sample was loaded in protein amount of 40 µg to 10-15% linear gradient gel. Protein bands were detected by silver stain. Mr was standard marker proteins, and numerals represented molecular masses in kDa.


Fig. 6
Antigunicities of tegumental proteins of P. westermani as analyzed by immunoblot. Tegumental proteins of 5 groups (from A to E in SDS-PAGE/immunoblot) are antigenic proteins which are matched with proteins in tegumental protein extract (PwT). Their respective antigens reacted with 7 sera out of 10 human paragonimiasis but react with none of 5 sera of human clonorchiasis.

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