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Korean J Parasitol > Volume 34(4):1996 > Article

Original Article
Korean J Parasitol. 1996 Dec;34(4):215-224. English.
Published online Dec 20, 1996.  http://dx.doi.org/10.3347/kjp.1996.34.4.215
Copyright © 1996 by The Korean Society for Parasitology
Localization of cytoskeletal proteins in Cryptosporidium parvum using double immunogold labeling
Jae Ran Yu,*1 and Soon Hyung Lee2
1Department of Parasitology, College of Medicine, Kon-Kuk University, Choongju 380-701, Korea.
2Department of Parasitology and Institute of Endemic Diseases, Seoul National University College of Medicine, Seoul 110-799, Korea.
Received October 25, 1996; Accepted November 14, 1996.

Abstract

Actin and some actin binding proteins such as tropomyosin, α-actinin and troponin T were localized by simultaneous double immunogold labeling in several developmental stages of Cryptosporidium parvum. All of the observed developmental stages have many particles of tropomyosin and actin around pellicle and cytoplasm. Tropomyosin was labeled much more than the actin when these two proteins were labeled simultaneously. And α-actinin was labeled mostly in the pellicle, but troponin T labeling was very rarely observed. From this study, it was suggested that tropomyosin seems to be one of the major proteins of C. parvum, so it must be playing important roles in C. parvum.

Keywords: actin, tropomyosin, α-actinin, troponin T, Cryptosporidium parvum.

Figures


Figs. 1-3
Double immunogold labeling at actin and tropomyosin (TM) in C. parvum. The mouse small inestimal brush border was labeled with gold particles (Fig. 1). Trophozoite stage (Fig. 2). Type I meront; both pellices and cytoplasm showed tropomyosin labeling. Host actin particle were labeled under the electro-dense junction. 5 nm, TM; 10 nm, actin (Fig. 3). Bar, 200 nm.


Figs. 4-6
Figs. 4-6. Double immunogold labeling at actin and TM in C. parvum. Developign meronts. 5nm, TM; 10 nm, actin (Fig. 4). Trophozoites and type I meronts showed many gold particles labeled at TM. 5 nm, actin; 10 nm, tropomyosin (Fig. 5-6). Bar, 200 nm.


Figs. 7-8
Fig. 7. Double immunogold labeling at actin and TM in TM in oocyst of C. parvum. 5 nm, actin; 10 nm, TM. Bar, 200 nm. Fig. 8. Immunogold labeling of only TM with silver enhancement in C. parvum. × 5000. Bar, 1 µm.


Figs. 9-10
G. muris immunogold labeled at TM and actin simultaneously. Labeled gold particles were much less than in C. parvum. Vesicles around the flagellum were mostly labeled by gold (Fig. 10). 5 nm, TM; 10 nm, actin. Bar, 200 nm.


Fig. 11
Double immunogold labeling at TM and α-actinin in developing meronts of C. parvum. α-actinin was located mainly around the parasite pellicle and the amount was much less than TM. 5 nm, TM; 15 nm, α-actinin. Bar, 200 nm.


Figs. 12-13
Double immunogold labeling at TM and α-actinin in type I (Fig. 12) and type II meronts (Fig. 13). 5 nm, TM; 15 nm, αactinin. Bar, 200 nm.


Figs. 14-15
Double immunogold labeling at TM and troponin-T in trophozoites (Fig. 14) and type I meronts (Fig. 15). Labeled troponin-T can hardly be seen. 5 nm, TM; 10 nm, troponin-T. Bar, 200 nm.

References
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4. Kim K, Gooze L, Petersen C, Gut J, Nelson RG. Isolation, sequence and molecular karyotype analysis of the actin gene of Cryptosporidium parvum. Mol Biochem Parasitol 1992;50(1):105–113.
  
5. Lau SY, Sanders C, Smillie LB. Amino acid sequence of chicken gizzard gamma-tropomyosin. J Biol Chem 1985;260(12):7257–7263.
 
7. Xu H, Rekosh DM, Andrews W, Higashi GI, Nicholson L, Loverde PT. Schistosoma mansoni tropomyosin: production and purification of the recombinant protein and studies on its immunodiagnostic potential. Am J Trop Med Hyg 1991;45(1):121–131.
 
8. Yu JR, Chai JY. Localization of actin and myosin in Cryptosporidium parvum using immunogold staining. Korean J Parasitol 1995;33(3):155–164.
  
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