Amylopectin:: a major component of the residual body in Cryptosporidium parvum oocysts

被引:14
作者
Harris, JR
Adrian, M
Petry, F
机构
[1] Univ Mainz, Inst Med Microbiol & Hyg, D-55101 Mainz, Germany
[2] Univ Lausanne, Lab Anal Ultrastruct, CH-1015 Lausanne, Switzerland
[3] Univ Mainz, Inst Zool, D-55099 Mainz, Germany
关键词
amylopectin; Crytosporidium parvum; residual body; sporozoite; electron microscopy; negative staining;
D O I
10.1017/S003118200300458X
中图分类号
R38 [医学寄生虫学]; Q [生物科学];
学科分类号
07 ; 0710 ; 09 ; 100103 ;
摘要
Amylopectin is used for carbohydrate storage in different life-stages of a number of apicomplexan parasites. We have performed all ultrastructural analysis of amylopectin granules from the oocyst residual body and sporozoites of cryptos-poridium parvum. Amylopectin granules were studied in situ and after isolation from 'French' press disrupted parasites, by conventional transmission electron microscopy (TEM) of sectioned oocysts and various negative staining and cryoelectron microscopy techniques. Within the membrane-enclosed oocyst residuum large amylopectin (0.1-0.3 mum) can be found besides a characteristic large lipid body and a crystalline protein inclusion. Smaller granules were detected in sectioned sporozoites. Negative staining of isolated amylopectin granules revealed some ultrastructural features not readily visible in sectioned material. The large amylopectin granules had a smooth surface with a 'ball of string'-like inner structure. Granules isolated from sporozoites were more irregularly shaped and showed a rod-like particulate composition. With the exception of alpha-amylase, which led to some degree of damage of the surface of the particles, treatment of amylopectin granules with other glycohydrolases had little effect on the overall structure. However, granules adhered to one another. Only when the granules were boiled did the 'ball of string' structure gradually dissolve.
引用
收藏
页码:269 / 282
页数:14
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