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

Published online by Cambridge University Press:  03 March 2004

J. R. HARRIS
Affiliation:
Institute of Zoology, Johannes Gutenberg-University, D-55099 Mainz, Germany
M. ADRIAN
Affiliation:
Bâtiment de Biologie, Laboratoire d'Analyse Ultrastructurale, Université de Lausanne, CH 1015 Lausanne, Switzerland
F. PETRY
Affiliation:
Institute of Medical Microbiology and Hygiene, Johannes Gutenberg-University, D-55101 Mainz, Germany

Abstract

Amylopectin is used for carbohydrate storage in different life-stages of a number of apicomplexan parasites. We have performed an ultrastructural analysis of amylopectin granules from the oocyst residual body and sporozoites of Cryptosporidium 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 granules (0·1–0·3 μm) 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 α-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.

Type
Research Article
Copyright
2004 Cambridge University Press

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