title: Cryptosporidium parvum: structural components of the oocyst wall.
abstract: Cryptosporidium parvum, an enteropathogenic parasite, infects a wide range of mammals including man and constitutes a substantial veterinary and medical threat due to its ubiquitous distribution and the stability of the oocyst stage. The oocyst wall of C. parvum is known to be extremely resistant to chemical and mechanical disruption. Isolated oocyst walls are shown by both thin sectioning and negative staining transmission electron microscopy to possess a filamentous array on the inner surface. This filamentous array can be greatly depleted by digestion with proteinase K and trypsin, but pepsin has less effect. Ultrasonication of the untreated oocyst walls produced almost no fragmentation, but extension of the suture resulted in inward spiraling of the wall to generate ellipsoid and cigar-shaped multilayer bodies, with the filamentous array still present. When ultrasonicated, proteinase K-digested oocyst walls progressively fragmented into small sheets. These wall fragments, depleted of filaments, are shown by negative staining to possess a pronounced linearity, indicative of an integral highly complex lattice structure.
authors.affiliation: Institute of Zoology, Johannes Gutenberg-University of Mainz, Germany.
authors.forename: J R
authors.initials: JR
authors.lastname: Harris
authors.forename: F
authors.initials: F
authors.lastname: Petry
mesh_terms: D000818:Animals; D002473:Cell Wall / Q000737:chemistry / Q000648:ultrastructure; D016785:Cryptosporidium parvum / Q000737:chemistry / Q000648:ultrastructure*; D004591:Electrophoresis, Polyacrylamide Gel; D019286:Endopeptidase K / Q000378:metabolism; D008854:Microscopy, Electron; D010434:Pepsin A / Q000378:metabolism; D015800:Protozoan Proteins / Q000032:analysis; D013010:Sonication; D014357:Trypsin / Q000378:metabolism; D015053:Zygote / Q000737:chemistry / Q000648:ultrastructure*
chemical_list: D015800:Protozoan Proteins; D014357:Trypsin; D019286:Endopeptidase K; D010434:Pepsin A