title: Ultrastructural and cytochemical aspects of Schistosoma mansoni cercaria.
abstract: An alternative to identify the critical processes necessary to the parasite establishment of the host is to focus on the evolutionary stage responsible for the primary invasion, i.e. the infection structure. The objective of this study was to ultrastructurally characterize Schistosoma mansoni cercariae, using cytochemical techniques. In order to identify basic proteins, techniques such as ethanolic phosphotungstic acid (EPTA) and ammoniacal silver staining were used. Calcium sites location was achieved using the Hepler technique and to evidence anionic groups, we used cationic ferritin particles and enzyme treatment with trypsin Vibrio cholerae, chondroitinase and neuraminidase. The EPTA technique highlighted the presence of basic tegument proteins, nucleus and nucleolus from subtegumental cells, inclusion bodies and preacetabular glands. After using ammoniacal silver, we observed a strong staining in all infective larvae, particularly in the nuclei of muscle cells, circular muscle tissue and preacetabular glands. Calcium site locations were shown to be uniform, thereby limiting the inner spaces of the larvae, especially muscle cells. Samples treated with cationized ferritin particles presented strong staining at the cuticular level. Neuraminidase treatment did not alter the stained shape of such particles on the trematode surface. However, trypsin or chondroitinase treatment resulted in absence of staining on the larval surface. This information on the biochemical composition of the infecting S. mansoni larvae provides data for a better understanding of the biology of this parasite and background on the intriguing parasite-host relationship.
authors.affiliation: Departamento de Parasitologia, Centro de Pesquisas Aggeu Magalhães, Recife - PE, Brazil.
authors.forename: M G S
authors.initials: MG
authors.lastname: Cavalcanti
authors.forename: H R C
authors.initials: HR
authors.lastname: Araújo
authors.forename: M H S
authors.initials: MH
authors.lastname: Paiva
authors.forename: G M
authors.initials: GM
authors.lastname: Silva
authors.forename: C C G S
authors.initials: CC
authors.lastname: Barbosa
authors.forename: L F
authors.initials: LF
authors.lastname: Silva
authors.forename: F A
authors.initials: FA
authors.lastname: Brayner
authors.forename: L C
authors.initials: LC
authors.lastname: Alves
mesh_terms: D000818:Animals; D001485:Basement Membrane / Q000737:chemistry / Q000648:ultrastructure; D002118:Calcium / Q000737:chemistry; D002810:Chondroitinases and Chondroitin Lyases / Q000378:metabolism; D015801:Helminth Proteins / Q000737:chemistry / Q000648:ultrastructure; D006790:Host-Parasite Interactions / Q000502:physiology; D006801:Humans; D002479:Inclusion Bodies / Q000737:chemistry / Q000648:ultrastructure; D007814:Larva / Q000737:chemistry / Q000201:enzymology / Q000648:ultrastructure; D046529:Microscopy, Electron, Transmission; D009132:Muscles / Q000737:chemistry / Q000648:ultrastructure; D009439:Neuraminidase / Q000378:metabolism; D012550:Schistosoma mansoni / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D012552:Schistosomiasis / Q000469:parasitology; D014357:Trypsin / Q000378:metabolism
chemical_list: D015801:Helminth Proteins; D009439:Neuraminidase; D014357:Trypsin; D002810:Chondroitinases and Chondroitin Lyases; D002118:Calcium