title: Mechanism of adhesion and detachment at the anterior end of Merizocotyle icopae (Monogenea: Monocotylidae) including ultrastructure of the anterior adhesive matrix.
abstract: The anterior adhesive mechanism was studied for Merizocotyle icopae (Monogenea: Monocotylidae). Adult anterior apertures can open and close. In addition, duct endings terminating within the apertures are everted or retracted depending on the stage of attachment. Adhesive in adults is synthesized from all 3 secretory types (rod-shaped, small and large spheroidal bodies) found within anterior apertures. All exit together and undergo mixing to produce the adhesive matrix, a process that depletes duct contents. A greater number of ducts carrying rod-shaped bodies is depleted than ducts containing spheroidal bodies which changes the ratio of secretory types present on detachment. Detachment involves elongation of duct endings and secretion of additional matrix as the worm pulls away from the substrate. The change in secretory type ratio putatively modifies the properties of the secreted matrix enabling detachment. Only after detachment do ducts refill. During attachment, individual secretory bodies undergo morphological changes. The larval and adult adhesive matrix differs. Anterior adhesive in oncomiracidia does not show fibres with banding whereas banded fibres comprise a large part of adult adhesive. The data suggest that this is the result of adult spheroidal secretions modifying the way in which the adult adhesive matrix forms.
authors.affiliation: Centre for Microscopy and Microanalysis, The University of Queensland, Brisbane, Queensland 4072, Australia. b.cribb@uq.edu.au
authors.forename: B W
authors.initials: BW
authors.lastname: Cribb
authors.forename: W D
authors.initials: WD
authors.lastname: Armstrong
authors.forename: I D
authors.initials: ID
authors.lastname: Whittington
mesh_terms: D000268:Adhesiveness; D000818:Animals; D008854:Microscopy, Electron; D011793:Queensland; D012860:Skates, Fish / Q000469:parasitology*; D014200:Trematoda / Q000502:physiology* / Q000648:ultrastructure