title: Light and scanning electron microscopy of the ecdysis of Haemonchus contortus infective larvae.
abstract: During the second ecdysis of ruminant trichostrongyles, a region of the second molt cuticle is digested by a 44-kDa Zn-metalloprotease. We have examined this digestion process by light and scanning electron microscopy (SEM). The substrate region of the cuticle appeared, during the ecdysis process, as an indented ring at the 20th cuticular annulus coincident with the anterior terminus of the lateral alae. Continued digestion of the cuticle resulted in holes in the ring region that expanded until they became continuous and separation occurred between the anterior and posterior portions of the cuticle. Mechanical movements of the L3 forced aside the cuticle cap that generally remained attached on one side to the posterior portion as the larva escaped from the sheath. The site of secretion of the 44-kDa ecdysing enzyme causing cuticle digestion was not clear from morphological observations; however, existing evidence strongly points to the release of enzyme from the esophageal (pharyngeal) glands through the mouth.
authors.affiliation: United States Department of Agriculture, Agricultural Research Service, Livestock and Poultry Sciences Institute, Beltsville, Maryland 20705.
authors.forename: H R
authors.initials: HR
authors.lastname: Gamble
authors.forename: J R
authors.initials: JR
authors.lastname: Lichtenfels
authors.forename: J P
authors.initials: JP
authors.lastname: Purcell
mesh_terms: D000818:Animals; D006189:Haemonchus / Q000201:enzymology / Q000254:growth & development / Q000648:ultrastructure*; D007814:Larva / Q000648:ultrastructure; D008855:Microscopy, Electron, Scanning; D010447:Peptide Hydrolases / Q000378:metabolism*; D014251:Trichostrongyloidea / Q000648:ultrastructure*
chemical_list: D010447:Peptide Hydrolases