Surface associated glycoproteins from Toxocara canis larval parasites.

The surface of infective larvae of Toxocara canis, the dog ascarid nematode, reveals relatively few exposed surface proteins which can be recovered in soluble form. The major components identified by surface labelling have molecular weights of 32, 55, 70 and 120 kilodaltons (kDa), and are all significantly glycosylated. All are recognised by the immune response in definitive (canine) and paratenic (murine or human) hosts. Expression of these antigens on the parasite surface begins after the larvae hatch from infective ova in vitro, and presumably in vivo. Each of these molecules may also be found in the set of secreted (ES) glycoconjugates released by larval parasites cultivated in vitro, and currently available biochemical and functional data on the surface/secreted ES glycoproteins are presented. Analysis with monoclonal antibodies (MAbs) confirms the identity of surface and ES molecules, and these MAbs show differing patterns of binding to the epicuticle, the cuticular matrix and to the oral orifice. Alternative mechanisms for antigen synthesis, insertion into the cuticle and export from the parasite are discussed.