Changing surface antigen and carbohydrate patterns during the development of Oesophagostomum dentatum.
Living and fixed specimen of Oesophagostomum dentatum were labelled in situ with serum antibodies or a panel of biotin-labelled lectins. Specific binding of antibodies was observed in all parasitic stages--freshly exsheathed 3rd-stage larvae (L3), 3rd- and 4th-stage (L4) larvae cultured in vitro and L3 and L4 and adults isolated from pig intestines. The shedding of the stained layer by motile larvae was inhibited by levamisole-induced paralysis. Larvae cultured in vitro exposed serum-derived proteins on their surface which could be labelled with secondary antibody directed against the respective serum donor species. While freshly exsheathed larvae were recognized by O. dentatum-positive serum only, older larvae and adults cross-reacted with serum from pigs infected with O. quadrispinulatum, a closely related species. Lectin binding varied considerably between stages. While binding was not observed in pre-parasitic stages, Concanavalin A, Soybean Agglutinin, Wheat Germ Agglutinin, Ricinus communis Agglutinin and Peanut Agglutinin bound to developing larvae in varying degrees. Dolichos biflorus Agglutinin only bound to advanced (luminal) larval stages, while adults generally displayed only weak or partial lectin binding (except with Concanavalin A and Wheat Germ Agglutinin). Ulex europaeus Agglutinin only labelled larvae derived from cultures containing 10% pig serum. Cleavage of the carbohydrate residues by sodium periodate treatment resulted in reduction of antibody binding to cultured larvae, but not to freshly exsheathed L3. Concanavalin A, Soybean Agglutinin, and Peanut Agglutinin binding was also reduced by periodate treatment, while binding of Wheat Germ Agglutinin and Ricinus communis Agglutinin was inhibited only in early L3, but not in older stages. The different lectin labelling patterns are related to the different stages of the nematode--infective, invasive, histotropic, and luminal--and may serve as a mode of adaptation for the parasite against the host's immune attack by surface glycoprotein variation, together with antigen shedding (as demonstrated by labelling of motile larvae) and a possible acquisition of host molecules at the parasite's surface. Furthermore, a possible role of this developmental variation in surface carbohydrates in parasite-parasite interactions is discussed.
Joachim
A
A
Institut für Parasitologie, Tierärztliche Hochschule Hannover, Germany.
Ruttkowski
B
B
Daugschies
A
A
D000818:Animals; D000871:Anthelmintics / Q000737:chemistry; D000909:Antibodies, Helminth / Q000737:chemistry / Q000276:immunology; D000947:Antigens, Helminth / Q000737:chemistry* / Q000276:immunology; D000954:Antigens, Surface / Q000737:chemistry / Q000276:immunology; D003208:Concanavalin A / Q000737:chemistry / Q000276:immunology; D000939:Epitopes / Q000276:immunology; D018507:Gene Expression Regulation, Developmental; D007814:Larva / Q000254:growth & development / Q000276:immunology; D037102:Lectins / Q000737:chemistry* / Q000276:immunology; D007978:Levamisole / Q000737:chemistry; D009814:Oesophagostomiasis / Q000276:immunology / Q000469:parasitology / Q000662:veterinary*; D009815:Oesophagostomum / Q000254:growth & development* / Q000276:immunology; D019887:Peanut Agglutinin / Q000737:chemistry / Q000276:immunology; D037121:Plant Lectins; D012756:Sheep; D030262:Soybean Proteins; D013552:Swine; D013553:Swine Diseases / Q000276:immunology / Q000469:parasitology*; D014909:Wheat Germ Agglutinins / Q000737:chemistry / Q000276:immunology; D010835:Phytohemagglutinins
D000871:Anthelmintics; D000909:Antibodies, Helminth; D000947:Antigens, Helminth; D000954:Antigens, Surface; D003208:Concanavalin A; D000939:Epitopes; D037102:Lectins; D007978:Levamisole; D019887:Peanut Agglutinin; D037121:Plant Lectins; D030262:Soybean Proteins; D014909:Wheat Germ Agglutinins; C017707:Ricinus communis agglutinin-1; C036554:dolichos biflorus agglutinin; C028824:soybean lectin; D010835:Phytohemagglutinins