Ultrastructural colocalization of phosphorylcholine and a phosphorylcholine-associated epitope in first-stage larvae of Trichinella spiralis.
Although the presence of phosphorylcholine (PC) in Trichinella is well established, the structures of the TSL-4 antigens that bear this epitope are unknown. A subset of TSL-4 antigens (TSL-8 antigens) has been reported to be absent from the surface of first-stage T. spiralis larvae. We report experiments with a monoclonal antibody (mAb US2) developed in mice with a relative inability to produce antibodies to PC. In immunoblotting, mAb US2 and anti-PC mAb (BH8) showed apparently identical binding patterns. In addition, we used an immunogold double-labeling technique to study the anatomical distribution of the epitopes recognized by these mAbs; the results obtained indicate close colocalization of epitopes for BH8 and US2 in tissues of T. spiralis first-stage larvae. On the basis of these results, we suggest that US2 probably binds to all T. spiralis TSL-4 antigens, including TSL-8 antigens. We also clarify some conflicting previous reports on the distribution of PC immunoreactivity in first-stage larvae of T. spiralis.
Hernández
S
S
Departamento de Parasitología, Facultad d Universidad de Córdoba, Spain.
Romarís
F
F
Acosta
I
I
Gutiérrez
P N
PN
Ubeira
F M
FM
D000818:Animals; D000909:Antibodies, Helminth / Q000276:immunology*; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000947:Antigens, Helminth / Q000032:analysis* / Q000276:immunology; D000939:Epitopes / Q000032:analysis* / Q000276:immunology; D005260:Female; D008297:Male; D051379:Mice; D008807:Mice, Inbred BALB C; D008808:Mice, Inbred CBA; D010767:Phosphorylcholine / Q000032:analysis* / Q000276:immunology; D017160:Trichinella spiralis / Q000276:immunology* / Q000648:ultrastructure; D014235:Trichinellosis / Q000276:immunology* / Q000469:parasitology
D000909:Antibodies, Helminth; D000911:Antibodies, Monoclonal; D000947:Antigens, Helminth; D000939:Epitopes; D010767:Phosphorylcholine