Heterogeneity and immunogenicity of the Trichinella TSL‐1 antigen gp53

• Published in: Parasite immunology Vol. 25; no. 6; pp. 297 - 305
• Main Authors: Romarís, F., Dea‐Ayuela, M. A., Bolás, F., Martínez‐Fernández, A. R., Sanmartín, M. L., Ubeira, F. M.
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Science Ltd 01.06.2003
• Subjects: Animals; Antibodies, Helminth - blood; Antigenic Variation - immunology; Antigens, Helminth - immunology; Blotting, Western; Enzyme-Linked Immunosorbent Assay; Epitopes - immunology; Escherichia coli - genetics; Female; glycoprotein gp53; Glycoproteins - immunology; gp53; Haemonchus contortus; Helminth Proteins - immunology; Hexoses - immunology; immune response; Mice; Mice, Inbred BALB C; monoclonal antibodies; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Species Specificity; species‐specific epitopes; Trichinella; Trichinella - genetics; Trichinella - immunology; Trichinella britovi; Trichinella murrelli; TSL-1 antigen; US4; US5; US9
• ISSN: 0141-9838; 1365-3024
• DOI: 10.1046/j.1365-3024.2003.00635.x

SUMMARY This study investigates the heterogeneity and immunogenicity of the Trichinella TSL‐1 antigen gp53. Western blotting analysis of several Trichinella isolates with the gp53‐specific monoclonal antibodies (mAbs) US5 and US9, produced in Btkxid mice, revealed that gp53 from the species T. britovi, T. murrelli and genotype T8 had higher MW (60 kDa) than gp53 from T. spiralis, T. nelsoni and genotype T6 (53 kDa) and from T. nativa (55 kDa). mAb US5 reacted only with gp53 from T. spiralis. Experiments including immunoassays of gp53 binding by sera from T. spiralis‐infected mice, in the presence of different potential inhibitors (recombinant gp53, US5, T. britovi‐crude larval extract (CLE), and CLE N‐ and O‐glycans), indicate (i) that gp53 from T. spiralis bears specific epitopes that induce antibody formation during infection; (ii) that the protein epitopes of gp53 are much more important (76 or 68% of total antibody reactivity in BALB/c and Swiss CD‐1 mice, respectively) than the corresponding glycan epitopes including tyvelose (11 or 32% of total reactivity) for the induction of anti‐gp53 circulating antibodies; and (iii) that the species‐specific epitopes present on gp53 are differentially recognized in different mouse strains. Whereas in BALB/c mice US5‐ and non‐US5‐recognized species‐specific epitopes on gp53 bind about 84% of circulating antibodies on day 80 post‐infection, this percentage was only 38% in Swiss CD‐1 mice. These data on the antigenicity of gp53 contrast with data for Trichinella CLE antigens, in that most circulating antibodies reactive with CLE antigens recognized tyvelose‐containing epitopes (57% and 58% of circulating antibodies in BALB/c and Swiss CD‐1 mice, respectively). Together these results demonstrate that gp53 is recognized during infection but is antigenically different from other Trichinella TSL‐1 antigens.