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The occurrence of antibodies to hidden and exposed determinants of surface antigens of Trichinella spiralis

Published online by Cambridge University Press:  06 April 2009

Guadalupe Ortega-Pierres ,
Ann Chayen ,
N. W. T. Clark  and
R. M. E. Parkhouse
Guadalupe Ortega-Pierres
Affiliation:
Division of Immunology, National Institute for Medical Research, Mill Hill, London NW7 1AA
Ann Chayen
Affiliation:
Division of Immunology, National Institute for Medical Research, Mill Hill, London NW7 1AA
N. W. T. Clark
Affiliation:
Division of Immunology, National Institute for Medical Research, Mill Hill, London NW7 1AA
R. M. E. Parkhouse
Affiliation:
Division of Immunology, National Institute for Medical Research, Mill Hill, London NW7 1AA
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Summary

Mice were infected per os with Trichinella spiralis and their lymphocytes were removed and fused with mouse myeloma cell line P3 × 63Ag8653P3 for the selection of monoclonal antibodies to biochemically defined, stage-specific surface antigens of 3 parasite developmental stages: muscle larvae, adults and newborn larvae. Two separate antibodies against a defined single surface antigen of each stage were isolated. In each separate case the pair of monoclonal antibodies precipitated the same component from detergent-solubilized surface antigen preparations, but only one was able to bind to the surface of the living worm. The other must therefore be directed against an antigenic epitope which is obscured in the intact worm surface. The latter type of antibody is unlikely to be involved in the initial phase of parasite rejection and hence is another example of a non-protective host antibody response. The stimulus for its synthesis may be release of surface antigen, which does occur in vitro. One surface antigen of the newborn larvae is only detected by antibody in the first 6 h after birth; thereafter its presence is obscured as other antigens appear. The major surface antigen of the infective larvae contains carbohydrate determinants which are not available at the parasite surface. In addition, it displays great molecular heterogeneity but all variants appear to be derived from a common polypeptide structure.

Type
Research Article
Information
Parasitology , Volume 88 , Issue 2 , April 1984 , pp. 359 - 369
Copyright
Copyright © Cambridge University Press 1984

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