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Tvichostrongylus colubriformis : analysis of monoclonal antibody and lectin binding to the larval cuticle
Author(s) -
MILNER A. R.,
MACK W. N.
Publication year - 1988
Publication title -
parasite immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.795
H-Index - 75
eISSN - 1365-3024
pISSN - 0141-9838
DOI - 10.1111/j.1365-3024.1988.tb00232.x
Subject(s) - biology , wheat germ agglutinin , parasite hosting , epitope , monoclonal antibody , lectin , excretory system , antibody , antigen , western blot , microbiology and biotechnology , cuticle (hair) , nematode , glycoprotein , biochemistry , immunology , anatomy , ecology , gene , world wide web , computer science
Summary A monoclonal antibody (VRI 86‐1) raised against third stage Trichostrongylus colubriformis preferentially bound to the excretory pore of living exsheathed larvae, with little or no binding to other sites on the parasite surface. A similar binding pattern was observed with fluorescein‐labelled wheat germ agglutinin (WGA), although the anterior end of the parasite was also stained. To gain information at the molecular level regarding the parasite components at these sites, the residues recognized by WGA (i.e. N ‐acetylglucosamine and N ‐acetylneuraminic acid) were radiolabelled on the surface of living larvae. After homogenization and detergent extraction of the larvae, Tour dominant bands and a number of minor bands were revealed by SDS‐PAGE and fluorography. None of these bands was specifically immunoprecipilated or recognized on a Western blot by VRI 86‐1, suggesting that the epitope recognized by this antibody either resides on a different molecule or is destroyed or changed during the radiolabelling procedures. These results provide further evidence that the nematodc cuticle is not uniform at the molecular level, and that the excretory pore contains molecules and antigens that may be unique to that site.