A glycosylated component with affinity for wheat germ agglutinin (specific binding to n-acetyl-D-glucosamine monomers and oligomers) and weak affinity for poke weed mitogen (specific binding to n-acetyl-D-glucosamine oligomers) was detected temporally on the surface of Ascaris suum larvae developing in vitro and on in vivo-derived larvae. The component was identified on the surface of in vitro-derived late second stage larvae, on all late third stage larvae (derived from pig lung), and all fourth stage larvae (obtained from pig intestines and from in vitro culture) of A. suum. None of the newly hatched first molt, L2, or early L3 bound any of the lectins tested. The component exhibited no affinity for concanavalin A (specific binding to alpha-D-mannosyl and alpha-D-glucosyl residues) or Dolichos biflorus lectin (specific binding to n-acetyl-D-galactosamine). A component with similar lectin binding specificities had previously been found on the cuticle of adult A. suum.
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http://dx.doi.org/10.1016/0014-4894(91)90110-i | DOI Listing |
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