Lectins and the radioallergosorbent test.
An investigation into the possible role of lectin binding of IgE in RAST of legume and wheat extracts is reported. Lectins from pea, broad bean, lentil, jack bean, soybean, peanut, and wheat germ were coupled to RAST discs. The discs were pretreated with lectin-specific sugars in an attempt to inhibit RAST with sera from 11 sensitive patients. In all cases, RAST was almost unaffected by the inhibitory sugars, indicating that nonimmune binding of IgE by lectins in legume or wheat RAST was not significant when RAST was carried out with allergens bound to the usual paper discs. IgE contains binding sites for all the lectins examined, and five of the sera had high total IgE greater than 300 IU/ml. It is suggested that competition by IgG and other serum glycoproteins may explain the lack of effect by the added sugars. All sera contained endogenous glucose at a level of about 3 mmol/L that may have accounted for some self-inhibition of the lectin binding by pea, broad bean, lentil, and jack bean lectins. There was, however, significant immune binding of some of the lectins by specific IgE, and it is concluded that these lectins may be important in expression of IgE-mediated allergic responses.
Barnett
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Commonwealth Scientific and Industrial Research Organization, Division of Food Research, North Ryde, Australia.
Howden
M E
ME
D010367:Arachis; D001786:Blood Glucose / Q000276:immunology; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology; D037102:Lectins / Q000276:immunology*; D037121:Plant Lectins; D011852:Radioallergosorbent Test; D011863:Radioimmunoassay; D014909:Wheat Germ Agglutinins / Q000276:immunology
D001786:Blood Glucose; D007074:Immunoglobulin G; D037102:Lectins; D037121:Plant Lectins; D014909:Wheat Germ Agglutinins