Usage of Aplysia lectin interactions with T antigen and poly-N-acetyllactosamine for screening of E. coli strains which bear glycoforms cross-reacting with cancer-associated antigens.
Aplysia gonad lectin (AGL), which strongly agglutinates cancer cells, was found, in the present study, to bind to erythrocyte T antigen, in addition to its affinity to Ii system antigens. These antigens were reported to be overexpressed and to contribute to tumor progression and invasion. In healthy human sera, there are antibodies against them, stimulated by the normal intestinal microflora, which bear similar glycoforms. Since the levels of these antibodies were reported to be lower in most cancer patients' sera, we have examined the applicability of AGL to isolation of enteric commensal Escherichia coli strains which bear glycoforms cross-reacting with the cancer-associated antigens. Among 30 E. coli isolates examined, two were agglutinated by AGL. One of them was also agglutinated by certain related galactophilic lectins, which bind to the T and Tn antigens. The agglutination of the two bacteria by healthy human sera, as a group, was stronger than that displayed by the cancer patients' sera. These results indicate that AGL might be useful for identification of the desired bacteria, which could potentially serve for cancer diagnosis and therapy.
Gilboa-Garber
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Faculty of Life Sciences, Bar-Ilan University, 52900, Ramat Gan, Israel. garben@mail.biu.ac.il
Sudakevitz
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D
D000372:Agglutination Tests; D000951:Antigens, Neoplasm / Q000235:genetics / Q000276:immunology*; D000957:Antigens, Viral, Tumor / Q000276:immunology*; D004926:Escherichia coli / Q000235:genetics / Q000302:isolation & purification*; D037161:Galectins; D006388:Hemagglutinins; D006801:Humans; D011134:Polysaccharides / Q000276:immunology*; D011485:Protein Binding; D013696:Temperature
D000951:Antigens, Neoplasm; D000957:Antigens, Viral, Tumor; D037161:Galectins; D006388:Hemagglutinins; D011134:Polysaccharides; C037199:poly-N-acetyllactosamine