Inhibition of Escherichia coli heat-labile enterotoxin by neoglycoprotein and anti-lectin antibodies which mimic GM1 receptor |
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| Authors: | Menezes Caroline A Amianti Jackeline Harayama Hebert S Koga Paula C M Trabulsi Luiz R Piazza Roxane M F |
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| Affiliation: | 1. Korea University Business School, Korea University, Anam-Dong, Seongbuk-Gu, Seoul 136-701, Republic of Korea;2. School of Graduate Professional Studies, The Pennsylvania State University, 30 East Swedesford Road, Malvern, PA 19355-1443, United States;1. International Business School, Shaanxi Normal University, Shaanxi, China;2. Rural Education Action Project, Stanford University, CA, United States;3. Center for Experimental Economics of Education, Shaanxi Normal University, Shaanxi, China;4. Castilleja School, Palo Alto, CA, United States;5. School of Accountancy, The Chinese University of Hong Kong, China;6. School of Advanced Agricultural Sciences, China Center for Agricultural Policy, Peking University, Beijing, China;1. Department of Vascular Surgery, Peking Union Medical College Hospital, Chinese Academy of Medical Science, and Peking Union Medical College, Beijing, China;2. R&D Center of Beijing Northland Biotech. Co., Ltd., Beijing, China |
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| Abstract: | ![]()
Escherichia coli producing heat-labile enterotoxin is responsible for numerous cases of diarrhea worldwide, leading to considerable morbidity and mortality. The B subunits of this toxin are responsible for the binding to the receptor, the complex ganglioside GM1 which has galactose as its terminal sugar. In this study we showed that analogs of galactose (gal) and N-acetylgalactosamine (GalNAc) interfere with the binding of heat-labile toxin to GM1. Antibodies to lectins which mimic sugar structures and neoglycoprotein were employed. These compounds were able to inhibit heat-labile toxin activity efficiently in Vero cells: 37 microg of IgG-enriched fraction from an antiserum inhibited up to 70% of this activity, and 50% of the binding of heat-labile toxin to GM1. Neoglycoprotein was more efficient than antibodies, since 2.5 microg of this ligand completely abolished the activity of heat-labile toxin on Vero cells. These data suggest that these molecules could be developed for prophylaxis and diagnosis of diarrhea caused by heat-labile toxin. |
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| Keywords: | GM1 receptor Heat-labile enterotoxin Neoglycoprotein Anti-lectin antibody Escherichia coli |
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