ArticleMolecular and cellular biochemistry1999
Interaction of cholera toxin and Escherichia coli heat-labile enterotoxin with glycoconjugates from rabbit intestinal brush border membranes: relationship with ABH blood group determinants.
Article in Molecular and cellular biochemistry, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- Fucosylation of glycoproteins and glycolipids: opposing roles in cholera intoxication.Nature chemical biology · 2025Article
- Fucosylated glycoproteins and fucosylated glycolipids play opposing roles in cholera intoxication.bioRxiv : the preprint server for biology · 2023Article
- Galectin-9 recognizes and exhibits antimicrobial activity toward microbes expressing blood group-like antigens.The Journal of biological chemistry · 2022Article
- Crystal structures of cholera toxin in complex with fucosylated receptors point to importance of secondary binding site.Scientific reports · 2019Article
- GM1 ganglioside-independent intoxication by Cholera toxin.PLoS pathogens · 2018Article
- High-Resolution Crystal Structures Elucidate the Molecular Basis of Cholera Blood Group Dependence.PLoS pathogens · 2016Article
- Blood Groups in Infection and Host Susceptibility.Clinical microbiology reviews · 2015Review
- Preparation of biocompatible heat-labile enterotoxin subunit B-bovine serum albumin nanoparticles for improving tumor-targeted drug delivery via heat-labile enterotoxin subunit B mediation.International journal of nanomedicine · 2014Article
- Towards a structural basis for the relationship between blood group and the severity of El Tor cholera.Angewandte Chemie (International ed. in English) · 2012Article
- Heat-labile enterotoxin: beyond G(m1) binding.Toxins · 2010Review
- No direct binding of the heat-labile enterotoxin of Escherichia coli to E. coli lipopolysaccharides.Glycoconjugate journal · 2010Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The capacity of cholera toxin (CT) and type I heat-labile enterotoxin produced by Escherichia coli isolated from human intestine (LTh) to interact with glycoconjugates bearing ABH blood group determinants from rabbit intestinal brush border membranes (BBM) was studied. On the basis of the type of intestinal compounds related to the human ABH blood group antigens, rabbits were classified as AB or H. Toxin binding to the intestinal glycolipids and glycoproteins depends on the blood group determinant borne by the glycoconjugate and on the analyzed toxin. LTh was capable of interacting preferentially with several blood group A- and B-active BBM glycolipids compared to those isolated from animals lacking these antigens (H rabbits). Also, LTh preferably bound to several BBM glycoproteins from AB rabbit intestines compared to those from H ones. One of these glycoproteins, the sucrase-isomaltase complex (EC 3.2.1.48-10) isolated from AB and H rabbits showed the same differential LTh binding. Conversely, CT practically did not recognize either blood group A-, B-, or H-active glycolipids and glycoproteins. These results may be relevant for carrying out in vivo experiments in rabbits in order to disclose the role of ABH active-glycoconjugates in the secretory response induced by LTh in rabbit intestine.
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