Colonization factor CS30 from enterotoxigenic Escherichia coli binds to sulfatide in human and porcine small intestine

The ability to adhere via colonization factors to specific receptors located on the intestinal mucosa is a key virulence factor in enterotoxigenic Escherichia coli (ETEC) pathogenesis. Here, the potential glycosphingolipid receptors of the novel human ETEC colonization factor CS30 were examined by b...

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Autores principales: Astrid Von Mentzer, Dani Zalem, Zofia Chrienova, Susann Teneberg
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Publicado: Taylor & Francis Group 2020
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spelling oai:doaj.org-article:a428fc35df25481694a39ad273dced732021-11-17T14:21:58ZColonization factor CS30 from enterotoxigenic Escherichia coli binds to sulfatide in human and porcine small intestine2150-55942150-560810.1080/21505594.2020.1749497https://doaj.org/article/a428fc35df25481694a39ad273dced732020-12-01T00:00:00Zhttp://dx.doi.org/10.1080/21505594.2020.1749497https://doaj.org/toc/2150-5594https://doaj.org/toc/2150-5608The ability to adhere via colonization factors to specific receptors located on the intestinal mucosa is a key virulence factor in enterotoxigenic Escherichia coli (ETEC) pathogenesis. Here, the potential glycosphingolipid receptors of the novel human ETEC colonization factor CS30 were examined by binding of CS30-expressing bacteria to glycosphingolipids on thin-layer chromatograms. We thereby found a highly specific binding of CS30-expressing bacteria to a fast-migrating acid glycosphingolipid of human and porcine small intestine, while no binding was obtained with a mutant ETEC strain unable to express CS30 fimbriae. The CS30 binding glycosphingolipid from human small intestine was isolated and characterized by mass spectrometry as sulfatide (SO3-3Galβ1Cer). Comparative binding studies using sulfatides with different ceramide compositions gave a preferential binding of CS30 to sulfatide with d18:1-h24:0 ceramide. This ceramide species of sulfatide was also isolated from human small intestine and characterized by mass spectrometry and antibody binding. These studies implicate sulfatide as candidate receptor for mediating attachment of CS30-fimbriated ETEC to human and porcine small intestinal cells. Our findings may be a basis for designing receptor saccharide analogues for inhibition of the intestinal adhesion of CS30-expressing E. coli.Astrid Von MentzerDani ZalemZofia ChrienovaSusann TenebergTaylor & Francis Grouparticleenterotoxigenic e. colicolonization factor cs30microbial adhesioncarbohydrate bindingglycosphingolipid characterizationsulfatideInfectious and parasitic diseasesRC109-216ENVirulence, Vol 11, Iss 1, Pp 381-390 (2020)
institution DOAJ
collection DOAJ
language EN
topic enterotoxigenic e. coli
colonization factor cs30
microbial adhesion
carbohydrate binding
glycosphingolipid characterization
sulfatide
Infectious and parasitic diseases
RC109-216
spellingShingle enterotoxigenic e. coli
colonization factor cs30
microbial adhesion
carbohydrate binding
glycosphingolipid characterization
sulfatide
Infectious and parasitic diseases
RC109-216
Astrid Von Mentzer
Dani Zalem
Zofia Chrienova
Susann Teneberg
Colonization factor CS30 from enterotoxigenic Escherichia coli binds to sulfatide in human and porcine small intestine
description The ability to adhere via colonization factors to specific receptors located on the intestinal mucosa is a key virulence factor in enterotoxigenic Escherichia coli (ETEC) pathogenesis. Here, the potential glycosphingolipid receptors of the novel human ETEC colonization factor CS30 were examined by binding of CS30-expressing bacteria to glycosphingolipids on thin-layer chromatograms. We thereby found a highly specific binding of CS30-expressing bacteria to a fast-migrating acid glycosphingolipid of human and porcine small intestine, while no binding was obtained with a mutant ETEC strain unable to express CS30 fimbriae. The CS30 binding glycosphingolipid from human small intestine was isolated and characterized by mass spectrometry as sulfatide (SO3-3Galβ1Cer). Comparative binding studies using sulfatides with different ceramide compositions gave a preferential binding of CS30 to sulfatide with d18:1-h24:0 ceramide. This ceramide species of sulfatide was also isolated from human small intestine and characterized by mass spectrometry and antibody binding. These studies implicate sulfatide as candidate receptor for mediating attachment of CS30-fimbriated ETEC to human and porcine small intestinal cells. Our findings may be a basis for designing receptor saccharide analogues for inhibition of the intestinal adhesion of CS30-expressing E. coli.
format article
author Astrid Von Mentzer
Dani Zalem
Zofia Chrienova
Susann Teneberg
author_facet Astrid Von Mentzer
Dani Zalem
Zofia Chrienova
Susann Teneberg
author_sort Astrid Von Mentzer
title Colonization factor CS30 from enterotoxigenic Escherichia coli binds to sulfatide in human and porcine small intestine
title_short Colonization factor CS30 from enterotoxigenic Escherichia coli binds to sulfatide in human and porcine small intestine
title_full Colonization factor CS30 from enterotoxigenic Escherichia coli binds to sulfatide in human and porcine small intestine
title_fullStr Colonization factor CS30 from enterotoxigenic Escherichia coli binds to sulfatide in human and porcine small intestine
title_full_unstemmed Colonization factor CS30 from enterotoxigenic Escherichia coli binds to sulfatide in human and porcine small intestine
title_sort colonization factor cs30 from enterotoxigenic escherichia coli binds to sulfatide in human and porcine small intestine
publisher Taylor & Francis Group
publishDate 2020
url https://doaj.org/article/a428fc35df25481694a39ad273dced73
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AT zofiachrienova colonizationfactorcs30fromenterotoxigenicescherichiacolibindstosulfatideinhumanandporcinesmallintestine
AT susannteneberg colonizationfactorcs30fromenterotoxigenicescherichiacolibindstosulfatideinhumanandporcinesmallintestine
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