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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Taylor & Francis Group
2020
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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) |
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enterotoxigenic e. coli colonization factor cs30 microbial adhesion carbohydrate binding glycosphingolipid characterization sulfatide Infectious and parasitic diseases RC109-216 |
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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 |
work_keys_str_mv |
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1718425500188147712 |