En route to photoaffinity labeling of the bacterial lectin FimH
Mannose-specific adhesion of Escherichia coli bacteria to cell surfaces, the cause of various infections, is mediated by a fimbrial lectin, called FimH. X-ray studies have revealed a carbohydrate recognition domain (CRD) on FimH that can complex α-D-mannosides. However, as the precise nature of the...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Beilstein-Institut
2010-08-01
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| Series: | Beilstein Journal of Organic Chemistry |
| Subjects: | |
| Online Access: | https://doi.org/10.3762/bjoc.6.91 |
| _version_ | 1818913518982791168 |
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| author | Thisbe K. Lindhorst Michaela Märten Andreas Fuchs Stefan D. Knight |
| author_facet | Thisbe K. Lindhorst Michaela Märten Andreas Fuchs Stefan D. Knight |
| author_sort | Thisbe K. Lindhorst |
| collection | DOAJ |
| description | Mannose-specific adhesion of Escherichia coli bacteria to cell surfaces, the cause of various infections, is mediated by a fimbrial lectin, called FimH. X-ray studies have revealed a carbohydrate recognition domain (CRD) on FimH that can complex α-D-mannosides. However, as the precise nature of the ligand–receptor interactions in mannose-specific adhesion is not yet fully understood, it is of interest to identify carbohydrate recognition domains on the fimbrial lectin also in solution. Photoaffinity labeling serves as an appropriate methodology in this endeavour and hence biotin-labeled photoactive mannosides were designed and synthesized for photoaffinity labeling of FimH. So far, the photo-crosslinking properties of the new photoactive mannosides could be detailed with the peptide angiotensin II and labeling of FimH was shown both by MS/MS studies and by affino dot–blot analysis. |
| first_indexed | 2024-12-19T23:31:46Z |
| format | Article |
| id | doaj.art-2a80bfb54ff2403080a2547d1d06c86f |
| institution | Directory Open Access Journal |
| issn | 1860-5397 |
| language | English |
| last_indexed | 2024-12-19T23:31:46Z |
| publishDate | 2010-08-01 |
| publisher | Beilstein-Institut |
| record_format | Article |
| series | Beilstein Journal of Organic Chemistry |
| spelling | doaj.art-2a80bfb54ff2403080a2547d1d06c86f2022-12-21T20:01:42ZengBeilstein-InstitutBeilstein Journal of Organic Chemistry1860-53972010-08-016181082210.3762/bjoc.6.911860-5397-6-91En route to photoaffinity labeling of the bacterial lectin FimHThisbe K. Lindhorst0Michaela Märten1Andreas Fuchs2Stefan D. Knight3Christiana Albertina University of Kiel, Otto Diels Institute of Organic Chemistry, Otto-Hahn-Platz 4, D-24098 Kiel, Germany, Fax: +49 431 8807410Christiana Albertina University of Kiel, Otto Diels Institute of Organic Chemistry, Otto-Hahn-Platz 4, D-24098 Kiel, Germany, Fax: +49 431 8807410Christiana Albertina University of Kiel, Otto Diels Institute of Organic Chemistry, Otto-Hahn-Platz 4, D-24098 Kiel, Germany, Fax: +49 431 8807410Swedish University of Agricultural Sciences, Department of Molecular Biology, Uppsala Biomedical Center, SE-75124 Uppsala, SwedenMannose-specific adhesion of Escherichia coli bacteria to cell surfaces, the cause of various infections, is mediated by a fimbrial lectin, called FimH. X-ray studies have revealed a carbohydrate recognition domain (CRD) on FimH that can complex α-D-mannosides. However, as the precise nature of the ligand–receptor interactions in mannose-specific adhesion is not yet fully understood, it is of interest to identify carbohydrate recognition domains on the fimbrial lectin also in solution. Photoaffinity labeling serves as an appropriate methodology in this endeavour and hence biotin-labeled photoactive mannosides were designed and synthesized for photoaffinity labeling of FimH. So far, the photo-crosslinking properties of the new photoactive mannosides could be detailed with the peptide angiotensin II and labeling of FimH was shown both by MS/MS studies and by affino dot–blot analysis.https://doi.org/10.3762/bjoc.6.91diazirinesFimHlectinsMS/MS analysisphotoactive mannoside ligandsphotoaffinity labeling |
| spellingShingle | Thisbe K. Lindhorst Michaela Märten Andreas Fuchs Stefan D. Knight En route to photoaffinity labeling of the bacterial lectin FimH Beilstein Journal of Organic Chemistry diazirines FimH lectins MS/MS analysis photoactive mannoside ligands photoaffinity labeling |
| title | En route to photoaffinity labeling of the bacterial lectin FimH |
| title_full | En route to photoaffinity labeling of the bacterial lectin FimH |
| title_fullStr | En route to photoaffinity labeling of the bacterial lectin FimH |
| title_full_unstemmed | En route to photoaffinity labeling of the bacterial lectin FimH |
| title_short | En route to photoaffinity labeling of the bacterial lectin FimH |
| title_sort | en route to photoaffinity labeling of the bacterial lectin fimh |
| topic | diazirines FimH lectins MS/MS analysis photoactive mannoside ligands photoaffinity labeling |
| url | https://doi.org/10.3762/bjoc.6.91 |
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