The Bacterial Lectin FimH, a Target for Drug Discovery - Carbohydrate Inhibitors of Type 1 Fimbriae-Mediated Bacterial Adhesion
Adhesion is a prerequisite for bacteria to colonize cell surfaces. To accomplish cellular adhesion, many bacteria use carbohydrate‐specific lectins, which are expressed as part of capillary protein appendages expanding from their surface, called fimbriae or pili. For bacteria, colonization of cell s...
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Published in | European Journal of Organic Chemistry Vol. 2011; no. 20-21; pp. 3583 - 3609 |
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Main Authors | , |
Format | Book Review Journal Article |
Language | English |
Published |
Weinheim
WILEY-VCH Verlag
01.07.2011
WILEY‐VCH Verlag |
Subjects | |
Online Access | Get full text |
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Summary: | Adhesion is a prerequisite for bacteria to colonize cell surfaces. To accomplish cellular adhesion, many bacteria use carbohydrate‐specific lectins, which are expressed as part of capillary protein appendages expanding from their surface, called fimbriae or pili. For bacteria, colonization of cell surfaces offers advantageous conditions to persist and multiply. For the host, however, bacterial colonization can be affiliated with severe health problems such as inflammation. Therefore, to combat bacterial adhesion and inflammatory diseases, investigation of the molecular and biophysical details of the relevant lectin–carbohydrate interactions is important. Understanding molecular carbohydrate recognition can lead to the development of high‐affinity inhibitors of bacterial lectins. That way, interfering with the bacterial attachment to surfaces proves the vision of an antiadhesion therapy, among others, against uropathogenic E. coli (UPEC). One of the most important and best investigated bacterial lectins is the mannose‐specific protein FimH, which is expressed on the tips of type 1 fimbriae. During the last 30 years, many natural as well as synthetic mannosidic ligands of FimH have been designed and tested for their inhibitory potencies. We report key results and comment on key problems and perspectives of this research.
FimH is a well‐investigated lectin, which is used by bacteria to adhere to glycosylated surfaces, such as cells. This microreview gives an overview of the development of FimH ligands, structural properties of the lectin and in vitro testing methods applied in the screen for putative inhibitors of type 1 fimbriae‐mediated bacterial adhesion. |
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Bibliography: | Deutsche Forschungsgemeinschaft (DFG) Christiana Albertina University ark:/67375/WNG-RGLK1X7F-F ArticleID:EJOC201100407 istex:BF3A1727E61F817F6948B4D2F085605126BA1131 |
ISSN: | 1434-193X 1099-0690 |
DOI: | 10.1002/ejoc.201100407 |