Chapter 3 : Sugar Recognition and Bacterial Attachment

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Many bacteria harbor adhesins at the tip of adhesive organelles called pili or fimbriae. This chapter discusses the contribution of structural biology to the understanding of the molecular basis of bacterial attachment to glycoprotein and glycolipid host receptors. The chaperone-usher pathway is involved in the biogenesis of more than 100 different pili structures in pathogenic gram-negative bacteria. Examples of pili and fimbriae that are assembled through the chaperone-usher pathway are type 1 pili, P pili, and G and F17 fimbriae. To date, the adhesive interactions between host and pathogenic bacteria of over 300 different species have been investigated. Bacteria have learned to exploit the fact that mammalian tissues have glycoproteins and glycolipds in their membranes by expressing lectins at the tips of their pili. Recently, the crystal structures of FimH, PapGII, GafD, and F17a-G have been determined and are providing a wealth of information on lectin-host receptor interactions. The crystal structures of FimH, PapGII, GafD, and F17a-G provide an opportunity for understanding the molecular details of host-pathogen interactions as well as the evolutionary relationships between the different adhesins. The detailed structural analysis of bacterial adhesins has demonstrated their central role in the host-pathogen interface during the infection process and has made them attractive targets for the development of new antimicrobial therapies. Differences in pilus structure, along with differences in the lectin-binding domains, allow the bacterium to orient their adhesin in order to effectively and efficiently bind to their receptors.

Citation: Smith C, Dodson K, Hultgren S, Waksman G. 2005. Sugar Recognition and Bacterial Attachment, p 37-48. In Waksman G, Caparon M, Hultgren S (ed), Structural Biology of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818395.ch3

Key Concept Ranking

Type 1 Pili
Bacterial Pathogenesis
Bacterial Proteins
Nuclear Magnetic Resonance Spectroscopy
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