Carbohydrate processing by bacterial pathogens: structural and functional analyses of glycoside hydrolases.

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dc.contributor.author Gregg, Katie Jean
dc.date.accessioned 2011-12-14T23:29:27Z
dc.date.available 2011-12-14T23:29:27Z
dc.date.copyright 2011 en_US
dc.date.issued 2011-12-14
dc.identifier.uri http://hdl.handle.net/1828/3726
dc.description.abstract Carbohydrates are important in a large number of cellular, physiological, and pathological processes. Carbohydrates often function as the human host’s first line of defence against pathogen invasion by coating surfaces of epithelial cells and as glycan-rich mucins which line the entrances to the body. Various pathogenic bacteria exploit their hosts by modifying their glycans through the production of carbohydrate-active enzymes. Two kinds of pathogenic bacteria that are notable for their production of carbohydrate-active enzymes are Streptococcus pneumoniae and Clostridium perfringens. Both S. pneumoniae and C. perfringens inhabit glycan-rich niches in the human body, the respiratory and gastrointestinal tracts, respectively. To properly colonize their human hosts both bacteria have developed an extensive repertoire of glycoside hydrolases (GHs) which are enzymes responsible for the breakdown of carbohydrates. These GHs have known or predicted specificities for human glycans, specifically those found in mucins. We chose C. perfringens and S. pneumoniae as model systems to study these enzymes due to their large complements of GHs, many of which are known virulence factors. The objectives are to probe the key features of the GHs from these two different kinds of bacteria that inhabit similar human niches and to study catalysis, modularity and overall enzyme structure. This work uses a multidisciplinary approach and provides molecular level insight into the S. pneumoniae and C. perfringens host-pathogen interaction. en_US
dc.language English eng
dc.language.iso en en_US
dc.subject Biochemistry en_US
dc.subject Structural Biology en_US
dc.title Carbohydrate processing by bacterial pathogens: structural and functional analyses of glycoside hydrolases. en_US
dc.type Thesis en_US
dc.contributor.supervisor Boraston, Alisdair Bennett
dc.degree.department Dept. of Biochemistry and Microbiology en_US
dc.degree.level Doctor of Philosophy Ph.D. en_US
dc.rights.temp Available to the World Wide Web en_US
dc.description.scholarlevel Graduate en_US

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