| DOI | Resolve DOI: https://doi.org/10.1016/B978-0-12-374546-0.00008-0 |
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| Author | Search for: Logan, Susan M.1; Search for: Schoenhofen, Ian C.1; Search for: Soo, Evelyn C.2 |
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| Editor | Search for: Holst, Otto; Search for: Brennan, Patrick J.; Search for: von Itzstein, Mark |
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| Affiliation | - National Research Council of Canada. NRC Institute for Biological Sciences
- National Research Council of Canada. NRC Institute for Marine Biosciences
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| Format | Text, Book Chapter |
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| Subject | bacterial flagellin; archael flagellin; protein glycosylation; O-linked glycan; N-linked glycan |
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| Abstract | The biosynthesis, assembly and regulation of the flagellar organelle has been extensively described over many decades and has focused primarily on the peritrichous flagella of Escherichia coli and Salmonella enterica. More recently, the characterization of flagellar systems from other bacterial and archaeal species has revealed distinct differences in flagellar composition and mode of assembly. Glycosylation of the flagellin structural protein has been identified as an important feature of numerous systems and has been shown to play an integral role in flagellar assembly or in virulence of a number of pathogenic species. This chapter focuses on the structural diversity of flagellar glycans, methods for characterization of flagellin glycoproteins and novel glycan biosynthetic pathways. the relevance of the glycosylation process to assembly as well as other novel biological roles is discussed. |
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| Publication date | 2009-08-31 |
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| Publisher | Elsevier |
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| In | |
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| Language | English |
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| NRC number | NRCC 42802 |
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| NPARC number | 21268318 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 6e6b9ec7-560d-4e46-8874-7380fab26822 |
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| Record created | 2013-06-19 |
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| Record modified | 2020-06-17 |
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