Glycosylation of bacterial and archaeal flagellins

DOIResolve DOI:
AuthorSearch for: ; Search for: ; Search for:
EditorSearch for: Holst, Otto; Search for: Brennan, Patrick J.; Search for: von Itzstein, Mark
TypeBook Chapter
Book titleMicrobial Glycobiology : Structures, Relevance and Applications
Pages129146; # of pages: 18
SubjectBacterial flagellin; Archael flagellin; Protein glycosylation; O-Linked glycan; N-Linked glycan
AbstractThe 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.
Publication date
AffiliationNational Research Council Canada; NRC Institute for Biological Sciences; NRC Institute for Marine Biosciences
Peer reviewedNo
NRC number42802
NPARC number21268318
Export citationExport as RIS
Report a correctionReport a correction
Record identifier6e6b9ec7-560d-4e46-8874-7380fab26822
Record created2013-06-19
Record modified2016-05-09
Bookmark and share
  • Share this page with Facebook (Opens in a new window)
  • Share this page with Twitter (Opens in a new window)
  • Share this page with Google+ (Opens in a new window)
  • Share this page with Delicious (Opens in a new window)
Date modified: