Analysis of the role of pglI in pilin glycosylation of Neisseria meningitidis


Autoria(s): Warren, Matthew J.; Roddam, Louise F.; Power, Peter M.; Terry, Tamsin D.; Jennings, Michael P.
Data(s)

01/05/2004

Resumo

Pilin is the major subunit of the essential virulence factor pili and is glycosylated at Ser63. In this study we investigated the gene pglI to determine whether it is involved in the biosynthesis of the pilin-linked glycan of Neisseria meningitidis strain C311#3. A N. meningitidis C311#3pglI mutant resulted in a change of apparent molecular weight in SDS-PAGE and altered binding of antisera, consistent with a role in the biosynthesis of the pilin-linked glycan. These data, in conjunction with homology with well-characterised acyltransferases suggests a specific role for pglI in the biosynthesis of the basal 2,4-diacetamido-2,4,6-trideoxyhexose residue of the pilin-linked glycan. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Microbiological Societies.

Identificador

http://espace.library.uq.edu.au/view/UQ:70992

Idioma(s)

eng

Publicador

Elsevier Science Bv

Palavras-Chave #Immunology #Infectious Diseases #Microbiology #Complete Genome Sequence #Typhimurium O-antigen #Phase-variable Genes #Molecular Characterization #Pathogenic Neisseria #Meningococcal Pilin #Endothelial-cells #Serogroup-b #Strain Mc58 #Protein #C1 #270300 Microbiology #780105 Biological sciences
Tipo

Journal Article