Three distinct glycosylation pathways are involved in the decoration of
bacteriophage
cell wall
flippase
genomics
glycobiology
glycopolymer
glycosylation
glycosyltransferase
lactic acid bacteria
lipoteichoic acid (LTA)
peptidoglycan
phage receptor
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
17 04 2020
17 04 2020
Historique:
received:
28
08
2019
revised:
10
03
2020
pubmed:
15
3
2020
medline:
18
12
2020
entrez:
15
3
2020
Statut:
ppublish
Résumé
Extracytoplasmic sugar decoration of glycopolymer components of the bacterial cell wall contributes to their structural diversity. Typically, the molecular mechanism that underpins such a decoration process involves a three-component glycosylation system (TGS) represented by an undecaprenyl-phosphate (Und-P) sugar-activating glycosyltransferase (Und-P GT), a flippase, and a polytopic glycosyltransferase (PolM GT) dedicated to attaching sugar residues to a specific glycopolymer. Here, using bioinformatic analyses, CRISPR-assisted recombineering, structural analysis of cell wall-associated polysaccharides (CWPS) through MALDI-TOF MS and methylation analysis, we report on three such systems in the bacterium
Identifiants
pubmed: 32169901
pii: S0021-9258(17)48567-X
doi: 10.1074/jbc.RA119.010844
pmc: PMC7170526
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Deoxy Sugars
0
Lipopolysaccharides
0
Mannans
0
Teichoic Acids
0
rhamnan
111018-90-7
lipoteichoic acid
56411-57-5
Galactose
X2RN3Q8DNE
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
5519-5532Informations de copyright
© 2020 Theodorou et al.
Déclaration de conflit d'intérêts
The authors declare that they have no conflicts of interest with the contents of this article.
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