A New Sugar for an Old Phage: a c-di-GMP-Dependent Polysaccharide Pathway Sensitizes
DgcJ
DgcQ
ECA
Escherichia coli
ManNAc
N4 phage
NfrA
NfrB
PdeL
WecB
allosteric activation
arginine
c-di-GMP
dCache domain
exopolysaccharide
glycosyltransferase
phage infection
phage receptor
Journal
mBio
ISSN: 2150-7511
Titre abrégé: mBio
Pays: United States
ID NLM: 101519231
Informations de publication
Date de publication:
21 12 2021
21 12 2021
Historique:
pubmed:
15
12
2021
medline:
23
2
2022
entrez:
14
12
2021
Statut:
ppublish
Résumé
Bacteriophages are ubiquitous parasites of bacteria and major drivers of bacterial ecology and evolution. Despite an ever-growing interest in their biotechnological and therapeutic applications, detailed knowledge of the molecular mechanisms underlying phage-host interactions remains scarce. Here, we show that bacteriophage N4 exploits a novel surface glycan (NGR) as a receptor to infect its host Escherichia coli. We demonstrate that this process is regulated by the second messenger c-di-GMP and that N4 infection is specifically stimulated by the diguanylate cyclase DgcJ, while the phosphodiesterase PdeL effectively protects E. coli from N4-mediated killing. PdeL-mediated protection requires its catalytic activity to reduce c-di-GMP and includes a secondary role as a transcriptional repressor. We demonstrate that PdeL binds to and represses the promoter of the
Identifiants
pubmed: 34903045
doi: 10.1128/mbio.03246-21
pmc: PMC8669472
doi:
Substances chimiques
Escherichia coli Proteins
0
Glucans
0
Polysaccharides, Bacterial
0
bis(3',5')-cyclic diguanylic acid
61093-23-0
Nucleotidyltransferases
EC 2.7.7.-
yeaJ protein, E coli
EC 4.6.-
Carbohydrate Epimerases
EC 5.1.3.-
wecB protein, E coli
EC 5.1.3.14
Cyclic GMP
H2D2X058MU
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0324621Références
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