Characterization of the Attachment of Three New Coliphages onto the Ferrichrome Transporter FhuA.
Humans
Escherichia coli Proteins
/ chemistry
Bacterial Proteins
/ metabolism
Ferrichrome
/ metabolism
Bacterial Outer Membrane Proteins
/ metabolism
Lipopolysaccharides
/ metabolism
Receptors, Virus
/ metabolism
Membrane Transport Proteins
/ metabolism
Coliphages
/ genetics
Escherichia coli
/ genetics
Bacteriophages
/ genetics
FhuA
coliphage
phage attachment
phage evolution
Journal
Journal of virology
ISSN: 1098-5514
Titre abrégé: J Virol
Pays: United States
ID NLM: 0113724
Informations de publication
Date de publication:
27 07 2023
27 07 2023
Historique:
medline:
28
7
2023
pubmed:
13
6
2023
entrez:
13
6
2023
Statut:
ppublish
Résumé
Receptor-binding proteins (RBPs) allow phages to dock onto their host and initiate infection through the recognition of proteinaceous or saccharidic receptors located on the cell surface. FhuA is the ferrichrome hydroxamate transporter in Escherichia coli and serves as a receptor for the well-characterized phages T1, T5, and phi80. To further characterize how other FhuA-dependent phages attach to FhuA, we isolated and published the genomes of three new FhuA-dependent coliphages: JLBYU37, JLBYU41, and JLBYU60. We identified the egions of FhuA involved in phage attachment by testing the effect of mutant
Identifiants
pubmed: 37310294
doi: 10.1128/jvi.00667-23
pmc: PMC10373560
doi:
Substances chimiques
Escherichia coli Proteins
0
Bacterial Proteins
0
Ferrichrome
15630-64-5
Bacterial Outer Membrane Proteins
0
Lipopolysaccharides
0
Receptors, Virus
0
Membrane Transport Proteins
0
FhuA protein, E coli
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0066723Déclaration de conflit d'intérêts
The authors declare no conflict of interest.
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