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- W2060101911 abstract "Filamentous bacteriophages infecting gram-negative bacteria display tropism for a variety of pilus structures. However, the obligatory coreceptor of phage infection, postulated from genetic studies, has remained elusive. Here we identify the C-terminal domain of the periplasmic protein TolA as the coreceptor for infection of Escherichia coli by phage fd and the N-terminal domain of the phage minor coat protein g3p as its cognate ligand. The neighboring g3p domain binds the primary receptor of phage infection, the F pilus, and blocks TolA binding in its absence. Contact with the pilus releases this blockage during infection. Our findings support a sequential two-way docking mechanism for phage infection, analogous to infection pathways proposed for a range of eukaryotic viruses including herpes simplex, adenoviruses, and also lentiviruses like HIV-1." @default.
- W2060101911 created "2016-06-24" @default.
- W2060101911 creator A5012304923 @default.
- W2060101911 creator A5068463880 @default.
- W2060101911 date "1997-07-01" @default.
- W2060101911 modified "2023-10-16" @default.
- W2060101911 title "The C-Terminal Domain of TolA Is the Coreceptor for Filamentous Phage Infection of E. coli" @default.
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- W2060101911 doi "https://doi.org/10.1016/s0092-8674(00)80342-6" @default.
- W2060101911 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9244308" @default.
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