PMID:24673724

Citation	Habann, M, Leiman, PG, Vandersteegen, K, Van den Bossche, A, Lavigne, R, Shneider, MM, Bielmann, R, Eugster, MR, Loessner, MJ and Klumpp, J (2014) Listeria phage A511, a model for the contractile tail machineries of SPO1-related bacteriophages. Mol. Microbiol. 92:84-99
Abstract	Recognition of the bacterial host and attachment to its surface are two critical steps in phage infection. Here we report the identification of Gp108 as the host receptor-binding protein of the broad host-range, virulent Listeria phage A511. The ligands for Gp108 were found to be N-acetylglucosamine and rhamnose substituents of the wall teichoic acids of the bacterial cell wall. Transmission electron microscopy and immunogold-labelling allowed us to create a model of the A511 baseplate in which Gp108 forms emanating short tail fibres. Data obtained for related phages, such as Staphylococcus phages ISP and Twort, demonstrate the evolutionary conservation of baseplate components and receptor-binding proteins within the Spounavirinae subfamily, and contractile tail machineries in general. Our data reveal key elements in the infection process of large phages infecting Gram-positive bacteria and generate insights into the complex adsorption process of phage A511 to its bacterial host.
Links	PubMed Online version:10.1111/mmi.12539
Keywords	Bacterial Proteins/metabolism; Cell Wall/metabolism; Genome, Viral; Listeria/virology; Microscopy, Electron, Transmission; Myoviridae/classification; Myoviridae/physiology; Rhamnose/metabolism; Teichoic Acids/metabolism; Viral Proteins/metabolism
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
BPA51:Q37916		GO:0098027: virus tail, sheath	ECO:0000314:		C		The author's exposed Listeria Bacteriophage A511 baseplate to a-Gp proteins, purified antibodies for cross-linking (with Staphylococcus ISP), and immunogold labeling. The results were found by use of transmission electron micrograph. In Figure 7, TEM images depict the antibody cross-linking of A511 and ISP. Immunogold labelling is seen as well by black dots on the image. A contracted tail fiber was identified in the A511 tail through the identification of Gp108. In Figure 8, an immunogold label TEM shows the contracted tail of A511. In addition to antibody cross-linking and in silico prediction, a model of the A511 tail was generated and compared to the TEM image. The presumed location of gene products including tsh (tail sheath protein) are seen in the model.	complete CACAO 10875
BPA51:Q37916	part_of	GO:0098027: virus tail, sheath	ECO:0000314: direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
BPA51:A8ASU2		GO:0098024: virus tail, fiber	ECO:0000314: direct assay evidence used in manual assertion		C		Figure 7. Panel O, shows the gp108 tail fiber in electron microscopy, at the appropriate location for the function of a tail fiber. Specifically, the immunogold particles binding near the baseplate, which is where you would expect to see the tail fiber.	complete CACAO 11884
BPA51:A8ASU2		GO:0019062: virion attachment to host cell	ECO:0000314: direct assay evidence used in manual assertion		P		Figure 2 shows how the antibody of gp108 tail fiber protein inhibits adsorption of bacteriophage A511 to the WSLC 3009 host cell. The bars on the graphs above the label WSLC3009 + gp108 show a significant decrease in efficiency in plating and adorption. This indicates the antibody gp108's ability to block the binding of the A511 to the host cell.	complete CACAO 12013

References

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