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L isteria phage A 511, a model for the contractile tail machineries of SPO 1‐related bacteriophages
Author(s) -
Habann Matthias,
Leiman Petr G.,
Vandersteegen Katrien,
Van den Bossche An,
Lavigne Rob,
Shneider Mikhail M.,
Bielmann Regula,
Eugster Marcel R.,
Loessner Martin J.,
Klumpp Jochen
Publication year - 2014
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12539
Subject(s) - biology , subfamily , teichoic acid , siphoviridae , microbiology and biotechnology , virulence , bacteriophage , bacteria , bacterial cell structure , escherichia coli , genetics , peptidoglycan , gene
Summary Recognition of the bacterial host and attachment to its surface are two critical steps in phage infection. Here we report the identification of Gp 108 as the host receptor‐binding protein of the broad host‐range, virulent L isteria phage A 511. The ligands for Gp 108 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 A 511 baseplate in which Gp 108 forms emanating short tail fibres. Data obtained for related phages, such as S taphylococcus phages ISP and T wort, demonstrate the evolutionary conservation of baseplate components and receptor‐binding proteins within the S pounavirinae subfamily, and contractile tail machineries in general. Our data reveal key elements in the infection process of large phages infecting G ram‐positive bacteria and generate insights into the complex adsorption process of phage A 511 to its bacterial host.