The phage tail tape measure protein, an inner membrane protein and a periplasmic chaperone play connected roles in the genome injection process of E. coli phage HK97.
Cumby, Nichole 1,2; Reimer, Kelly 1,2; Mengin-Lecreulx, Dominique 3; Davidson, Alan R. 1,4; Maxwell, Karen L. 2
[Article] Molecular Microbiology. 96(3):437-447, May 2015.

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Summary: Phages play critical roles in the spread of virulence factors and control of bacterial populations through their predation of bacteria. An essential step in the phage lifecycle is genome entry, where the infecting phage must productively interact with the components of the bacterial cell envelope in order to transmit its genome out of the viral particle and into the host cell cytoplasm. In this study, we characterize this process for the Escherichia coli phage HK97. We have discovered that HK97 genome injection requires the activities of the inner membrane glucose transporter protein, PtsG, and the periplasmic chaperone, FkpA. The requirements for PtsG and FkpA are determined by the sequence of the phage tape measure protein (TMP). We also identify a region of the TMP that mediates inhibition of phage genome injection by the HK97 superinfection exclusion protein, gp15. This region of the TMP also determines the PtsG requirement, and we show that gp15-mediated inhibition requires PtsG. Based on these data, we present a model for the in vivo genome injection process of phage HK97 and postulate a mechanism by which the inhibitory action of gp15 is reliant upon PtsG.

The phage HK97 infection process requires the presence of the bacterial inner membrane transporter protein, PtsG, and periplasmic folding chaperone, FkpA. Specific amino acid sequences in the HK97 tape measure protein encode the dependencies on these host proteins, as well as superinfection exclusion by the HK97 gp15 protein. Based on these data we propose a model for the in vivo genome injection process of HK97.

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