Abstract
Recently, a large number of new technologies have been developed that exploit the unique properties of bacteriophage receptor binding proteins (RBPs). These include their use in diagnostic applications that selectively capture bacteria and as therapeutics that reduce bacterial colonization in vivo. RBPs exhibit comparable, and in many cases superior, stability, receptor specificity, and affinity to other carbohydrate binding proteins such as antibodies or lectins. In order to further exploit the use of RBPs, we have developed an assay for discovering RBPs using phage genome expression libraries and protein screens to identify binding partners that recognize the host bacterium. When phage P22 was screened using this assay, Gp9 was the only RBP discovered, confirming previous predictions that this is the sole RBP encoded by this phage. We then examined the Escherichia coli O157:H7 typing phage 1 in our assay and identified a previously undescribed RBP. This general approach has the potential to assist in the identification of RBPs from other bacteriophages.
Highlights
Bacteriophage receptor binding proteins (RBPs) have recently been developed into a number of tools that make use of their high specificity and robustness [1]. These technologies include diagnostics involving RBPs bound to surfaces [2], or to beads [3,4], for the selective capture of bacteria
RBPs have been employed as therapeutics that reduce specific bacterial colonization in vivo, either alone [5] or as part of a larger molecular machine [6]
Receptor binding proteins are the components used by phages for host recognition and attachment
Summary
Bacteriophage receptor binding proteins (RBPs) have recently been developed into a number of tools that make use of their high specificity and robustness [1]. GTAs are non-replicative phage-like particles that package portions of the bacterial chromosome and inject that DNA into a neighboring target cell [14] Both of these machines rely on their RBPs for binding to and identification of their host, and present other natural reservoirs for proteins of this class. Lambda phage has been shown to be a useful tool for annotating phage genomes, to date there is no rapid method for identifying phage RBPs, even within sequenced genomes This is a result of the fact that RBPs are difficult to identify based on homology, since RBPs each bind to distinct receptors. Together these results demonstrate the utility of an assay for accurate RBP identification from phages belonging to two of the three major families of tailed phages
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