Abstract
The rapid discovery of new and diverse bacteriophages has driven the innovation of approaches aimed at detailing interactions with their bacterial hosts. Previous studies on receptor binding proteins (RBPs) mainly relied on their identification in silico and are based on similarities to well-characterized systems. Thus, novel phage RBPs unlike those currently annotated in genomic and proteomic databases remain largely undiscovered. In this study, we employed a screen to identify RBPs in flagellotropic Agrobacterium phage 7-7-1. Flagellotropic phages utilize bacterial flagella as receptors. The screen identified three candidate RBPs, Gp4, Gp102, and Gp44. Homology modelling predicted that Gp4 is a trimeric, tail associated protein with a central β-barrel, while the structure and function of Gp102 and Gp44 are less obvious. Studies with purified Gp41-247 confirmed its ability to bind and interact with host cells, highlighting the robustness of the RBP screen. We also discovered that Gp41-247 inhibits the growth of host cells in a motility and lipopolysaccharide (LPS) dependent fashion. Hence, our results suggest interactions between Gp41-247, rotating flagellar filaments and host glycans to inhibit host cell growth, which presents an impactful and intriguing focus for future studies.
Highlights
The rapid discovery of new and diverse bacteriophages has driven the innovation of approaches aimed at detailing interactions with their bacterial hosts
These efforts are hindered by two conflicting factors: (1) the need for rapid discovery of phages with specific host ranges for phage therapy applications versus (2) the time-consuming experimental characterization of phage gene product function
This finding indicated the possibility for the presence of multiple receptor binding proteins (RBPs) within phage 7-7-1 virions
Summary
Bacteriophage centered research and applications have boomed in recent years due to greater numbers of antibiotic resistant bacterial infections and the growing need for antibiotic alternatives [1,2,3]. Phage-host interactions during viral entry are typically investigated unilaterally, largely focusing on the bacterial hosts Such studies have identified outer membrane proteins, efflux pumps, capsular polysaccharide (CPS), lipopolysaccharide (LPS), pili, and flagella as receptors used by bacteriophages [8,9,10,11,12,13,14]. Phages that use polysaccharides as receptors carry proteins with the ability to enzymatically degrade these sugar chains These proteins are broadly defined as depolymerases and target glycan-containing bacterial components on host cell surfaces such as LPS, EPS, and CPS via their central domains [1,2,4,24,25]. Information gained from these studies will contribute to a model that delineates flagella-dependent phage entry mechanisms and informs possible protein-based therapeutics against Agrobacterium spp
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