Abstract
The inherent ability of bacteriophages (phages) to infect specific bacterial hosts makes them ideal candidates to develop into antimicrobial agents for pathogen-specific remediation in food processing, biotechnology, and medicine (e.g., phage therapy). Conversely, phage contaminations of fermentation processes are a major concern to dairy and bioprocessing industries. The first stage of any successful phage infection is adsorption to a bacterial host cell, mediated by receptor-binding proteins (RBPs). As the first point of contact, the binding specificity of phage RBPs is the primary determinant of bacterial host range, and thus defines the remediative potential of a phage for a given bacterium. Co-evolution of RBPs and their bacterial receptors has forced endless adaptation cycles of phage-host interactions, which in turn has created a diverse array of phage adsorption mechanisms utilizing an assortment of RBPs. Over the last decade, these intricate mechanisms have been studied intensely using electron microscopy and X-ray crystallography, providing atomic-level details of this fundamental stage in the phage infection cycle. This review summarizes current knowledge surrounding the molecular basis of host interaction for various socioeconomically important Gram-positive targeting phage RBPs to their protein- and saccharide-based receptors. Special attention is paid to the abundant and best-characterized Siphoviridae family of tailed phages. Unravelling these complex phage-host dynamics is essential to harness the full potential of phage-based technologies, or for generating novel strategies to combat industrial phage contaminations.
Highlights
This review summarizes current knowledge surrounding the molecular basis of host interaction for various socioeconomically important Gram-positive targeting phage Receptor binding proteins (RBPs) to their proteinand saccharide-based receptors
In TP901-1, 18 BppU proteins assemble as six asymmetric trimers, forming a ring structure that attaches to the central Distal Tail Protein (Dit) hub via their
Teichoic acids are represented as lipoteichoic acids (LTAs), which are anchored to the cell membrane via a diglyceride group, or wall teichoic acid (WTA), which are covalently linked to the PG using a conserved disaccharide linker [89]
Summary
Bacteriophages (phages) are viruses that infect bacteria. As the most abundant and ubiquitous biological entities on Earth, with an estimated global population of >1031 particles [1], phages play important roles in global ecology and bacterial pathogenicity [2,3]. 3 of 25 host to it, i.e., how RBPs specific cell wall receptors, is crucial for understanding phage range, for the development of novel detection and biocontrol tools, and to evaluate the efficacy of Understanding how phages targeting Gram-positive bacteria recognize their host and absorb to anti-phage mechanisms fermented. This for review aims to phage draw host attention it, i.e., how their RBPs in bind specific cellfood wall production. Draw attention to a number of remarkable studies that describe the molecular basis of host recognition by phages infecting Gram-
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
