Biophysical Reviews

, Volume 10, Issue 2, pp 535–542 | Cite as

Review of the nature, diversity and structure of bacteriophage receptor binding proteins that target Gram-positive bacteria

Review

Abstract

As the importance of bacteriophages as novel antimicrobials and potential diagnostics comes increasingly into focus, there is a heightened interest in understanding the mechanisms of how they interact with their bacterial hosts. The first step of a bacteriophage (phage) infection is the recognition of specific moieties on the bacterial cell surface as determined by their phage receptor binding proteins (RBPs). Knowledge of RBPs and how they interact with bacteria has been driven by studies of model phages and of industrially important phages, such as those that impact the dairy industry. Therefore, data from these phage groups constitute the majority of this review. We start with a brief introduction to phages, their life cycles and known receptors. We then review the state-of-the-art knowledge of phage RBPs of Gram-positive bacteria in the context of the better understood Gram-negative bacterial RBPs. In general, more is known about the RBPs of siphoviruses than myoviruses, which is reflected here, but for both virus families, where possible, we show what RBPs are, how they are arranged within phage genomes and what is known about their structures. As RBPs are the key determinant of phage specificity, studying and characterising them is important, for downstream applications such as diagnostic and therapeutic purposes.

Keywords

Receptor binding proteins Siphoviruses Myoviruses Gram-positive bacteria Bacteria–phage interaction 

Notes

Acknowledgements

We are grateful to the Libyan Ministry of Higher Education for funding the PhD studies of ASAD.

Compliance with ethical standards

Conflict of interest

Ahmed S.A. Dowah declares that he has no conflict of interest. Martha R. J. Clokie declares that she has no conflict of interest.

Ethical approval

This article does not contain any studies with human participants or animals performed by any of the authors.

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Copyright information

© International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature 2017

Authors and Affiliations

  1. 1.Department of Infection, Immunity and InflammationUniversity of LeicesterLeicesterUK

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