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Phage lytic enzymes: a history

Virologica Sinica volume 30, pages 26–32 (2015)Cite this article

Abstract

There are many recent studies regarding the efficacy of bacteriophage-related lytic enzymes: the enzymes of ‘bacteria-eaters’ or viruses that infect bacteria. By degrading the cell wall of the targeted bacteria, these lytic enzymes have been shown to efficiently lyse Gram-positive bacteria without affecting normal flora and non-related bacteria. Recent studies have suggested approaches for lysing Gram-negative bacteria as well (Briersa Y, et al., 2014). These enzymes include: phage-lysozyme, endolysin, lysozyme, lysin, phage lysin, phage lytic enzymes, phageassociated enzymes, enzybiotics, muralysin, muramidase, virolysin and designations such as Ply, PAE and others. Bacteriophages are viruses that kill bacteria, do not contribute to antimicrobial resistance, are easy to develop, inexpensive to manufacture and safe for humans, animals and the environment. The current focus on lytic enzymes has been on their use as anti-infectives in humans and more recently in agricultural research models. The initial translational application of lytic enzymes, however, was not associated with treating or preventing a specific disease but rather as an extraction method to be incorporated in a rapid bacterial detection assay (Bernstein D, 1997).The current review traces the translational history of phage lytic enzymes-from their initial discovery in 1986 for the rapid detection of group A streptococcus in clinical specimens to evolving applications in the detection and prevention of disease in humans and in agriculture.

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  1. New Horizons Diagnostic Corporation, Reisterstown, Baltimore, MD, 21227, USA

    David Trudil

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  1. David Trudil
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Correspondence to David Trudil.

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ORCID: 0000-0002-4114-8138

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Trudil, D. Phage lytic enzymes: a history. Virol. Sin. 30, 26–32 (2015). https://doi.org/10.1007/s12250-014-3549-0

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  • DOI: https://doi.org/10.1007/s12250-014-3549-0

Keywords

  • bacteriophage
  • phage lytic enzymes
  • translational application
  • lysin