Enzymes and Mechanisms Employed by Tailed Bacteriophages to Breach the Bacterial Cell Barriers

Viruses. 2018 Jul 27;10(8):396. doi: 10.3390/v10080396.

Abstract

Monoderm bacteria possess a cell envelope made of a cytoplasmic membrane and a cell wall, whereas diderm bacteria have and extra lipid layer, the outer membrane, covering the cell wall. Both cell types can also produce extracellular protective coats composed of polymeric substances like, for example, polysaccharidic capsules. Many of these structures form a tight physical barrier impenetrable by phage virus particles. Tailed phages evolved strategies/functions to overcome the different layers of the bacterial cell envelope, first to deliver the genetic material to the host cell cytoplasm for virus multiplication, and then to release the virion offspring at the end of the reproductive cycle. There is however a major difference between these two crucial steps of the phage infection cycle: virus entry cannot compromise cell viability, whereas effective virion progeny release requires host cell lysis. Here we present an overview of the viral structures, key protein players and mechanisms underlying phage DNA entry to bacteria, and then escape of the newly-formed virus particles from infected hosts. Understanding the biological context and mode of action of the phage-derived enzymes that compromise the bacterial cell envelope may provide valuable information for their application as antimicrobials.

Keywords: LysB; bacterial cell envelope; cell wall; depolymerase; endolysin; holin; lysin; peptidoglycan; proton motive force; spanin.

Publication types

  • Review

MeSH terms

  • Bacteria / virology*
  • Bacteriophages / enzymology*
  • Bacteriophages / physiology
  • Cell Wall / virology*
  • Endopeptidases / metabolism
  • Peptidoglycan / chemistry
  • Proton-Motive Force
  • Viral Proteins / metabolism
  • Viral Tail Proteins / metabolism*
  • Virion / metabolism
  • Virus Internalization*

Substances

  • Peptidoglycan
  • Viral Proteins
  • Viral Tail Proteins
  • Endopeptidases
  • endolysin