Lysin

Lysozyme-like phage lysin
Crystal structure of the modular CPL-1 endolysin from Streptococcus phage Cp-1 complexed with a peptidoglycan analogue. PDB entry 2j8g.[1]
Identifiers
EC no.3.2.1.17
CAS no.9001-63-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Lysins, also known as endolysins or murein hydrolases, are hydrolytic enzymes produced by bacteriophages in order to cleave the host's cell wall during the final stage of the lytic cycle. Lysins are highly evolved enzymes that are able to target one of the five bonds in peptidoglycan (murein), the main component of bacterial cell walls, which allows the release of progeny virions from the lysed cell. Cell-wall-containing Archaea are also lysed by specialized pseudomurein-cleaving lysins,[2] while most archaeal viruses employ alternative mechanisms.[3] Similarly, not all bacteriophages synthesize lysins: some small single-stranded DNA and RNA phages produce membrane proteins that activate the host's autolytic mechanisms such as autolysins.[4]

Lysins were first used therapeutically in 2001 by the Fischetti lab (see below) and are now being used as antibacterial agents due to their high effectiveness and specificity in comparison with antibiotics, which are susceptible to bacterial resistance.[5] Because lysins are essential for bacteriophage survival, resistance to lysins is an extremely rare event. Over the >20 years of lysin development as therapeutics, resistance has not been observed, even when resistance is forced by mutagenesis experiments.

  1. ^ Pérez-Dorado I, Campillo NE, Monterroso B, Hesek D, Lee M, Páez JA, García P, Martínez-Ripoll M, García JL, Mobashery S, Menéndez M, Hermoso JA (August 2007). "Elucidation of the molecular recognition of bacterial cell wall by modular pneumococcal phage endolysin CPL-1". J. Biol. Chem. 282 (34): 24990–9. doi:10.1074/jbc.M704317200. hdl:10261/12517. PMID 17581815.
  2. ^ Visweswaran GR, Dijkstra BW, Kok J (November 2010). "Two major archaeal pseudomurein endoisopeptidases: PeiW and PeiP". Archaea. 2010: 480492. doi:10.1155/2010/480492. PMC 2989375. PMID 21113291.
  3. ^ Quemin ER, Quax TE (5 June 2015). "Archaeal viruses at the cell envelope: entry and egress". Frontiers in Microbiology. 6: 552. doi:10.3389/fmicb.2015.00552. PMC 4456609. PMID 26097469.
  4. ^ Young R (September 1992). "Bacteriophage lysis: mechanism and regulation". Microbiological Reviews. 56 (3): 430–81. doi:10.1128/mr.56.3.430-481.1992. PMC 372879. PMID 1406491.
  5. ^ Fischetti VA (Oct 2008). "Bacteriophage lysins as effective antibacterials". Current Opinion in Microbiology. 11 (5): 393–400. doi:10.1016/j.mib.2008.09.012. PMC 2597892. PMID 18824123.