Bacteriophage virion-associated peptidoglycan hydrolases: potential new enzybiotics

References

• Abedon ST. (2011). Lysis from without. Bacteriophage, 1, 46–49.
   PubMedGoogle Scholar
• Bateman A, Rawlings ND. (2003). The CHAP domain: a large family of amidases including GSP amidase and peptidoglycan hydrolases. Trends Biochem Sci, 28, 234–237.
   Google Scholar
• Boulanger P, Jacquot P, Plançon L, Chami M, Engel A, Parquet C, Herbeuval C, Letellier L. (2008). Phage T5 straight tail fiber is a multifunctional protein acting as a tape measure and carrying fusogenic and muralytic activities. J Biol Chem, 283, 13556–13564.
   PubMed Web of Science ®Google Scholar
• Briers Y, Lavigne R, Plessers P, Hertveldt K, Hanssens I, Engelborghs Y, Volckaert G. (2006). Stability analysis of the bacteriophage phiKMV lysin gp36C and its putative role during infection. Cell Mol Life Sci, 63, 1899–1905.
   PubMed Web of Science ®Google Scholar
• Briers Y, Miroshnikov K, Chertkov O, Nekrasov A, Mesyanzhinov V, Volckaert G, Lavigne R. (2008). The structural peptidoglycan hydrolase gp181 of bacteriophage phiKZ. Biochem Biophys Res Commun, 374, 747–751.
   PubMed Web of Science ®Google Scholar
• Caldentey J, Bamford DH. (1992). The lytic enzyme of the Pseudomonas phage phi 6. Purification and biochemical characterization. Biochim Biophys Acta, 1159, 44–50.
   PubMed Web of Science ®Google Scholar
• Callewaert L, Walmagh M, Michiels CW, Lavigne R. (2011). Food applications of bacterial cell wall hydrolases. Curr Opin Biotechnol, 22, 164–171.
   PubMed Web of Science ®Google Scholar
• Courchesne NM, Parisien A, Lan CQ. (2009). Production and application of bacteriophage and bacteriophage-encoded lysins. Recent Pat Biotechnol, 3, 37–45.
   PubMedGoogle Scholar
• Clark JR, March JB. (2006). Bacteriophages and biotechnology: vaccines, gene therapy and antibacterials. Trends Biotechnol, 24, 212–218.
   PubMed Web of Science ®Google Scholar
• Daugelavicius R, Cvirkaite V, Gaidelyte A, Bakiene E, Gabrenaite-Verkhovskaya R, Bamford DH. (2005). Penetration of enveloped double-stranded RNA bacteriophages phi13 and phi6 into Pseudomonas syringae cells. J Virol, 79, 5017–5026.
   PubMed Web of Science ®Google Scholar
• Delbrück M. (1940). The growth of bacteriophage and lysis of the host. J Gen Physiol, 23, 643–660.
   PubMedGoogle Scholar
• During K, Porsch P, Fladung M, Lörz H. (1993). Transgenic potato plants resistant to the phytopathogenic bacterium Erwinia carotovora. Plant J, 3, 587–598.
   Web of Science ®Google Scholar
• Fallico V, Ross RP, Fitzgerald GF, McAuliffe O. (2011). Genetic response to bacteriophage infection in Lactococcus lactis reveals a four-strand approach involving induction of membrane stress proteins, D-alanylation of the cell wall, maintenance of proton motive force, and energy conservation. J Virol, 85, 12032–12042.
   PubMed Web of Science ®Google Scholar
• Fenton M, Ross P, McAuliffe O, O’Mahony J, Coffey A. (2010). Recombinant bacteriophage lysins as antibacterials. Bioeng Bugs, 1, 9–16.
   PubMedGoogle Scholar
• Fischetti VA. (2005). Bacteriophage lytic enzymes: novel anti-infectives. Trends Microbiol, 13, 491–496.
   PubMed Web of Science ®Google Scholar
• Fischetti VA. (2010). Bacteriophage endolysins: a novel anti-infective to control Gram-positive pathogens. Int J Med Microbiol, 300, 357–362.
   PubMed Web of Science ®Google Scholar
• Fraser JS, Maxwell KL, Davidson AR. (2007). Immunoglobulin-like domains on bacteriophage: weapons of modest damage? Curr Opin Microbiol, 10, 382–387.
   Google Scholar
• Frias MJ, Melo-Cristino J, Ramirez M. (2009). The autolysin LytA contributes to efficient bacteriophage progeny release in Streptococcus pneumoniae. J Bacteriol, 191, 5428–5440.
   PubMed Web of Science ®Google Scholar
• García P, Martínez B, Obeso JM, Rodríguez A. (2008). Bacteriophages and their application in food safety. Lett Appl Microbiol, 47, 479–485.
   PubMed Web of Science ®Google Scholar
• García P, Rodríguez L, Rodríguez A, Martínez B. (2010). Food biopreservation: promising strategies using bacteriocins, bacteriophages and endolysins. Trends Food Sci Tech, 21, 373–382.
   Web of Science ®Google Scholar
• Hendrix RW, Lawrence JG, Hatfull GF, Casjens S. (2000). The origins and ongoing evolution of viruses. Trends Microbiol, 8, 504–508.
   PubMed Web of Science ®Google Scholar
• Hermoso JA, García JL, García P. (2007). Taking aim on bacterial pathogens: from phage therapy to enzybiotics. Curr Opin Microbiol, 10, 461–472.
   PubMed Web of Science ®Google Scholar
• Kanamaru S, Ishiwata Y, Suzuki T, Rossmann MG, Arisaka F. (2005). Control of bacteriophage T4 tail lysozyme activity during the infection process. J Mol Biol, 346, 1013–1020.
   PubMed Web of Science ®Google Scholar
• Kao SH, McClain WH. (1980). Baseplate protein of bacteriophage T4 with both structural and lytic functions. J Virol, 34, 95–103.
   PubMed Web of Science ®Google Scholar
• Kasman LM, Kasman A, Westwater C, Dolan J, Schmidt MG, Norris JS. (2002). Overcoming the phage replication threshold: a mathematical model with implications for phage therapy. J Virol, 76, 5557–5564.
   PubMed Web of Science ®Google Scholar
• Kenny JG, McGrath S, Fitzgerald GF, van Sinderen D. (2004). Bacteriophage Tuc2009 encodes a tail-associated cell wall-degrading activity. J Bacteriol, 186, 3480–3491.
   Google Scholar
• Kivelä HM, Daugelavicius R, Hankkio RH, Bamford JK, Bamford DH. (2004). Penetration of membrane-containing double-stranded-DNA bacteriophage PM2 into Pseudoalteromonas hosts. J Bacteriol, 186, 5342–5354.
   PubMed Web of Science ®Google Scholar
• Lavigne R, Briers Y, Hertveldt K, Robben J, Volckaert G. (2004). Identification and characterization of a highly thermostable bacteriophage lysozyme. Cell Mol Life Sci, 61, 2753–2759.
   PubMed Web of Science ®Google Scholar
• Leiman PG, Arisaka F, van Raaij MJ, Kostyuchenko VA, Aksyuk AA, Kanamaru S, Rossmann MG. (2010). Morphogenesis of the T4 tail and tail fibers. Virol J, 7, 355.
   PubMed Web of Science ®Google Scholar
• Letellier L, Plançon L, Bonhivers M, Boulanger P. (1999). Phage DNA transport across membranes. Res Microbiol, 150, 499–505.
   PubMed Web of Science ®Google Scholar
• López R, García E. (2004). Recent trends on the molecular biology of pneumococcal capsules, lytic enzymes, and bacteriophage. FEMS Microbiol Rev, 28, 553–580.
   PubMed Web of Science ®Google Scholar
• Lu TK, Collins JJ. (2007). Dispersing biofilms with engineered enzymatic bacteriophage. Proc Natl Acad Sci USA, 104, 11197–11202.
   PubMed Web of Science ®Google Scholar
• Lu TK, Koeris MS. (2011). The next generation of bacteriophage therapy. Curr Opin Microbiol, 14, 524–531.
   PubMed Web of Science ®Google Scholar
• Lukacik P, Barnard TJ, Keller PW, Chaturvedi KS, Seddiki N, Fairman JW, Noinaj N, Kirby TL, Henderson JP, Steven AC, Hinnebusch BJ, Buchanan SK. (2012). Structural engineering of a phage lysin that targets gram-negative pathogens. Proc Natl Acad Sci USA, 109, 9857–9862.
   PubMed Web of Science ®Google Scholar
• Mahony J, McAuliffe O, Ross RP, van Sinderen D. (2011). Bacteriophages as biocontrol agents of food pathogens. Curr Opin Biotechnol, 22, 157–163.
   PubMed Web of Science ®Google Scholar
• Manoharadas S, Witte A, Bläsi U. (2009). Antimicrobial activity of a chimeric enzybiotic towards Staphylococcus aureus. J Biotechnol, 139, 118–123.
   PubMed Web of Science ®Google Scholar
• Matsuzaki S, Rashel M, Uchiyama J, Sakurai S, Ujihara T, Kuroda M, Ikeuchi M, Tani T, Fujieda M, Wakiguchi H, Imai S. (2005). Bacteriophage therapy: a revitalized therapy against bacterial infectious diseases. J Infect Chemother, 11, 211–219.
   PubMed Web of Science ®Google Scholar
• Mindich L, Lehman J. (1979). Cell wall lysin as a component of the bacteriophage phi 6 virion. J Virol, 30, 489–496.
   PubMed Web of Science ®Google Scholar
• Moak M, Molineux IJ. (2000). Role of the Gp16 lytic transglycosylase motif in bacteriophage T7 virions at the initiation of infection. Mol Microbiol, 37, 345–355.
   PubMed Web of Science ®Google Scholar
• Moak M, Molineux IJ. (2004). Peptidoglycan hydrolytic activities associated with bacteriophage virions. Mol Microbiol, 51, 1169–1183.
   PubMed Web of Science ®Google Scholar
• Nelson DC, Schmelcher M, Rodriguez-Rubio L, Klumpp J, Pritchard DG, Dong S, Donovan DM. (2012). Endolysins as antimicrobials. Adv Virus Res, 83, 299–365.
   PubMed Web of Science ®Google Scholar
• Nishima W, Kanamaru S, Arisaka F, Kitao A. (2011). Screw motion regulates multiple functions of T4 phage protein gene product 5 during cell puncturing. J Am Chem Soc, 133, 13571–13576.
   PubMed Web of Science ®Google Scholar
• Paul VD, Rajagopalan SS, Sundarrajan S, George SE, Asrani JY, Pillai R, Chikkamadaiah R, Durgaiah M, Sriram B, Padmanabhan S. (2011). A novel bacteriophage Tail-Associated Muralytic Enzyme (TAME) from Phage K and its development into a potent antistaphylococcal protein. BMC Microbiol, 11, 226.
   PubMed Web of Science ®Google Scholar
• Piuri M, Hatfull GF. (2006). A peptidoglycan hydrolase motif within the mycobacteriophage TM4 tape measure protein promotes efficient infection of stationary phase cells. Mol Microbiol, 62, 1569–1585.
   PubMed Web of Science ®Google Scholar
• Rashel M, Uchiyama J, Takemura I, Hoshiba H, Ujihara T, Takatsuji H, Honke K, Matsuzaki S. (2008). Tail-associated structural protein gp61 of Staphylococcus aureus phage phi MR11 has bifunctional lytic activity. FEMS Microbiol Lett, 284, 9–16.
   PubMed Web of Science ®Google Scholar
• Ribelles P, Rodríguez I, Suárez JE. (2012). LysA2, the Lactobacillus casei bacteriophage A2 lysin is an endopeptidase active on a wide spectrum of lactic acid bacteria. Appl Microbiol Biotechnol, 94, 101–110.
   PubMed Web of Science ®Google Scholar
• Rodríguez L, Martínez B, Zhou Y, Rodríguez A, Donovan DM, García P. (2011). Lytic activity of the virion-associated peptidoglycan hydrolase HydH5 of Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88. BMC Microbiol, 11, 138.
   Google Scholar
• Rodríguez-Rubio L, Martínez B, Rodríguez A, Donovan DM, García P. (2012a). Enhanced staphylolytic activity of the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88 HydH5 virion-associated peptidoglycan hydrolase: fusions, deletions, and synergy with LysH5. Appl Environ Microbiol, 78, 2241–2248.
   PubMed Web of Science ®Google Scholar
• Rodríguez-Rubio L, Gutiérrez D, Martínez B, Rodríguez A, Götz F, García P. (2012b). The Tape Measure Protein of the Staphylococcus aureus Bacteriophage vB_SauS-phiIPLA35 Has an Active Muramidase Domain. Appl Environ Microbiol, 78, 6369–6371.
   PubMed Web of Science ®Google Scholar
• Rydman PS, Bamford DH. (2000). Bacteriophage PRD1 DNA entry uses a viral membrane-associated transglycosylase activity. Mol Microbiol, 37, 356–363.
   PubMed Web of Science ®Google Scholar
• Rydman PS, Bamford DH. (2002). The lytic enzyme of bacteriophage PRD1 is associated with the viral membrane. J Bacteriol, 184, 104–110.
   PubMed Web of Science ®Google Scholar
• Sharma M, Anand SK. (2002). Characterization of constitutive microflora of biofilms in dairy processing lines. Food Microbiol, 19, 627–636.
   Google Scholar
• Sudiarta IP, Fukushima T, Sekiguchi J. (2010). Bacillus subtilis CwlP of the SP-{beta} prophage has two novel peptidoglycan hydrolase domains, muramidase and cross-linkage digesting DD-endopeptidase. J Biol Chem, 285, 41232–41243.
   PubMed Web of Science ®Google Scholar
• Takác M, Bläsi U. (2005). Phage P68 virion-associated protein 17 displays activity against clinical isolates of Staphylococcus aureus. Antimicrob Agents Chemother, 49, 2934–2940.
   PubMed Web of Science ®Google Scholar
• Vipra AA, Desai SN, Roy P, Patil R, Raj JM, Narasimhaswamy N, Paul VD, Chikkamadaiah R, Sriram B. (2012). Antistaphylococcal activity of bacteriophage derived chimeric protein P128. BMC Microbiol, 12, 41.
   PubMed Web of Science ®Google Scholar
• Wattinger L, Stephan R, Layer F, Johler S. (2012). Comparison of Staphylococcus aureus isolates associated with food intoxication with isolates from human nasal carriers and human infections. Eur J Clin Microbiol Infect Dis, 31, 455–464.
   PubMed Web of Science ®Google Scholar
• Yoong P, Schuch R, Nelson D, Fischetti VA. (2004). Identification of a broadly active phage lytic enzyme with lethal activity against antibiotic-resistant Enterococcus faecalis and Enterococcus faecium. J Bacteriol, 186, 4808–4812.
   PubMed Web of Science ®Google Scholar
• Young I, Wang I, Roof WD. (2000). Phages will out: strategies of host cell lysis. Trends Microbiol, 8, 120–128.
   PubMed Web of Science ®Google Scholar
• Zimmer M, Vukov N, Scherer S, Loessner MJ. (2002). The murein hydrolase of the bacteriophage phi3626 dual lysis system is active against all tested Clostridium perfringens strains. Appl Environ Microbiol, 68, 5311–5317.
   PubMed Web of Science ®Google Scholar
• Zou Y, Hou C. (2010). Systematic analysis of an amidase domain CHAP in 12 Staphylococcus aureus genomes and 44 staphylococcal phage genomes. Comput Biol Chem, 34, 251–257.
   PubMed Web of Science ®Google Scholar