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Volumn 11, Issue 10, 2013, Pages 675-687

Revenge of the phages: Defeating bacterial defences

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BINDING PROTEIN; CRISPR ASSOCIATED PROTEIN; PROTEIN CRISPR; UNCLASSIFIED DRUG;

EID: 84884286187     PISSN: 17401526     EISSN: 17401534     Source Type: Journal    
DOI: 10.1038/nrmicro3096     Document Type: Review
Times cited : (505)

References (125)
  • 1
    • 0037059610 scopus 로고    scopus 로고
    • Phage Genomics: Small is beautiful
    • DOI 10.1016/S0092-8674(01)00637-7
    • Brüssow, H. & Hendrix, R. W. Phage genomics: small is beautiful. Cell 108, 13-16 (2002). (Pubitemid 34137008)
    • (2002) Cell , vol.108 , Issue.1 , pp. 13-16
    • Brussow, H.1    Hendrix, R.W.2
  • 3
    • 34548792911 scopus 로고    scopus 로고
    • Marine viruses - Major players in the global ecosystem
    • DOI 10.1038/nrmicro1750, PII NRMICRO1750
    • Suttle, C. A. Marine viruses - major players in the global ecosystem. Nature Rev. Microbiol. 5, 801-812 (2007). (Pubitemid 47423768)
    • (2007) Nature Reviews Microbiology , vol.5 , Issue.10 , pp. 801-812
    • Suttle, C.A.1
  • 4
    • 34447252342 scopus 로고    scopus 로고
    • On kinetics of phage adsorption
    • DOI 10.1529/biophysj.106.102962
    • Moldovan, R., Chapman-McQuiston, E. & Wu, X. L. On kinetics of phage adsorption. Biophys. J. 93, 303-315 (2007). (Pubitemid 47041675)
    • (2007) Biophysical Journal , vol.93 , Issue.1 , pp. 303-315
    • Moldovan, R.1    Chapman-McQuiston, E.2    Wu, X.L.3
  • 5
    • 80051788970 scopus 로고    scopus 로고
    • Bacteriophage-host interactions leading to genome internalization
    • Bertin, A., de Frutos, M. & Letellier, L. Bacteriophage-host interactions leading to genome internalization. Curr. Opin. Microbiol. 14, 492-496 (2011).
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 492-496
    • Bertin, A.1    De Frutos, M.2    Letellier, L.3
  • 6
    • 77957945540 scopus 로고    scopus 로고
    • Bacteriophage receptors, mechanisms of phage adsorption and penetration into host cell
    • Rakhuba, D. V., Kolomiets, E. I., Dey, E. S. & Novik, G. I. Bacteriophage receptors, mechanisms of phage adsorption and penetration into host cell. Pol. J. Microbiol. 59, 145-155 (2010).
    • (2010) Pol. J. Microbiol. , vol.59 , pp. 145-155
    • Rakhuba, D.V.1    Kolomiets, E.I.2    Dey, E.S.3    Novik, G.I.4
  • 7
    • 79960300327 scopus 로고    scopus 로고
    • Single-virus tracking reveals a spatial receptor-dependent search mechanism
    • Rothenberg, E. et al. Single-virus tracking reveals a spatial receptor-dependent search mechanism. Biophys. J. 100, 2875-2882 (2011).
    • (2011) Biophys. J. , vol.100 , pp. 2875-2882
    • Rothenberg, E.1
  • 8
    • 84871763191 scopus 로고    scopus 로고
    • Phase variable expression of capsular polysaccharide modifications allows Campylobacter jejuni to avoid bacteriophage infection in chickens
    • Sorensen, M. C. et al. Phase variable expression of capsular polysaccharide modifications allows Campylobacter jejuni to avoid bacteriophage infection in chickens. Front. Cell. Infect. Microbiol. 2, 11 (2012).
    • (2012) Front. Cell. Infect. Microbiol. , vol.2 , pp. 11
    • Sorensen, M.C.1
  • 9
    • 84867461986 scopus 로고    scopus 로고
    • Spontaneous and transient defence against bacteriophage by phase-variable glucosylation of O-antigen in Salmonella enterica serovar Typhimurium
    • Kim, M. & Ryu, S. Spontaneous and transient defence against bacteriophage by phase-variable glucosylation of O-antigen in Salmonella enterica serovar Typhimurium. Mol. Microbiol. 86, 411-425 (2012).
    • (2012) Mol. Microbiol. , vol.86 , pp. 411-425
    • Kim, M.1    Ryu, S.2
  • 11
    • 84870625727 scopus 로고    scopus 로고
    • Interaction of bacteriophage l with its E. Coli receptor
    • Chatterjee, S. & Rothenberg, E. Interaction of bacteriophage l with its E. coli receptor, LamB. Viruses 4, 3162-3178 (2012).
    • (2012) LamB. Viruses , vol.4 , pp. 3162-3178
    • Chatterjee, S.1    Rothenberg, E.2
  • 12
    • 84863393863 scopus 로고    scopus 로고
    • Repeatability and contingency in the evolution of a key innovation in phage lambda
    • Meyer, J. R. et al. Repeatability and contingency in the evolution of a key innovation in phage lambda. Science 335, 428-432 (2012).
    • (2012) Science , vol.335 , pp. 428-432
    • Meyer, J.R.1
  • 13
    • 78149460978 scopus 로고    scopus 로고
    • Bacteriophage PhiX174's ecological niche and the flexibility of its Escherichia coli lipopolysaccharide receptor
    • Michel, A., Clermont, O., Denamur, E. & Tenaillon, O. Bacteriophage PhiX174's ecological niche and the flexibility of its Escherichia coli lipopolysaccharide receptor. Appl. Environ. Microbiol. 76, 7310-7313 (2010).
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 7310-7313
    • Michel, A.1    Clermont, O.2    Denamur, E.3    Tenaillon, O.4
  • 14
    • 55549105742 scopus 로고    scopus 로고
    • Genomic evolution in a virus under specific selection for host recognition
    • Pepin, K. M., Domsic, J. & McKenna, R. Genomic evolution in a virus under specific selection for host recognition. Infect. Genet. Evol. 8, 825-834 (2008).
    • (2008) Infect. Genet. Evol. , vol.8 , pp. 825-834
    • Pepin, K.M.1    Domsic, J.2    McKenna, R.3
  • 15
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: The Keio collection
    • 2006.0008
    • Baba, T. et al. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol. Syst. Biol. 2, 2006.0008 (2006).
    • (2006) Mol. Syst. Biol. , vol.2
    • Baba, T.1
  • 17
    • 0036223970 scopus 로고    scopus 로고
    • A conserved C-terminal region in Gp71 of the small isometric-head phage LL-H and ORF474 of the prolate-head phage JCL1032 is implicated in specificity of adsorption of phage to its host, Lactobacillus delbrueckii
    • DOI 10.1128/JB.184.9.2455-2459.2002
    • Ravin, V., Raisanen, L. & Alatossava, T. A conserved C-terminal region in Gp71 of the small isometric-head phage LL-H and ORF474 of the prolate-head phage JCL1032 is implicated in specificity of adsorption of phage to its host, Lactobacillus delbrueckii. J. Bacteriol. 184, 2455-2459 (2002). (Pubitemid 34311138)
    • (2002) Journal of Bacteriology , vol.184 , Issue.9 , pp. 2455-2459
    • Ravin, V.1    Raisanen, L.2    Alatossava, T.3
  • 18
    • 79959842126 scopus 로고    scopus 로고
    • Genomic island variability facilitates Prochlorococcus-virus coexistence
    • Avrani, S., Wurtzel, O., Sharon, I., Sorek, R. & Lindell, D. Genomic island variability facilitates Prochlorococcus-virus coexistence. Nature 474, 604-608 (2011).
    • (2011) Nature , vol.474 , pp. 604-608
    • Avrani, S.1    Wurtzel, O.2    Sharon, I.3    Sorek, R.4    Lindell, D.5
  • 19
    • 78650916252 scopus 로고    scopus 로고
    • Genetic basis of infectivity evolution in a bacteriophage
    • Scanlan, P. D., Hall, A. R., Lopez-Pascua, L. D. & Buckling, A. Genetic basis of infectivity evolution in a bacteriophage. Mol. Ecol. 20, 981-989 (2011).
    • (2011) Mol. Ecol. , vol.20 , pp. 981-989
    • Scanlan, P.D.1    Hall, A.R.2    Lopez-Pascua, L.D.3    Buckling, A.4
  • 20
    • 77949423965 scopus 로고    scopus 로고
    • Antagonistic coevolution accelerates molecular evolution
    • Paterson, S. et al. Antagonistic coevolution accelerates molecular evolution. Nature 464, 275-278 (2010).
    • (2010) Nature , vol.464 , pp. 275-278
    • Paterson, S.1
  • 21
    • 23744448545 scopus 로고    scopus 로고
    • Escherichia coli K1's capsule is a barrier to bacteriophage T7
    • DOI 10.1128/AEM.71.8.4872-4874.2005
    • Scholl, D., Adhya, S. & Merril, C. Escherichia coli K1's capsule is a barrier to bacteriophage T7. Appl. Environ. Microbiol. 71, 4872-4874 (2005). (Pubitemid 41129547)
    • (2005) Applied and Environmental Microbiology , vol.71 , Issue.8 , pp. 4872-4874
    • Scholl, D.1    Adhya, S.2    Merril, C.3
  • 23
    • 33745262326 scopus 로고    scopus 로고
    • Evolution of bacteriophages infecting encapsulated bacteria: Lessons from Escherichia coli K1-specific phages
    • Stummeyer, K. et al. Evolution of bacteriophages infecting encapsulated bacteria: lessons from Escherichia coli K1-specific phages. Mol. Microbiol. 60, 1123-1135 (2006).
    • (2006) Mol. Microbiol. , vol.60 , pp. 1123-1135
    • Stummeyer, K.1
  • 24
    • 0036645702 scopus 로고    scopus 로고
    • The hyaluronan lyase of Streptococcus pyogenes bacteriophage H4489A
    • DOI 10.1042/BJ20020149
    • Baker, J. R., Dong, S. & Pritchard, D. G. The hyaluronan lyase of Streptococcus pyogenes bacteriophage H4489A. Biochem. J. 365, 317-322 (2002). (Pubitemid 34756167)
    • (2002) Biochemical Journal , vol.365 , Issue.1 , pp. 317-322
    • Baker, J.R.1    Dong, S.2    Pritchard, D.G.3
  • 25
    • 84870686757 scopus 로고    scopus 로고
    • Identification of EPS-degrading activity within the tail spikes of the novel Pseudomonas putida phage AF
    • Cornelissen, A. et al. Identification of EPS-degrading activity within the tail spikes of the novel Pseudomonas putida phage AF. Virology 434, 251-256 (2012).
    • (2012) Virology , vol.434 , pp. 251-256
    • Cornelissen, A.1
  • 26
    • 74049108861 scopus 로고    scopus 로고
    • Bacteriophage-derived enzyme that depolymerizes the alginic acid capsule associated with cystic fibrosis isolates of Pseudomonas aeruginosa
    • Glonti, T., Chanishvili, N. & Taylor, P. W. Bacteriophage-derived enzyme that depolymerizes the alginic acid capsule associated with cystic fibrosis isolates of Pseudomonas aeruginosa. J. Appl. Microbiol. 108, 695-702 (2010).
    • (2010) J. Appl. Microbiol. , vol.108 , pp. 695-702
    • Glonti, T.1    Chanishvili, N.2    Taylor, P.W.3
  • 30
    • 34548607346 scopus 로고    scopus 로고
    • Diversity-generating retroelements
    • DOI 10.1016/j.mib.2007.06.004, PII S1369527407000884, Host-microbe interactions: fungi/parasites/viruses
    • Medhekar, B. & Miller, J. F. Diversity-generating retroelements. Curr. Opin. Microbiol. 10, 388-395 (2007). (Pubitemid 47404952)
    • (2007) Current Opinion in Microbiology , vol.10 , Issue.4 , pp. 388-395
    • Medhekar, B.1    Miller, J.F.2
  • 31
    • 84874293279 scopus 로고    scopus 로고
    • The lactococcal phages Tuc2009 and TP901-1 incorporate two alternate forms of their tail fiber into their virions for infection specialization
    • Stockdale, S. R. et al. The lactococcal phages Tuc2009 and TP901-1 incorporate two alternate forms of their tail fiber into their virions for infection specialization. J. Biol. Chem. 288, 5581-5590 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 5581-5590
    • Stockdale, S.R.1
  • 32
    • 0342576226 scopus 로고    scopus 로고
    • Bacteriophage T4 host range is expanded by duplications of a small domain of the tail fiber adhesin
    • DOI 10.1006/jmbi.1996.0281
    • Tetart, F., Repoila, F., Monod, C. & Krisch, H. M. Bacteriophage T4 host range is expanded by duplications of a small domain of the tail fiber adhesin. J. Mol. Biol. 258, 726-731 (1996). (Pubitemid 26150875)
    • (1996) Journal of Molecular Biology , vol.258 , Issue.5 , pp. 726-731
    • Tetart, F.1    Repoila, F.2    Monod, C.3    Krisch, H.M.4
  • 33
    • 84863036350 scopus 로고    scopus 로고
    • A T3 and T7 recombinant phage acquires efficient adsorption and a broader host range
    • Lin, T. Y. et al. A T3 and T7 recombinant phage acquires efficient adsorption and a broader host range. PLoS ONE 7, e30954 (2012).
    • (2012) PLoS ONE , vol.7
    • Lin, T.Y.1
  • 34
    • 84869068027 scopus 로고    scopus 로고
    • A multivalent adsorption apparatus explains the broad host range of phage phi92: A comprehensive genomic and structural analysis
    • Schwarzer, D. et al. A multivalent adsorption apparatus explains the broad host range of phage phi92: a comprehensive genomic and structural analysis. J. Virol. 86, 10384-10398 (2012).
    • (2012) J. Virol. , vol.86 , pp. 10384-10398
    • Schwarzer, D.1
  • 35
    • 0037389511 scopus 로고    scopus 로고
    • A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes
    • Roberts, R. J. et al. A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes. Nucleic Acids Res. 31, 1805-1812 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 1805-1812
    • Roberts, R.J.1
  • 36
    • 22544464152 scopus 로고    scopus 로고
    • The biology of restriction and anti-restriction
    • DOI 10.1016/j.mib.2005.06.003, PII S1369527405000779, Host-Microbe Interactions: Fungi / Parasites
    • Tock, M. R. & Dryden, D. T. The biology of restriction and anti-restriction. Curr. Opin. Microbiol. 8, 466-472 (2005). (Pubitemid 41021909)
    • (2005) Current Opinion in Microbiology , vol.8 , Issue.4 , pp. 466-472
    • Tock, M.R.1    Dryden, D.T.F.2
  • 37
    • 0036146923 scopus 로고    scopus 로고
    • Immigration control of DNA in bacteria: Self versus non-self
    • Murray, N. E. Fred Griffith review lecture. Immigration control of DNA in bacteria: self versus non-self. Microbiology 148, 3-20 (2001). (Pubitemid 34083180)
    • (2002) Microbiology , vol.148 , Issue.1 , pp. 3-20
    • Murray, N.E.1
  • 38
    • 0016745114 scopus 로고
    • A deoxyribonuclease of Diplococcus pneumoniae specific for methylated DNA
    • Lacks, S. & Greenberg, B. A deoxyribonuclease of Diplococcus pneumoniae specific for methylated DNA. J. Biol. Chem. 250, 4060-4066 (1975).
    • (1975) J. Biol. Chem. , vol.250 , pp. 4060-4066
    • Lacks, S.1    Greenberg, B.2
  • 39
    • 0020575930 scopus 로고
    • Bacteriophage survival: Multiple mechanisms for avoiding the deoxyribonucleic acid restriction systems of their hosts
    • Kruger, D. H. & Bickle, T. A. Bacteriophage survival: multiple mechanisms for avoiding the deoxyribonucleic acid restriction systems of their hosts. Microbiol. Rev. 47, 345-360 (1983). (Pubitemid 13004240)
    • (1983) Microbiological Reviews , vol.47 , Issue.3 , pp. 345-360
    • Kruger, D.H.1    Bickle, T.A.2
  • 40
    • 0027324744 scopus 로고
    • Biology of DNA restriction
    • Bickle, T. A. & Kruger, D. H. Biology of DNA restriction. Microbiol. Rev. 57, 434-450 (1993). (Pubitemid 23170101)
    • (1993) Microbiological Reviews , vol.57 , Issue.2 , pp. 434-450
    • Bickle, T.A.1    Kruger, D.H.2
  • 41
    • 0024284313 scopus 로고
    • EcoRII can be activated to cleave refractory DNA recognition sites
    • Kruger, D. H., Barcak, G. J., Reuter, M. & Smith, H. O. EcoRII can be activated to cleave refractory DNA recognition sites. Nucleic Acids Res. 16, 3997-4008 (1988).
    • (1988) Nucleic Acids Res. , vol.16 , pp. 3997-4008
    • Kruger, D.H.1    Barcak, G.J.2    Reuter, M.3    Smith, H.O.4
  • 42
    • 0026584744 scopus 로고
    • Type III restriction enzymes need two inversely oriented recognition sites for DNA cleavage
    • Meisel, A., Bickle, T. A., Kruger, D. H. & Schroeder, C. Type III restriction enzymes need two inversely oriented recognition sites for DNA cleavage. Nature 355, 467-469 (1992).
    • (1992) Nature , vol.355 , pp. 467-469
    • Meisel, A.1    Bickle, T.A.2    Kruger, D.H.3    Schroeder, C.4
  • 43
    • 0019248608 scopus 로고
    • Modified bases in bacteriophage DNAs
    • Warren, R. A. Modified bases in bacteriophage DNAs. Annu. Rev. Microbiol. 34, 137-158 (1980).
    • (1980) Annu. Rev. Microbiol. , vol.34 , pp. 137-158
    • Warren, R.A.1
  • 44
    • 33846591325 scopus 로고    scopus 로고
    • A Type IV Modification Dependent Restriction Nuclease that Targets Glucosylated Hydroxymethyl Cytosine Modified DNAs
    • DOI 10.1016/j.jmb.2006.11.051, PII S0022283606015919
    • Bair, C. L. & Black, L. W. A type IV modification dependent restriction nuclease that targets glucosylated hydroxymethyl cytosine modified DNAs. J. Mol. Biol. 366, 768-778 (2007). (Pubitemid 46175865)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.3 , pp. 768-778
    • Bair, C.L.1    Black, L.W.2
  • 45
    • 0026634757 scopus 로고
    • McrBC: A multisubunit GTP-dependent restriction endonuclease
    • Sutherland, E., Coe, L. & Raleigh, E. A. McrBC: a multisubunit GTP-dependent restriction endonuclease. J. Mol. Biol. 225, 327-348 (1992).
    • (1992) J. Mol. Biol. , vol.225 , pp. 327-348
    • Sutherland, E.1    Coe, L.2    Raleigh, E.A.3
  • 46
    • 37349090077 scopus 로고    scopus 로고
    • Restriction Endonuclease Inhibitor IPI of Bacteriophage T4: A Novel Structure for a Dedicated Target
    • DOI 10.1016/j.jmb.2007.10.064, PII S0022283607014234
    • Rifat, D., Wright, N. T., Varney, K. M., Weber, D. J. & Black, L. W. Restriction endonuclease inhibitor IPI*of bacteriophage T4: a novel structure for a dedicated target. J. Mol. Biol. 375, 720-734 (2008). (Pubitemid 350297286)
    • (2008) Journal of Molecular Biology , vol.375 , Issue.3 , pp. 720-734
    • Rifat, D.1    Wright, N.T.2    Varney, K.M.3    Weber, D.J.4    Black, L.W.5
  • 47
    • 0023092429 scopus 로고
    • - phages
    • DOI 10.1016/0042-6822(87)90324-2
    • Iida, S., Streiff, M. B., Bickle, T. A. & Arber, W. Two DNA antirestriction systems of bacteriophage P1, darA, and darB: characterization of darA- phages. Virology 157, 156-166 (1987). (Pubitemid 17029993)
    • (1987) Virology , vol.157 , Issue.1 , pp. 156-166
    • Iida, S.1    Streiff, M.B.2    Bickle, T.A.3    Arber, W.4
  • 48
    • 0037106445 scopus 로고    scopus 로고
    • Interaction of the ocr gene 0.3 protein of bacteriophage T7 with EcoKI restriction/modification enzyme
    • Atanasiu, C., Su, T. J., Sturrock, S. S. & Dryden, D. T. Interaction of the ocr gene 0.3 protein of bacteriophage T7 with EcoKI restriction/ modification enzyme. Nucleic Acids Res. 30, 3936-3944 (2002).
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3936-3944
    • Atanasiu, C.1    Su, T.J.2    Sturrock, S.S.3    Dryden, D.T.4
  • 50
    • 0026338873 scopus 로고
    • Restriction and modification systems
    • Wilson, G. G. & Murray, N. E. Restriction and modification systems. Annu. Rev. Genet. 25, 585-627 (1991). (Pubitemid 21903734)
    • (1991) Annual Review of Genetics , vol.25 , Issue.1 , pp. 585-627
    • Wilson, G.G.1    Murray, N.E.2
  • 51
    • 0025738784 scopus 로고
    • In vivo genetic exchange of a functional domain from a type II A methylase between lactococcal plasmid pTR2030 and a virulent bacteriophage
    • Hill, C., Miller, L. A. & Klaenhammer, T. R. In vivo genetic exchange of a functional domain from a type II A methylase between lactococcal plasmid pTR2030 and a virulent bacteriophage. J. Bacteriol. 173, 4363-4370 (1991).
    • (1991) J. Bacteriol. , vol.173 , pp. 4363-4370
    • Hill, C.1    Miller, L.A.2    Klaenhammer, T.R.3
  • 53
  • 54
    • 0022476166 scopus 로고
    • Modification enhancement by the restriction alleviation protein (Ral) of bacteriophage
    • DOI 10.1016/0022-2836(86)90071-9
    • Loenen, W. A. & Murray, N. E. Modification enhancement by the restriction alleviation protein (Ral) of bacteriophage γ. J. Mol. Biol. 190, 11-22 (1986). (Pubitemid 16000230)
    • (1986) Journal of Molecular Biology , vol.190 , Issue.1 , pp. 11-22
    • Loenen, W.A.M.1    Murray, N.E.2
  • 55
    • 0018942446 scopus 로고
    • The ral gene of phage. I. Identification of a non-essential gene that modulates restriction and modification in E. coli
    • DOI 10.1007/BF00268447
    • Zabeau, M., Friedman, S., Van Montagu, M. & Schell, J. The ral gene of phage γ. I. Identification of a non-essential gene that modulates restriction and modification in E. coli. Mol. Gen. Genet. 179, 63-73 (1980). (Pubitemid 10026241)
    • (1980) Molecular and General Genetics , vol.179 , Issue.1 , pp. 63-73
    • Zabeau, M.1    Friedman, S.2    Van Montagu, M.3    Schell, J.4
  • 56
    • 0029070828 scopus 로고
    • Restriction alleviation and modification enhancement by the Rac prophage of Escherichia coli K-12
    • King, G. & Murray, N. E. Restriction alleviation and modification enhancement by the Rac prophage of Escherichia coli K-12. Mol. Microbiol. 16, 769-777 (1995).
    • (1995) Mol. Microbiol. , vol.16 , pp. 769-777
    • King, G.1    Murray, N.E.2
  • 57
    • 0029055234 scopus 로고
    • Phage T4-coded Stp: Double-edged effector of coupled DNA and tRNA-restriction systems
    • Penner, M., Morad, I., Snyder, L. & Kaufmann, G. Phage T4-coded Stp: double-edged effector of coupled DNA and tRNA-restriction systems. J. Mol. Biol. 249, 857-868 (1995).
    • (1995) J. Mol. Biol. , vol.249 , pp. 857-868
    • Penner, M.1    Morad, I.2    Snyder, L.3    Kaufmann, G.4
  • 58
    • 0017156121 scopus 로고
    • SAMase gene of bacteriophage T3 is responsible for overcoming host restriction
    • Studier, F. W. & Movva, N. R. SAMase gene of bacteriophage T3 is responsible for overcoming host restriction. J. Virol. 19, 136-145 (1976).
    • (1976) J. Virol. , vol.19 , pp. 136-145
    • Studier, F.W.1    Movva, N.R.2
  • 59
    • 78149261827 scopus 로고    scopus 로고
    • The CRISPR/Cas bacterial immune system cleaves bacteriophage and plasmid DNA
    • Garneau, J. E. et al. The CRISPR/Cas bacterial immune system cleaves bacteriophage and plasmid DNA. Nature 468, 67-71 (2010).
    • (2010) Nature , vol.468 , pp. 67-71
    • Garneau, J.E.1
  • 61
    • 84857097177 scopus 로고    scopus 로고
    • RNA-guided genetic silencing systems in bacteria and archaea
    • Wiedenheft, B., Sternberg, S. H. & Doudna, J. A. RNA-guided genetic silencing systems in bacteria and archaea. Nature 482, 331-338 (2012).
    • (2012) Nature , vol.482 , pp. 331-338
    • Wiedenheft, B.1    Sternberg, S.H.2    Doudna, J.A.3
  • 63
    • 80755145195 scopus 로고    scopus 로고
    • The Streptococcus thermophilus CRISPR/Cas system provides immunity in Escherichia coli
    • Sapranauskas, R. et al. The Streptococcus thermophilus CRISPR/Cas system provides immunity in Escherichia coli. Nucleic Acids Res. 39, 9275- 9282 (2011).
    • (2011) Nucleic Acids Res. , vol.39 , pp. 9275-9282
    • Sapranauskas, R.1
  • 64
    • 79959963663 scopus 로고    scopus 로고
    • Interference by clustered regularly interspaced short palindromic repeat (CRISPR) RNA is governed by a seed sequence
    • Semenova, E. et al. Interference by clustered regularly interspaced short palindromic repeat (CRISPR) RNA is governed by a seed sequence. Proc. Natl Acad. Sci. USA 108, 10098-10103 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 10098-10103
    • Semenova, E.1
  • 65
    • 84864864464 scopus 로고    scopus 로고
    • Molecular memory of prior infections activates the CRISPR/Cas adaptive bacterial immunity system
    • Datsenko, K. A. et al. Molecular memory of prior infections activates the CRISPR/Cas adaptive bacterial immunity system. Nature Commun. 3, 945 (2012).
    • (2012) Nature Commun. , vol.3 , pp. 945
    • Datsenko, K.A.1
  • 66
    • 84868118560 scopus 로고    scopus 로고
    • Function and regulation of clustered regularly interspaced short palindromic repeats (CRISPR) / CRISPR Associated (Cas) systems
    • Richter, C., Chang, J. T. & Fineran, P. C. Function and regulation of clustered regularly interspaced short palindromic repeats (CRISPR) / CRISPR Associated (Cas) systems. Viruses 4, 2291-2311 (2012).
    • (2012) Viruses , vol.4 , pp. 2291-2311
    • Richter, C.1    Chang, J.T.2    Fineran, P.C.3
  • 67
    • 84876001507 scopus 로고    scopus 로고
    • The population and evolutionary dynamics of phage and bacteria with CRISPR-mediated immunity
    • Levin, B. R., Moineau, S., Bushman, M. & Barrangou, R. The population and evolutionary dynamics of phage and bacteria with CRISPR-mediated immunity. PLoS Genet. 9, e1003312 (2013).
    • (2013) PLoS Genet. , vol.9
    • Levin, B.R.1    Moineau, S.2    Bushman, M.3    Barrangou, R.4
  • 68
    • 84872607723 scopus 로고    scopus 로고
    • Bacteriophage genes that inactivate the CRISPR/Cas bacterial immune system
    • Bondy-Denomy, J., Pawluk, A., Maxwell, K. L. & Davidson, A. R. Bacteriophage genes that inactivate the CRISPR/Cas bacterial immune system. Nature 493, 429-432 (2013).
    • (2013) Nature , vol.493 , pp. 429-432
    • Bondy-Denomy, J.1    Pawluk, A.2    Maxwell, K.L.3    Davidson, A.R.4
  • 69
    • 84879032013 scopus 로고    scopus 로고
    • In defense of phage: Viral suppressors of CRISPR-mediated adaptive immunity in bacteria
    • Wiedenheft, B. In defense of phage: viral suppressors of CRISPR-mediated adaptive immunity in bacteria. RNA Biol. 10, 886-890 (2013).
    • (2013) RNA Biol. , vol.10 , pp. 886-890
    • Wiedenheft, B.1
  • 70
    • 84874388110 scopus 로고    scopus 로고
    • A bacteriophage encodes its own CRISPR/ Cas adaptive response to evade host innate immunity
    • Seed, K. D., Lazinski, D. W., Calderwood, S. B. & Camilli, A. A bacteriophage encodes its own CRISPR/ Cas adaptive response to evade host innate immunity. Nature 494, 489-491 (2013).
    • (2013) Nature , vol.494 , pp. 489-491
    • Seed, K.D.1    Lazinski, D.W.2    Calderwood, S.B.3    Camilli, A.4
  • 71
    • 84874358510 scopus 로고    scopus 로고
    • Virology: Phages hijack a host's defence
    • Villion, M. & Moineau, S. Virology: phages hijack a host's defence. Nature 494, 433-434 (2013).
    • (2013) Nature , vol.494 , pp. 433-434
    • Villion, M.1    Moineau, S.2
  • 72
    • 84867049470 scopus 로고    scopus 로고
    • Staphylococcal pathogenicity island interference with helper phage reproduction is a paradigm of molecular parasitism
    • Ram, G. et al. Staphylococcal pathogenicity island interference with helper phage reproduction is a paradigm of molecular parasitism. Proc. Natl Acad. Sci. USA 109, 16300-16305 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 16300-16305
    • Ram, G.1
  • 73
    • 0025739484 scopus 로고
    • Host-parasite interactions: Recent developments in the genetics of abortive phage infections
    • Molineux, I. J. Host-parasite interactions: recent developments in the genetics of abortive phage infections. New Biol. 3, 230-236 (1991).
    • (1991) New Biol. , vol.3 , pp. 230-236
    • Molineux, I.J.1
  • 74
    • 0028953424 scopus 로고
    • Phage-exclusion enzymes: A bonanza of biochemical and cell biology reagents?
    • Snyder, L. Phage-exclusion enzymes: a bonanza of biochemical and cell biology reagents? Mol. Microbiol. 15, 415-420 (1995).
    • (1995) Mol. Microbiol. , vol.15 , pp. 415-420
    • Snyder, L.1
  • 75
    • 0038216560 scopus 로고    scopus 로고
    • Stationary phase-like properties of the bacteriophage " Rex exclusion phenotype
    • Slavcev, R. A. & Hayes, S. Stationary phase-like properties of the bacteriophage lambda Rex exclusion phenotype. Mol. Genet. Genom. 269, 40-48 (2003). (Pubitemid 36560679)
    • (2003) Molecular Genetics and Genomics , vol.269 , Issue.1 , pp. 40-48
    • Slavcev, R.A.1    Hayes, S.2
  • 76
    • 77958571327 scopus 로고    scopus 로고
    • Transcriptional control in the prereplicative phase of T4 development
    • Hinton, D. M. Transcriptional control in the prereplicative phase of T4 development. Virol. J. 7, 289 (2010).
    • (2010) Virol. J. , vol.7 , pp. 289
    • Hinton, D.M.1
  • 77
    • 0023502391 scopus 로고
    • Wild-type bacteriophage T4 is restricted by the γ Rex genes
    • Shinedling, S., Parma, D. & Gold, L. Wild-type bacteriophage T4 is restricted by the γ Rex genes. J. Virol. 61, 3790-3794 (1987).
    • (1987) Rex Genes. J. Virol. , vol.61 , pp. 3790-3794
    • Shinedling, S.1    Parma, D.2    Gold, L.3
  • 79
    • 0025309798 scopus 로고
    • A site in the T4 bacteriophage major head protein gene that can promote the inhibition of all translation in Escherichia coli
    • DOI 10.1016/S0022-2836(05)80209-8
    • Bergsland, K. J., Kao, C., Yu, Y. T., Gulati, R. & Snyder, L. A site in the T4 bacteriophage major head protein gene that can promote the inhibition of all translation in Escherichia coli. J. Mol. Biol. 213, 477-494 (1990). (Pubitemid 20194527)
    • (1990) Journal of Molecular Biology , vol.213 , Issue.3 , pp. 477-494
    • Bergsland, K.J.1    Kao, C.2    Nicco Yu, Y.-T.3    Gulati, R.4    Snyder, L.5
  • 80
    • 0034725704 scopus 로고    scopus 로고
    • The major head protein of bacteriophage T4 binds specifically to elongation factor Tu
    • DOI 10.1074/jbc.M002546200
    • Bingham, R., Ekunwe, S. I., Falk, S., Snyder, L. & Kleanthous, C. The major head protein of bacteriophage T4 binds specifically to elongation factor Tu. J. Biol. Chem. 275, 23219-23226 (2000). (Pubitemid 30646219)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.30 , pp. 23219-23226
    • Bingham, R.1    Ekunwe, S.I.N.2    Falk, S.3    Snyder, L.4    Kleanthous, C.5
  • 81
    • 0028120890 scopus 로고
    • Translation elongation factor Tu cleaved by a phage-exclusion system
    • Yu, Y. T. & Snyder, L. Translation elongation factor Tu cleaved by a phage-exclusion system. Proc. Natl Acad. Sci. USA 91, 802-806 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 802-806
    • Yu, Y.T.1    Snyder, L.2
  • 82
    • 0020051892 scopus 로고
    • The gol site: A cis-acting bacteriophage T4 regulatory region that can affect expression of all the T4 late genes
    • DOI 10.1016/0022-2836(82)90478-8
    • Champness, W. C. & Snyder, L. The gol site: a cis-acting bacteriophage T4 regulatory region that can affect expression of all the T4 late genes. J. Mol. Biol. 155, 395-407 (1982). (Pubitemid 12117708)
    • (1982) Journal of Molecular Biology , vol.155 , Issue.4 , pp. 395-407
    • Champness, W.C.1    Snyder, L.2
  • 83
    • 22544481439 scopus 로고    scopus 로고
    • Phage abortive infection in lactococci: Variations on a theme
    • DOI 10.1016/j.mib.2005.06.006, PII S1369527405000809, Host-Microbe Interactions: Fungi / Parasites
    • Chopin, M. C., Chopin, A. & Bidnenko, E. Phage abortive infection in lactococci: variations on a theme. Curr. Opin. Microbiol. 8, 473-479 (2005). (Pubitemid 41021910)
    • (2005) Current Opinion in Microbiology , vol.8 , Issue.4 , pp. 473-479
    • Chopin, M.-C.1    Chopin, A.2    Bidnenko, E.3
  • 84
    • 84873455145 scopus 로고    scopus 로고
    • Structure and activity of AbiQ, a lactococcal endoribonuclease belonging to the type III toxin- antitoxin system
    • Samson, J. E., Spinelli, S., Cambillau, C. & Moineau, S. Structure and activity of AbiQ, a lactococcal endoribonuclease belonging to the type III toxin- antitoxin system. Mol. Microbiol. 87, 756-768 (2013).
    • (2013) Mol. Microbiol. , vol.87 , pp. 756-768
    • Samson, J.E.1    Spinelli, S.2    Cambillau, C.3    Moineau, S.4
  • 85
    • 0029007417 scopus 로고
    • Phage operon involved in sensitivity to the Lactococcus lactis abortive infection mechanism AbiD1
    • Bidnenko, E., Ehrlich, D. & Chopin, M. C. Phage operon involved in sensitivity to the Lactococcus lactis abortive infection mechanism AbiD1. J. Bacteriol. 177, 3824-3829 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 3824-3829
    • Bidnenko, E.1    Ehrlich, D.2    Chopin, M.C.3
  • 86
    • 0031858916 scopus 로고    scopus 로고
    • Lactococcus lactis phage operon coding for an endonuclease homologous to RuvC
    • DOI 10.1046/j.1365-2958.1998.00845.x
    • Bidnenko, E., Ehrlich, S. D. & Chopin, M. C. Lactococcus lactis phage operon coding for an endonuclease homologous to RuvC. Mol. Microbiol. 28, 823-834 (1998). (Pubitemid 28234391)
    • (1998) Molecular Microbiology , vol.28 , Issue.4 , pp. 823-834
    • Bidnenko, E.1    Ehrlich, S.D.2    Chopin, M.-C.3
  • 87
    • 63449102824 scopus 로고    scopus 로고
    • Activation of mRNA translation by phage protein and low temperature: The case of Lactococcus lactis abortive infection system AbiD1
    • Bidnenko, E., Chopin, A., Ehrlich, S. D. & Chopin, M. C. Activation of mRNA translation by phage protein and low temperature: the case of Lactococcus lactis abortive infection system AbiD1. BMC Mol. Biol. 10, 4 (2009).
    • (2009) BMC Mol. Biol. , vol.10 , pp. 4
    • Bidnenko, E.1    Chopin, A.2    Ehrlich, S.D.3    Chopin, M.C.4
  • 88
    • 80053182210 scopus 로고    scopus 로고
    • A reverse transcriptase-related protein mediates phage resistance and polymerizes untemplated DNA in vitro
    • Wang, C. et al. A reverse transcriptase-related protein mediates phage resistance and polymerizes untemplated DNA in vitro. Nucleic Acids Res. 39, 7620-7629 (2011).
    • (2011) Nucleic Acids Res. , vol.39 , pp. 7620-7629
    • Wang, C.1
  • 89
    • 0034712773 scopus 로고    scopus 로고
    • Homologous recombination between a lactococcal bacteriophage and the chromosome of its host strain
    • DOI 10.1006/viro.2000.0226
    • Bouchard, J. D. & Moineau, S. Homologous recombination between a lactococcal bacteriophage and the chromosome of its host strain. Virology 270, 65-75 (2000). (Pubitemid 30256540)
    • (2000) Virology , vol.270 , Issue.1 , pp. 65-75
    • Bouchard, J.D.1    Moineau, S.2
  • 90
    • 2442662866 scopus 로고    scopus 로고
    • Lactococcal phage genes involved in sensitivity to AbiK and their relation to single-strand annealing proteins
    • DOI 10.1128/JB.186.11.3649-3652.2004
    • Bouchard, J. D. & Moineau, S. Lactococcal phage genes involved in sensitivity to AbiK and their relation to single-strand annealing proteins. J. Bacteriol. 186, 3649-3652 (2004). (Pubitemid 38661563)
    • (2004) Journal of Bacteriology , vol.186 , Issue.11 , pp. 3649-3652
    • Bouchard, J.D.1    Moineau, S.2
  • 91
    • 33846932976 scopus 로고    scopus 로고
    • Abortive infection mechanisms and prophage sequences significantly influence the genetic makeup of emerging lytic lactococcal phages
    • DOI 10.1128/JB.01111-06
    • Labrie, S. J. & Moineau, S. Abortive infection mechanisms and prophage sequences significantly influence the genetic make-up of emerging lytic lactococcal phages. J. Bacteriol. 189, 1482-1487 (2007). (Pubitemid 46239773)
    • (2007) Journal of Bacteriology , vol.189 , Issue.4 , pp. 1482-1487
    • Labrie, S.J.1    Moineau, S.2
  • 92
    • 77952581755 scopus 로고    scopus 로고
    • Deciphering the function of lactococcal phage ul36 Sak domains
    • Scaltriti, E. et al. Deciphering the function of lactococcal phage ul36 Sak domains. J. Struct. Biol. 170, 462-469 (2010).
    • (2010) J. Struct. Biol. , vol.170 , pp. 462-469
    • Scaltriti, E.1
  • 93
    • 79953058659 scopus 로고    scopus 로고
    • Lactococcal phage p2 ORF35-Sak3 is an ATPase involved in DNA recombination and AbiK mechanism
    • Scaltriti, E. et al. Lactococcal phage p2 ORF35-Sak3 is an ATPase involved in DNA recombination and AbiK mechanism. Mol. Microbiol. 80, 102-116 (2011).
    • (2011) Mol. Microbiol. , vol.80 , pp. 102-116
    • Scaltriti, E.1
  • 94
    • 64749089552 scopus 로고    scopus 로고
    • Identification and characterization of the phage gene sav, involved in sensitivity to the lactococcal abortive infection mechanism AbiV
    • Haaber, J., Rousseau, G. M., Hammer, K. & Moineau, S. Identification and characterization of the phage gene sav, involved in sensitivity to the lactococcal abortive infection mechanism AbiV. Appl. Environ. Microbiol. 75, 2484-2494 (2009).
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 2484-2494
    • Haaber, J.1    Rousseau, G.M.2    Hammer, K.3    Moineau, S.4
  • 95
    • 78149427597 scopus 로고    scopus 로고
    • Lactococcal abortive infection protein AbiV interacts directly with the phage protein SaV and prevents translation of phage proteins
    • Haaber, J. et al. Lactococcal abortive infection protein AbiV interacts directly with the phage protein SaV and prevents translation of phage proteins. Appl. Environ. Microbiol. 76, 7085-7092 (2010).
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 7085-7092
    • Haaber, J.1
  • 96
    • 84868313344 scopus 로고    scopus 로고
    • Involvement of the major capsid protein and two early-expressed phage genes in the activity of the lactococcal abortive infection mechanism AbiT
    • Labrie, S. J. et al. Involvement of the major capsid protein and two early-expressed phage genes in the activity of the lactococcal abortive infection mechanism AbiT. Appl. Environ. Microbiol. 78, 6890-6899 (2012).
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 6890-6899
    • Labrie, S.J.1
  • 97
    • 0036843003 scopus 로고    scopus 로고
    • Characterization of the two-component abortive phage infection mechanism abit from Lactococcus lactis
    • DOI 10.1128/JB.184.22.6325-6332.2002
    • Bouchard, J. D., Dion, E., Bissonnette, F. & Moineau, S. Characterization of the two-component abortive phage infection mechanism AbiT from Lactococcus lactis. J. Bacteriol. 184, 6325-6332 (2002). (Pubitemid 35265913)
    • (2002) Journal of Bacteriology , vol.184 , Issue.22 , pp. 6325-6332
    • Bouchard, J.D.1    Dion, E.2    Bissonnette, F.3    Moineau, S.4
  • 98
    • 80755144025 scopus 로고    scopus 로고
    • Toxin-antitoxin systems in bacteria and archaea
    • Yamaguchi, Y., Park, J. H. & Inouye, M. Toxin-antitoxin systems in bacteria and archaea. Annu. Rev. Genet. 45, 61-79 (2011).
    • (2011) Annu. Rev. Genet. , vol.45 , pp. 61-79
    • Yamaguchi, Y.1    Park, J.H.2    Inouye, M.3
  • 99
    • 84861347512 scopus 로고    scopus 로고
    • YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ, antagonizing the CbtA (YeeV) toxicity in Escherichia coli
    • Masuda, H., Tan, Q., Awano, N., Wu, K. P. & Inouye, M. YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ, antagonizing the CbtA (YeeV) toxicity in Escherichia coli. Mol. Microbiol. 84, 979-989 (2012).
    • (2012) Mol. Microbiol. , vol.84 , pp. 979-989
    • Masuda, H.1    Tan, Q.2    Awano, N.3    Wu, K.P.4    Inouye, M.5
  • 100
    • 84870279994 scopus 로고    scopus 로고
    • A new type v toxin-antitoxin system where mRNA for toxin GhoT is cleaved by antitoxin GhoS
    • Wang, X. et al. A new type V toxin-antitoxin system where mRNA for toxin GhoT is cleaved by antitoxin GhoS. Nature Chem. Biol. 8, 855-861 (2012).
    • (2012) Nature Chem. Biol. , vol.8 , pp. 855-861
    • Wang, X.1
  • 101
    • 84876095374 scopus 로고    scopus 로고
    • Discovery of functional toxin/antitoxin systems in bacteria by shotgun cloning
    • Sberro, H. et al. Discovery of functional toxin/antitoxin systems in bacteria by shotgun cloning. Mol. Cell. 50, 136-148 (2013).
    • (2013) Mol. Cell. , vol.50 , pp. 136-148
    • Sberro, H.1
  • 102
    • 78951480425 scopus 로고    scopus 로고
    • Escherichia coli rnlA and rnlB compose a novel toxin-antitoxin system
    • Koga, M., Otsuka, Y., Lemire, S. & Yonesaki, T. Escherichia coli rnlA and rnlB compose a novel toxin-antitoxin system. Genetics 187, 123-130 (2011).
    • (2011) Genetics , vol.187 , pp. 123-130
    • Koga, M.1    Otsuka, Y.2    Lemire, S.3    Yonesaki, T.4
  • 103
    • 84856573166 scopus 로고    scopus 로고
    • Dmd of bacteriophage T4 functions as an antitoxin against Escherichia coli LsoA and RnlA toxins
    • Otsuka, Y. & Yonesaki, T. Dmd of bacteriophage T4 functions as an antitoxin against Escherichia coli LsoA and RnlA toxins. Mol. Microbiol. 83, 669-681 (2012).
    • (2012) Mol. Microbiol. , vol.83 , pp. 669-681
    • Otsuka, Y.1    Yonesaki, T.2
  • 104
    • 58849150431 scopus 로고    scopus 로고
    • The phage abortive infection system, ToxIN, functions as a protein-RNA toxin- antitoxin pair
    • Fineran, P. C. et al. The phage abortive infection system, ToxIN, functions as a protein-RNA toxin- antitoxin pair. Proc. Natl Acad. Sci. USA 106, 894-899 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 894-899
    • Fineran, P.C.1
  • 105
    • 79551624663 scopus 로고    scopus 로고
    • A processed noncoding RNA regulates an altruistic bacterial antiviral system
    • Blower, T. R. et al. A processed noncoding RNA regulates an altruistic bacterial antiviral system. Nature Struct. Mol. Biol. 18, 185-190 (2011).
    • (2011) Nature Struct. Mol. Biol. , vol.18 , pp. 185-190
    • Blower, T.R.1
  • 106
    • 84872541994 scopus 로고    scopus 로고
    • Selectivity and self-assembly in the control of a bacterial toxin by an antitoxic noncoding RNA pseudoknot
    • Short, F. L. et al. Selectivity and self-assembly in the control of a bacterial toxin by an antitoxic noncoding RNA pseudoknot. Proc. Natl Acad. Sci. USA 110, E241-E249 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110
    • Short, F.L.1
  • 107
    • 84868095928 scopus 로고    scopus 로고
    • Viral evasion of a bacterial suicide system by RNA-based molecular mimicry enables infectious altruism
    • Blower, T. R., Evans, T. J., Przybilski, R., Fineran, P. C. & Salmond, G. P. Viral evasion of a bacterial suicide system by RNA-based molecular mimicry enables infectious altruism. PLoS Genet. 8, e1003023 (2012).
    • (2012) PLoS Genet. , vol.8
    • Blower, T.R.1    Evans, T.J.2    Przybilski, R.3    Fineran, P.C.4    Salmond, G.P.5
  • 109
    • 84883545198 scopus 로고    scopus 로고
    • Effect of the abortive infection mechanism and type III toxin/ antitoxin system AbiQ on the lytic cycle of Lactococcus lactis phages
    • Samson, J. E., Belanger, M. & Moineau, S. Effect of the abortive infection mechanism and type III toxin/ antitoxin system AbiQ on the lytic cycle of Lactococcus lactis phages. J. Bacteriol. http://dx.doi.org/10.1128/JB.00296- 13 (2013).
    • (2013) J. Bacteriol.
    • Samson, J.E.1    Belanger, M.2    Moineau, S.3
  • 111
    • 84875092761 scopus 로고    scopus 로고
    • Virus-host swinging party in the oceans: Incorporating biological complexity into paradigms of antagonistic coexistence
    • Avrani, S., Schwartz, D. A. & Lindell, D. Virus-host swinging party in the oceans: incorporating biological complexity into paradigms of antagonistic coexistence. Mob. Genet. Elements 2, 88-95 (2012).
    • (2012) Mob. Genet. Elements , vol.2 , pp. 88-95
    • Avrani, S.1    Schwartz, D.A.2    Lindell, D.3
  • 113
    • 84872024771 scopus 로고    scopus 로고
    • Competition and the origins of novelty: Experimental evolution of niche-width expansion in a virus
    • Bono, L. M., Gensel, C. L., Pfennig, D. W. & Burch, C. L. Competition and the origins of novelty: experimental evolution of niche-width expansion in a virus. Biol. Lett. 9, 20120616 (2013).
    • (2013) Biol. Lett. , vol.9 , pp. 20120616
    • Bono, L.M.1    Gensel, C.L.2    Pfennig, D.W.3    Burch, C.L.4
  • 114
    • 78650045540 scopus 로고    scopus 로고
    • The phage-host arms race: Shaping the evolution of microbes
    • Stern, A. & Sorek, R. The phage-host arms race: shaping the evolution of microbes. Bioessays 33, 43-51 (2011).
    • (2011) Bioessays , vol.33 , pp. 43-51
    • Stern, A.1    Sorek, R.2
  • 115
    • 84884289136 scopus 로고    scopus 로고
    • What can phages tell us about host-pathogen coevolution?
    • Dennehy, J. J. What can phages tell us about host-pathogen coevolution? Int. J. Evol. Biol. 2012, 396165 (2012).
    • (2012) Int. J. Evol. Biol. , vol.2012 , pp. 396165
    • Dennehy, J.J.1
  • 116
    • 60549087903 scopus 로고    scopus 로고
    • Phage evolution and ecology
    • Abedon, S. T. Phage evolution and ecology. Adv. Appl. Microbiol. 67, 1-45 (2009).
    • (2009) Adv. Appl. Microbiol. , vol.67 , pp. 1-45
    • Abedon, S.T.1
  • 117
    • 84874853719 scopus 로고    scopus 로고
    • Bacteriophages in food fermentations: New frontiers in a continuous arms race
    • Samson, J. E. & Moineau, S. Bacteriophages in food fermentations: new frontiers in a continuous arms race. Annu. Rev. Food Sci. Technol. 4, 347-368 (2013).
    • (2013) Annu. Rev. Food Sci. Technol. , vol.4 , pp. 347-368
    • Samson, J.E.1    Moineau, S.2
  • 118
    • 79956157571 scopus 로고    scopus 로고
    • Evolution and classification of the CRISP-Cas systems
    • Makarova, K. S. et al. Evolution and classification of the CRISP-Cas systems. Nature Rev. Microbiol. 9, 467-477 (2011).
    • (2011) Nature Rev. Microbiol. , vol.9 , pp. 467-477
    • Makarova, K.S.1
  • 119
    • 79953250082 scopus 로고    scopus 로고
    • CRISPR RNA maturation by trans-encoded small RNA and host factor RNase III
    • Deltcheva, E. et al. CRISPR RNA maturation by trans-encoded small RNA and host factor RNase III. Nature 471, 602-607 (2011).
    • (2011) Nature , vol.471 , pp. 602-607
    • Deltcheva, E.1
  • 120
    • 84864085433 scopus 로고    scopus 로고
    • Cleavage of phage DNA by the Streptococcus thermophilus CRISPR3-Cas system
    • Magadan, A. H., Dupuis, M. E., Villion, M. & Moineau, S. Cleavage of phage DNA by the Streptococcus thermophilus CRISPR3-Cas system. PLoS ONE 7, e40913 (2012).
    • (2012) PLoS ONE , vol.7
    • Magadan, A.H.1    Dupuis, M.E.2    Villion, M.3    Moineau, S.4
  • 121
    • 84868306630 scopus 로고    scopus 로고
    • Substitutions in the Escherichia coli RNA polymerase inhibitor T7 Gp2 that allow inhibition of transcription when the primary interaction interface between Gp2 and RNA polymerase becomes compromised
    • Shadrin, A., Sheppard, C., Severinov, K., Matthews, S. & Wigneshweraraj, S. Substitutions in the Escherichia coli RNA polymerase inhibitor T7 Gp2 that allow inhibition of transcription when the primary interaction interface between Gp2 and RNA polymerase becomes compromised. Microbiology 158, 2753-2764 (2012).
    • (2012) Microbiology , vol.158 , pp. 2753-2764
    • Shadrin, A.1    Sheppard, C.2    Severinov, K.3    Matthews, S.4    Wigneshweraraj, S.5
  • 124
    • 0034487424 scopus 로고    scopus 로고
    • Roles of molecular chaperones in cytoplasmic protein folding
    • DOI 10.1006/scdb.1999.0347
    • Agashe, V. R. & Hartl, F. U. Roles of molecular chaperones in cytoplasmic protein folding. Semin. Cell Dev. Biol. 11, 15-25 (2000). (Pubitemid 32096090)
    • (2000) Seminars in Cell and Developmental Biology , vol.11 , Issue.1 , pp. 15-25
    • Agashe, V.R.1    Hartl, F.-U.2
  • 125
    • 0017187520 scopus 로고
    • A genetic analysis of bacteriophage γ head assembly
    • Sternberg, N. A genetic analysis of bacteriophage γ head assembly. Virology 71, 568-582 (1976).
    • (1976) Virology , vol.71 , pp. 568-582
    • Sternberg, N.1


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