메뉴 건너뛰기




Volumn 477, Issue , 2015, Pages 110-118

Receptor binding proteins of Listeria monocytogenes bacteriophages A118 and P35 recognize serovar-specific teichoic acids

Author keywords

Baseplate model; Caudovirales; Fluorescence microscopy; Immuno gold labeling; Phage adsorption; Phage crosslink

Indexed keywords

BINDING PROTEIN; N ACETYLGLUCOSAMINE; PROTEIN GP16; PROTEIN GP18; PROTEIN GP19; PROTEIN GP20; RECEPTOR BINDING PROTEIN; RHAMNOSE; TEICHOIC ACID; UNCLASSIFIED DRUG; VIRUS PROTEIN; VIRAL PROTEIN; VIRUS RECEPTOR;

EID: 84929991156     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2014.12.035     Document Type: Article
Times cited : (44)

References (78)
  • 3
    • 47249159073 scopus 로고    scopus 로고
    • Phage SPP1 reversible adsorption to Bacillus subtilis cell wall teichoic acids accelerates virus recognition of membrane receptor YueB
    • Baptista C., Santos M.A., Sao-Jose C. Phage SPP1 reversible adsorption to Bacillus subtilis cell wall teichoic acids accelerates virus recognition of membrane receptor YueB. J. Bacteriol. 2008, 190:4989-4996.
    • (2008) J. Bacteriol. , vol.190 , pp. 4989-4996
    • Baptista, C.1    Santos, M.A.2    Sao-Jose, C.3
  • 4
    • 47249162887 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli phage HK620 tailspike: podoviral tailspike endoglycosidase modules are evolutionarily related
    • Barbirz S., Muller J.J., Uetrecht C., Clark A.J., Heinemann U., Seckler R. Crystal structure of Escherichia coli phage HK620 tailspike: podoviral tailspike endoglycosidase modules are evolutionarily related. Mol. Microbiol. 2008, 69:303-316.
    • (2008) Mol. Microbiol. , vol.69 , pp. 303-316
    • Barbirz, S.1    Muller, J.J.2    Uetrecht, C.3    Clark, A.J.4    Heinemann, U.5    Seckler, R.6
  • 6
    • 84939841852 scopus 로고    scopus 로고
    • Visualizing a complete Siphoviridae by single-particle electron microscopy: the structure of lactococcal phage TP901-1
    • Bebeacua C., Lai L., Vegge C.S., Brondsted L., van Heel M., Veesler D., Cambillau C. Visualizing a complete Siphoviridae by single-particle electron microscopy: the structure of lactococcal phage TP901-1. J. Virol. 2012.
    • (2012) J. Virol.
    • Bebeacua, C.1    Lai, L.2    Vegge, C.S.3    Brondsted, L.4    van Heel, M.5    Veesler, D.6    Cambillau, C.7
  • 9
    • 46649087608 scopus 로고    scopus 로고
    • Phage T5 straight tail fiber is a multifunctional protein acting as a tape measure and carrying fusogenic and muralytic activities
    • Boulanger P., Jacquot P., Plancon L., Chami M., Engel A., Parquet C., Herbeuval C., Letellier L. Phage T5 straight tail fiber is a multifunctional protein acting as a tape measure and carrying fusogenic and muralytic activities. J. Biol. Chem. 2008, 283:13556-13564.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13556-13564
    • Boulanger, P.1    Jacquot, P.2    Plancon, L.3    Chami, M.4    Engel, A.5    Parquet, C.6    Herbeuval, C.7    Letellier, L.8
  • 11
    • 27744503831 scopus 로고    scopus 로고
    • Bacteriophage P100 for control of Listeria monocytogenes in foods: genome sequence, bioinformatic analyses, oral toxicity study, and application
    • Carlton R.M., Noordman W.H., Biswas B., De Meester E.D., Loessner M.J. Bacteriophage P100 for control of Listeria monocytogenes in foods: genome sequence, bioinformatic analyses, oral toxicity study, and application. Regul. Toxicol. Pharmacol. 2005, 43:301-312.
    • (2005) Regul. Toxicol. Pharmacol. , vol.43 , pp. 301-312
    • Carlton, R.M.1    Noordman, W.H.2    Biswas, B.3    De Meester, E.D.4    Loessner, M.J.5
  • 12
    • 84870625727 scopus 로고    scopus 로고
    • Interaction of bacteriophage l with its E. coli receptor, LamB
    • Chatterjee S., Rothenberg E. Interaction of bacteriophage l with its E. coli receptor, LamB. Viruses 2012, 4:3162-3178.
    • (2012) Viruses , vol.4 , pp. 3162-3178
    • Chatterjee, S.1    Rothenberg, E.2
  • 14
    • 72249094991 scopus 로고    scopus 로고
    • Comparative genome analysis of Listeria bacteriophages reveals extensive mosaicism, programmed translational frameshifting, and a novel prophage insertion site
    • Dorscht J., Klumpp J., Bielmann R., Schmelcher M., Born Y., Zimmer M., Calendar R., Loessner M. Comparative genome analysis of Listeria bacteriophages reveals extensive mosaicism, programmed translational frameshifting, and a novel prophage insertion site. J. Bacteriol. 2009, 191:7206-7215.
    • (2009) J. Bacteriol. , vol.191 , pp. 7206-7215
    • Dorscht, J.1    Klumpp, J.2    Bielmann, R.3    Schmelcher, M.4    Born, Y.5    Zimmer, M.6    Calendar, R.7    Loessner, M.8
  • 15
    • 72249094991 scopus 로고    scopus 로고
    • Comparative genome analysis of Listeria bacteriophages reveals extensive mosaicism, programmed translational frameshifting, and a novel prophage insertion site
    • Dorscht J., Klumpp J., Bielmann R., Schmelcher M., Born Y., Zimmer M., Calendar R., Loessner M.J. Comparative genome analysis of Listeria bacteriophages reveals extensive mosaicism, programmed translational frameshifting, and a novel prophage insertion site. J. Bacteriol. 2009, 191:7206-7215.
    • (2009) J. Bacteriol. , vol.191 , pp. 7206-7215
    • Dorscht, J.1    Klumpp, J.2    Bielmann, R.3    Schmelcher, M.4    Born, Y.5    Zimmer, M.6    Calendar, R.7    Loessner, M.J.8
  • 16
    • 0034897928 scopus 로고    scopus 로고
    • Identification of a genetic determinant responsible for host specificity in Streptococcus thermophilus bacteriophages
    • Duplessis M., Moineau S. Identification of a genetic determinant responsible for host specificity in Streptococcus thermophilus bacteriophages. Mol. Microbiol. 2001, 41:325-336.
    • (2001) Mol. Microbiol. , vol.41 , pp. 325-336
    • Duplessis, M.1    Moineau, S.2
  • 17
    • 8144222607 scopus 로고    scopus 로고
    • Identification of the receptor-binding protein in 936-species lactococcal bacteriophages
    • Dupont K., Vogensen F.K., Neve H., Bresciani J., Josephsen J. Identification of the receptor-binding protein in 936-species lactococcal bacteriophages. Appl. Environ. Microbiol. 2004, 70:5818-5824.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 5818-5824
    • Dupont, K.1    Vogensen, F.K.2    Neve, H.3    Bresciani, J.4    Josephsen, J.5
  • 18
    • 80052741109 scopus 로고    scopus 로고
    • The cell wall binding domain of Listeria bacteriophage endolysin PlyP35 recognizes terminal GlcNAc residues in cell wall teichoic acid
    • Eugster M.R., Haug M.C., Huwiler S.G., Loessner M.J. The cell wall binding domain of Listeria bacteriophage endolysin PlyP35 recognizes terminal GlcNAc residues in cell wall teichoic acid. Mol. Microbiol. 2011, 81:1419-1432.
    • (2011) Mol. Microbiol. , vol.81 , pp. 1419-1432
    • Eugster, M.R.1    Haug, M.C.2    Huwiler, S.G.3    Loessner, M.J.4
  • 19
    • 84871050215 scopus 로고    scopus 로고
    • Wall teichoic acids restrict access of bacteriophage endolysin Ply118, Ply511, and PlyP40 cell wall binding domains to the Listeria monocytogenes peptidoglycan
    • Eugster M.R., Loessner M.J. Wall teichoic acids restrict access of bacteriophage endolysin Ply118, Ply511, and PlyP40 cell wall binding domains to the Listeria monocytogenes peptidoglycan. J. Bacteriol. 2012, 194:6498-6506.
    • (2012) J. Bacteriol. , vol.194 , pp. 6498-6506
    • Eugster, M.R.1    Loessner, M.J.2
  • 20
    • 84939841853 scopus 로고    scopus 로고
    • Bacteriophage predation promotes serovar diversification in Listeria monocytogenes (submitted for publication).
    • Eugster, M.R., Morax, L.S., Huels, V.J., Huwiler, S.G., Leclercq, A., Lecuit, M., Loessner, M.J. Bacteriophage predation promotes serovar diversification in Listeria monocytogenes (submitted for publication).
    • Eugster, M.R.1    Morax, L.S.2    Huels, V.J.3    Huwiler, S.G.4    Leclercq, A.5    Lecuit, M.6    Loessner, M.J.7
  • 21
    • 0025951915 scopus 로고
    • Listeria monocytogenes, a food-borne pathogen
    • Farber J.M., Peterkin P.I. Listeria monocytogenes, a food-borne pathogen. Microbiol. Rev. 1991, 55:476-511.
    • (1991) Microbiol. Rev. , vol.55 , pp. 476-511
    • Farber, J.M.1    Peterkin, P.I.2
  • 22
    • 0023897117 scopus 로고
    • Biochemistry of the cell surface of Listeria strains: a locating general view
    • Fiedler F. Biochemistry of the cell surface of Listeria strains: a locating general view. Infection 1988, 16(Suppl. 2):S92-S97.
    • (1988) Infection , vol.16 , pp. S92-S97
    • Fiedler, F.1
  • 23
    • 84864288397 scopus 로고    scopus 로고
    • New insights into pb5, the receptor binding protein of bacteriophage T5, and its interaction with its Escherichia coli receptor FhuA
    • Flayhan A., Wien F., Paternostre M., Boulanger P., Breyton C. New insights into pb5, the receptor binding protein of bacteriophage T5, and its interaction with its Escherichia coli receptor FhuA. Biochimie 2012, 94:1982-1989.
    • (2012) Biochimie , vol.94 , pp. 1982-1989
    • Flayhan, A.1    Wien, F.2    Paternostre, M.3    Boulanger, P.4    Breyton, C.5
  • 26
    • 0141706513 scopus 로고    scopus 로고
    • Gene cloning, purification, and stoichiometry quantification of phi29 anti-receptor gp12 with potential use as special ligand for gene delivery
    • Guo S., Shu D., Simon M.N., Guo P. Gene cloning, purification, and stoichiometry quantification of phi29 anti-receptor gp12 with potential use as special ligand for gene delivery. Gene 2003, 315:145-152.
    • (2003) Gene , vol.315 , pp. 145-152
    • Guo, S.1    Shu, D.2    Simon, M.N.3    Guo, P.4
  • 28
    • 84869038086 scopus 로고    scopus 로고
    • Reporter bacteriophage A511::celB transduces a hyperthermostable glycosidase from Pyrococcus furiosus for rapid and simple detection of viable Listeria cells
    • Hagens S., De Wouters T., Vollenweider P., Loessner M.J. Reporter bacteriophage A511::celB transduces a hyperthermostable glycosidase from Pyrococcus furiosus for rapid and simple detection of viable Listeria cells. Bacteriophage 2011, 1:143-151.
    • (2011) Bacteriophage , vol.1 , pp. 143-151
    • Hagens, S.1    De Wouters, T.2    Vollenweider, P.3    Loessner, M.J.4
  • 31
    • 0023647163 scopus 로고
    • Determination of bacteriophage lambda tail length by a protein ruler
    • Katsura I. Determination of bacteriophage lambda tail length by a protein ruler. Nature 1987, 327:73-75.
    • (1987) Nature , vol.327 , pp. 73-75
    • Katsura, I.1
  • 32
    • 2442650308 scopus 로고    scopus 로고
    • Bacteriophage Tuc2009 encodes a tail-associated cell wall-degrading activity
    • Kenny J.G., McGrath S., Fitzgerald G.F., van Sinderen D. Bacteriophage Tuc2009 encodes a tail-associated cell wall-degrading activity. J. Bacteriol. 2004, 186:3480-3491.
    • (2004) J. Bacteriol. , vol.186 , pp. 3480-3491
    • Kenny, J.G.1    McGrath, S.2    Fitzgerald, G.F.3    van Sinderen, D.4
  • 33
    • 0028942302 scopus 로고
    • Identification of receptor binding sites by competitive peptide mapping: phages T1, T5, and phi 80 and colicin M bind to the gating loop of FhuA
    • Killmann H., Videnov G., Jung G., Schwarz H., Braun V. Identification of receptor binding sites by competitive peptide mapping: phages T1, T5, and phi 80 and colicin M bind to the gating loop of FhuA. J. Bacteriol. 1995, 177:694-698.
    • (1995) J. Bacteriol. , vol.177 , pp. 694-698
    • Killmann, H.1    Videnov, G.2    Jung, G.3    Schwarz, H.4    Braun, V.5
  • 34
    • 50249163139 scopus 로고    scopus 로고
    • The terminally redundant, nonpermuted genome of Listeria bacteriophage A511: a model for the SPO1-like myoviruses of Gram-positive bacteria
    • Klumpp J., Dorscht J., Lurz R., Bielmann R., Wieland M., Zimmer M., Calendar R., Loessner M.J. The terminally redundant, nonpermuted genome of Listeria bacteriophage A511: a model for the SPO1-like myoviruses of Gram-positive bacteria. J. Bacteriol. 2008, 190:5753-5765.
    • (2008) J. Bacteriol. , vol.190 , pp. 5753-5765
    • Klumpp, J.1    Dorscht, J.2    Lurz, R.3    Bielmann, R.4    Wieland, M.5    Zimmer, M.6    Calendar, R.7    Loessner, M.J.8
  • 37
    • 84874089555 scopus 로고    scopus 로고
    • Listeria weihenstephanensis sp. nov., isolated from the water plant Lemna trisulca taken from a freshwater pond
    • Lang Halter E., Neuhaus K., Scherer S. Listeria weihenstephanensis sp. nov., isolated from the water plant Lemna trisulca taken from a freshwater pond. Int. J. Syst. Evol. Microbiol. 2013, 63:641-647.
    • (2013) Int. J. Syst. Evol. Microbiol. , vol.63 , pp. 641-647
    • Lang Halter, E.1    Neuhaus, K.2    Scherer, S.3
  • 40
    • 0025890182 scopus 로고
    • Improved procedure for bacteriophage typing of Listeria strains and evaluation of new phages
    • Loessner M.J. Improved procedure for bacteriophage typing of Listeria strains and evaluation of new phages. Appl. Environ. Microbiol. 1991, 57:882-884.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 882-884
    • Loessner, M.J.1
  • 41
    • 0025297908 scopus 로고
    • Bacteriophage typing of Listeria species
    • Loessner M.J., Busse M. Bacteriophage typing of Listeria species. Appl. Environ. Microbiol. 1990, 56:1912-1918.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 1912-1918
    • Loessner, M.J.1    Busse, M.2
  • 42
    • 0033959106 scopus 로고    scopus 로고
    • Complete nucleotide sequence, molecular analysis and genome structure of bacteriophage A118 of Listeria monocytogenes: implications for phage evolution
    • Loessner M.J., Inman R.B., Lauer P., Calendar R. Complete nucleotide sequence, molecular analysis and genome structure of bacteriophage A118 of Listeria monocytogenes: implications for phage evolution. Mol. Microbiol. 2000, 35:324-340.
    • (2000) Mol. Microbiol. , vol.35 , pp. 324-340
    • Loessner, M.J.1    Inman, R.B.2    Lauer, P.3    Calendar, R.4
  • 43
    • 0036231904 scopus 로고    scopus 로고
    • C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high-affinity binding to bacterial cell wall carbohydrates
    • Loessner M.J., Kramer K., Ebel F., Scherer S. C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high-affinity binding to bacterial cell wall carbohydrates. Mol. Microbiol. 2002, 44:335-349.
    • (2002) Mol. Microbiol. , vol.44 , pp. 335-349
    • Loessner, M.J.1    Kramer, K.2    Ebel, F.3    Scherer, S.4
  • 44
    • 0029930408 scopus 로고    scopus 로고
    • Construction of luciferase reporter bacteriophage A511::luxAB for rapid and sensitive detection of viable Listeria cells
    • Loessner M.J., Rees C.E., Stewart G.S., Scherer S. Construction of luciferase reporter bacteriophage A511::luxAB for rapid and sensitive detection of viable Listeria cells. Appl. Environ. Microbiol. 1996, 62:1133-1140.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1133-1140
    • Loessner, M.J.1    Rees, C.E.2    Stewart, G.S.3    Scherer, S.4
  • 45
    • 0029122651 scopus 로고
    • Heterogeneous endolysins in Listeria monocytogenes bacteriophages: a new class of enzymes and evidence for conserved holin genes within the siphoviral lysis cassettes
    • Loessner M.J., Wendlinger G., Scherer S. Heterogeneous endolysins in Listeria monocytogenes bacteriophages: a new class of enzymes and evidence for conserved holin genes within the siphoviral lysis cassettes. Mol. Microbiol. 1995, 16:1231-1241.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1231-1241
    • Loessner, M.J.1    Wendlinger, G.2    Scherer, S.3
  • 46
    • 84873474083 scopus 로고    scopus 로고
    • Long tail fibers of the novel broad host range T-even bacteriophage S16 specifically recognize Salmonella OmpC
    • Marti R., Zurfluh K., Hagens S., Pianezzi J., Klumpp J., Loessner M.J. Long tail fibers of the novel broad host range T-even bacteriophage S16 specifically recognize Salmonella OmpC. Mol. Microbiol. 2013, 87:818-834.
    • (2013) Mol. Microbiol. , vol.87 , pp. 818-834
    • Marti, R.1    Zurfluh, K.2    Hagens, S.3    Pianezzi, J.4    Klumpp, J.5    Loessner, M.J.6
  • 48
    • 42949161202 scopus 로고    scopus 로고
    • An intersubunit active site between supercoiled parallel beta helices in the trimeric tailspike endorhamnosidase of Shigella flexneri Phage Sf6
    • Muller J.J., Barbirz S., Heinle K., Freiberg A., Seckler R., Heinemann U. An intersubunit active site between supercoiled parallel beta helices in the trimeric tailspike endorhamnosidase of Shigella flexneri Phage Sf6. Structure 2008, 16:766-775.
    • (2008) Structure , vol.16 , pp. 766-775
    • Muller, J.J.1    Barbirz, S.2    Heinle, K.3    Freiberg, A.4    Seckler, R.5    Heinemann, U.6
  • 49
    • 0031573415 scopus 로고    scopus 로고
    • Comparison of DNA sequences with protein sequences
    • Pearson W.R., Wood T., Zhang Z., Miller W. Comparison of DNA sequences with protein sequences. Genomics 1997, 46:24-36.
    • (1997) Genomics , vol.46 , pp. 24-36
    • Pearson, W.R.1    Wood, T.2    Zhang, Z.3    Miller, W.4
  • 52
    • 84919828897 scopus 로고    scopus 로고
    • Structure and function of bacteriophage T4
    • Rossman M.G., Yap M.L. Structure and function of bacteriophage T4. Future Med. 2014, 9:1319-1327.
    • (2014) Future Med. , vol.9 , pp. 1319-1327
    • Rossman, M.G.1    Yap, M.L.2
  • 54
    • 10044293087 scopus 로고    scopus 로고
    • Bacillus subtilis operon encoding a membrane receptor for bacteriophage SPP1
    • Sao-Jose C., Baptista C., Santos M.A. Bacillus subtilis operon encoding a membrane receptor for bacteriophage SPP1. J. Bacteriol. 2004, 186:8337-8346.
    • (2004) J. Bacteriol. , vol.186 , pp. 8337-8346
    • Sao-Jose, C.1    Baptista, C.2    Santos, M.A.3
  • 55
    • 33744962964 scopus 로고    scopus 로고
    • The ectodomain of the viral receptor YueB forms a fiber that triggers ejection of bacteriophage SPP1 DNA
    • Sao-Jose C., Lhuillier S., Lurz R., Melki R., Lepault J., Santos M.A., Tavares P. The ectodomain of the viral receptor YueB forms a fiber that triggers ejection of bacteriophage SPP1 DNA. J. Biol. Chem. 2006, 281:11464-11470.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11464-11470
    • Sao-Jose, C.1    Lhuillier, S.2    Lurz, R.3    Melki, R.4    Lepault, J.5    Santos, M.A.6    Tavares, P.7
  • 60
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • Soding J. Protein homology detection by HMM-HMM comparison. Bioinformatics 2005, 21:951-960.
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Soding, J.1
  • 61
    • 33744900391 scopus 로고    scopus 로고
    • Modular structure of the receptor binding proteins of Lactococcus lactis phages. The RBP structure of the temperate phage TP901-1
    • Spinelli S., Campanacci V., Blangy S., Moineau S., Tegoni M., Cambillau C. Modular structure of the receptor binding proteins of Lactococcus lactis phages. The RBP structure of the temperate phage TP901-1. J. Biol. Chem. 2006, 281:14256-14262.
    • (2006) J. Biol. Chem. , vol.281 , pp. 14256-14262
    • Spinelli, S.1    Campanacci, V.2    Blangy, S.3    Moineau, S.4    Tegoni, M.5    Cambillau, C.6
  • 62
    • 30044442097 scopus 로고    scopus 로고
    • Lactococcal bacteriophage p2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses
    • Spinelli S., Desmyter A., Verrips C.T., De Haard H.J., Moineau S., Cambillau C. Lactococcal bacteriophage p2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses. Nat. Struct. Mol. Biol. 2006, 13:85-89.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 85-89
    • Spinelli, S.1    Desmyter, A.2    Verrips, C.T.3    De Haard, H.J.4    Moineau, S.5    Cambillau, C.6
  • 65
    • 0037466525 scopus 로고    scopus 로고
    • Identification of the host determinant of two prolate-headed phages infecting Lactococcus lactis
    • Stuer-Lauridsen B., Janzen T., Schnabl J., Johansen E. Identification of the host determinant of two prolate-headed phages infecting Lactococcus lactis. Virology 2003, 309:10-17.
    • (2003) Virology , vol.309 , pp. 10-17
    • Stuer-Lauridsen, B.1    Janzen, T.2    Schnabl, J.3    Johansen, E.4
  • 67
    • 0022666772 scopus 로고
    • Structural studies on teichoic acids in cell walls of several serotypes of Listeria monocytogenes
    • Uchikawa K., Sekikawa I., Azuma I. Structural studies on teichoic acids in cell walls of several serotypes of Listeria monocytogenes. J. Biochem. 1986, 99:315-327.
    • (1986) J. Biochem. , vol.99 , pp. 315-327
    • Uchikawa, K.1    Sekikawa, I.2    Azuma, I.3
  • 69
    • 80052206993 scopus 로고    scopus 로고
    • A common evolutionary origin for tailed-bacteriophage functional modules and bacterial machineries
    • Veesler D., Cambillau C. A common evolutionary origin for tailed-bacteriophage functional modules and bacterial machineries. Microbiol. Mol. Biol. Rev. 2011, 75:423-433.
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 423-433
    • Veesler, D.1    Cambillau, C.2
  • 70
    • 78449264344 scopus 로고    scopus 로고
    • Crystal structure of bacteriophage SPP1 distal tail protein (gp19.1): a baseplate hub paradigm in Gram-positive infecting phages
    • Veesler D., Robin G., Lichiere J., Auzat I., Tavares P., Bron P., Campanacci V., Cambillau C. Crystal structure of bacteriophage SPP1 distal tail protein (gp19.1): a baseplate hub paradigm in Gram-positive infecting phages. J. Biol. Chem. 2010, 285:36666-36673.
    • (2010) J. Biol. Chem. , vol.285 , pp. 36666-36673
    • Veesler, D.1    Robin, G.2    Lichiere, J.3    Auzat, I.4    Tavares, P.5    Bron, P.6    Campanacci, V.7    Cambillau, C.8
  • 72
    • 20444460783 scopus 로고    scopus 로고
    • Structural characterization and assembly of the distal tail structure of the temperate lactococcal bacteriophage TP901-1
    • Vegge C.S., Brondsted L., Neve H., Mc Grath S., van Sinderen D., Vogensen F.K. Structural characterization and assembly of the distal tail structure of the temperate lactococcal bacteriophage TP901-1. J. Bacteriol. 2005, 187:4187-4197.
    • (2005) J. Bacteriol. , vol.187 , pp. 4187-4197
    • Vegge, C.S.1    Brondsted, L.2    Neve, H.3    Mc Grath, S.4    van Sinderen, D.5    Vogensen, F.K.6
  • 73
    • 33644888327 scopus 로고    scopus 로고
    • Identification of the lower baseplate protein as the antireceptor of the temperate lactococcal bacteriophages TP901-1 and Tuc2009
    • Vegge C.S., Vogensen F.K., Mc Grath S., Neve H., van Sinderen D., Brondsted L. Identification of the lower baseplate protein as the antireceptor of the temperate lactococcal bacteriophages TP901-1 and Tuc2009. J. Bacteriol. 2006, 188:55-63.
    • (2006) J. Bacteriol. , vol.188 , pp. 55-63
    • Vegge, C.S.1    Vogensen, F.K.2    Mc Grath, S.3    Neve, H.4    van Sinderen, D.5    Brondsted, L.6
  • 74
    • 0033985920 scopus 로고    scopus 로고
    • The C-terminal portion of the tail fiber protein of bacteriophage lambda is responsible for binding to LamB, its receptor at the surface of Escherichia coli K-12
    • Wang J., Hofnung M., Charbit A. The C-terminal portion of the tail fiber protein of bacteriophage lambda is responsible for binding to LamB, its receptor at the surface of Escherichia coli K-12. J. Bacteriol. 2000, 182:508-512.
    • (2000) J. Bacteriol. , vol.182 , pp. 508-512
    • Wang, J.1    Hofnung, M.2    Charbit, A.3
  • 75
    • 0029914268 scopus 로고    scopus 로고
    • Bacteriophage receptors on Listeria monocytogenes cells are the N-acetylglucosamine and rhamnose substituents of teichoic acids or the peptidoglycan itself
    • Wendlinger G., Loessner M.J., Scherer S. Bacteriophage receptors on Listeria monocytogenes cells are the N-acetylglucosamine and rhamnose substituents of teichoic acids or the peptidoglycan itself. Microbiology 1996, 142(Part 4):985-992.
    • (1996) Microbiology , vol.142 , Issue.PART. 4 , pp. 985-992
    • Wendlinger, G.1    Loessner, M.J.2    Scherer, S.3
  • 76
    • 0028029005 scopus 로고
    • Adsorption of bacteriophage lambda on the LamB protein of Escherichia coli K-12: point mutations in gene J of lambda responsible for extended host range
    • Werts C., Michel V., Hofnung M., Charbit A. Adsorption of bacteriophage lambda on the LamB protein of Escherichia coli K-12: point mutations in gene J of lambda responsible for extended host range. J. Bacteriol. 1994, 176:941-947.
    • (1994) J. Bacteriol. , vol.176 , pp. 941-947
    • Werts, C.1    Michel, V.2    Hofnung, M.3    Charbit, A.4
  • 77
    • 0014748362 scopus 로고
    • Rapid bacteriophage sedimentation in the presence of polyethylene glycol and its application to large-scale virus purification
    • Yamamoto K.R., Alberts B.M., Benzinger R., Lawhorne L., Treiber G. Rapid bacteriophage sedimentation in the presence of polyethylene glycol and its application to large-scale virus purification. Virology 1970, 40:734-744.
    • (1970) Virology , vol.40 , pp. 734-744
    • Yamamoto, K.R.1    Alberts, B.M.2    Benzinger, R.3    Lawhorne, L.4    Treiber, G.5
  • 78
    • 0026500941 scopus 로고
    • Classification of virulent and temperate bacteriophages of Listeria spp. on the basis of morphology and protein analysis
    • Zink R., Loessner M.J. Classification of virulent and temperate bacteriophages of Listeria spp. on the basis of morphology and protein analysis. Appl. Environ. Microbiol. 1992, 58:296-302.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 296-302
    • Zink, R.1    Loessner, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.