메뉴 건너뛰기




Volumn 88, Issue 12, 2014, Pages 7005-7015

Molecular insights on the recognition of a Lactococcus lactis cell wall pellicle by the phage 1358 receptor binding protein

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; GLUCOSE 1 PHOSPHATE; MONOMER; MONOSACCHARIDE; PHAGE 1358 RECEPTOR BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 84901352128     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00739-14     Document Type: Article
Times cited : (59)

References (49)
  • 1
    • 80052248928 scopus 로고    scopus 로고
    • Bacteriophages of lactic acid bacteria and their impact on milk fermentations
    • Garneau JE, Moineau S. 2011. Bacteriophages of lactic acid bacteria and their impact on milk fermentations. Microb. Cell Fact 10(Suppl 1):S20. http://dx.doi.org/10.1186/1475-2859-10-S1-S20.
    • (2011) Microb. Cell Fact , vol.10 , Issue.SUPPL. 1
    • Garneau, J.E.1    Moineau, S.2
  • 2
    • 84858215696 scopus 로고    scopus 로고
    • Bacteriophage electron microscopy
    • Ackermann HW. 2012. Bacteriophage electron microscopy. Adv. Virus Res. 82:1-32. http://dx.doi.org/10.1016/B978-0-12-394621-8.00017-0.
    • (2012) Adv. Virus Res. , vol.82 , pp. 1-32
    • Ackermann, H.W.1
  • 5
    • 0023647163 scopus 로고
    • Determination of bacteriophage lambda tail length by a protein ruler
    • Katsura I. 1987. Determination of bacteriophage lambda tail length by a protein ruler. Nature 327:73-75. http://dx.doi.org/10.1038/327073a0.
    • (1987) Nature , vol.327 , pp. 73-75
    • Katsura, I.1
  • 6
    • 84871999238 scopus 로고    scopus 로고
    • Visualizing a complete Siphoviridae member by single-particle electron microscopy: the structure of lactococcal phage TP091-1
    • Bebeacua C, Lai L, Vegge CS, Brondsted L, van Heel M, Veesler D, Cambillau C. 2013. Visualizing a complete Siphoviridae member by single-particle electron microscopy: the structure of lactococcal phage TP091-1. J. Virol. 87:1061-1068. http://dx.doi.org/10.1128/JVI.02836-12.
    • (2013) J. Virol. , vol.87 , pp. 1061-1068
    • Bebeacua, C.1    Lai, L.2    Vegge, C.S.3    Brondsted, L.4    van Heel, M.5    Veesler, D.6    Cambillau, C.7
  • 7
    • 0025991231 scopus 로고
    • A membrane protein is required for bacteriophage c2 infection of Lactococcus lactis subsp. lactis C2
    • Valyasevi R, Sandine WE, Geller BL. 1991. A membrane protein is required for bacteriophage c2 infection of Lactococcus lactis subsp. lactis C2. J. Bacteriol. 173:6095-6100.
    • (1991) J. Bacteriol. , vol.173 , pp. 6095-6100
    • Valyasevi, R.1    Sandine, W.E.2    Geller, B.L.3
  • 8
    • 33644505795 scopus 로고    scopus 로고
    • Interaction of bacteriophage lambda with its cell surface receptor: an in vitro study of binding of the viral tail protein gpJ to LamB (maltoporin)
    • Berkane E, Orlik F, Stegmeier JF, Charbit A, Winterhalter M, Benz R. 2006. Interaction of bacteriophage lambda with its cell surface receptor: an in vitro study of binding of the viral tail protein gpJ to LamB (maltoporin). Biochemistry 45:2708-2720. http://dx.doi.org/10.1021/bi051800v.
    • (2006) Biochemistry , vol.45 , pp. 2708-2720
    • Berkane, E.1    Orlik, F.2    Stegmeier, J.F.3    Charbit, A.4    Winterhalter, M.5    Benz, R.6
  • 9
    • 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. 2012. New insights into pb5, the receptor binding protein of bacteriophage T5, and its interaction with its Escherichia coli receptor FhuA. Biochimie 94:1982-1989. http://dx.doi.org/10.1016/j.biochi.2012.05.021.
    • (2012) Biochimie , vol.94 , pp. 1982-1989
    • Flayhan, A.1    Wien, F.2    Paternostre, M.3    Boulanger, P.4    Breyton, C.5
  • 10
    • 85006911308 scopus 로고
    • Lactococcus lactis ssp. lactis C2 bacteriophage sk1 receptor involving rhamnose and glucose Moieties in the cell wall
    • Ruud V, William ES, Bruce LG. 1994. Lactococcus lactis ssp. lactis C2 bacteriophage sk1 receptor involving rhamnose and glucose Moieties in the cell wall. J. Dairy Sci. 77:1-6. http://dx.doi.org/10.3168/jds. S0022-0302(94)76921-6.
    • (1994) J. Dairy Sci. , vol.77 , pp. 1-6
    • Ruud, V.1    William, E.S.2    Bruce, L.G.3
  • 12
    • 33745126631 scopus 로고    scopus 로고
    • Biodiversity and classification of lactococcal phages
    • Deveau H, Labrie SJ, Chopin MC, Moineau S. 2006. Biodiversity and classification of lactococcal phages. Appl. Environ. Microbiol. 72:4338-4346. http://dx.doi.org/10.1128/AEM.02517-05.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 4338-4346
    • Deveau, H.1    Labrie, S.J.2    Chopin, M.C.3    Moineau, S.4
  • 14
    • 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 CT, de Haard HJ, Moineau S, Cambillau C. 2006. Lactococcal bacteriophage p2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses. Nat. Struct. Mol. Biol. 13:85-89. http://dx.doi.org/10.1038/nsmb1029.
    • (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
  • 15
    • 33645238119 scopus 로고    scopus 로고
    • Receptorbinding protein of Lactococcus lactis phages: identification and characterization of the saccharide receptor-binding site
    • Tremblay DM, Tegoni M, Spinelli S, Campanacci V, Blangy S, Huyghe C, Desmyter A, Labrie S, Moineau S, Cambillau C. 2006. Receptorbinding protein of Lactococcus lactis phages: identification and characterization of the saccharide receptor-binding site. J. Bacteriol. 188:2400-2410. http://dx.doi.org/10.1128/JB.188.7.2400-2410.2006.
    • (2006) J. Bacteriol. , vol.188 , pp. 2400-2410
    • Tremblay, D.M.1    Tegoni, M.2    Spinelli, S.3    Campanacci, V.4    Blangy, S.5    Huyghe, C.6    Desmyter, A.7    Labrie, S.8    Moineau, S.9    Cambillau, C.10
  • 17
    • 65549124070 scopus 로고    scopus 로고
    • Crystal structure of a chimeric receptor binding protein constructed from two lactococcal phages
    • Siponen M, Spinelli S, Blangy S, Moineau S, Cambillau C, Campanacci V. 2009. Crystal structure of a chimeric receptor binding protein constructed from two lactococcal phages. J. Bacteriol. 191:3220-3225. http://dx.doi.org/10.1128/JB.01637-08.
    • (2009) J. Bacteriol. , vol.191 , pp. 3220-3225
    • Siponen, M.1    Spinelli, S.2    Blangy, S.3    Moineau, S.4    Cambillau, C.5    Campanacci, V.6
  • 18
    • 33744900391 scopus 로고    scopus 로고
    • Modular structure of the receptor binding proteins of Lactococcus lactis phages. The RBP structure of the temperate phage TP091-1
    • Spinelli S, Campanacci V, Blangy S, Moineau S, Tegoni M, Cambillau C. 2006. Modular structure of the receptor binding proteins of Lactococcus lactis phages. The RBP structure of the temperate phage TP091-1. J. Biol. Chem. 281:14256-14262. http://dx.doi.org/10.1107/S0907444906022116.
    • (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
  • 24
    • 33748480449 scopus 로고    scopus 로고
    • Crystal structure of the receptorbinding protein head domain from Lactococcus lactis phage bIL170
    • Ricagno S, Campanacci V, Blangy S, Spinelli S, Tremblay D, Moineau S, Tegoni M, Cambillau C. 2006. Crystal structure of the receptorbinding protein head domain from Lactococcus lactis phage bIL170. J. Virol. 80:9331-9335. http://dx.doi.org/10.1128/JVI.01160-06.
    • (2006) J. Virol. , vol.80 , pp. 9331-9335
    • Ricagno, S.1    Campanacci, V.2    Blangy, S.3    Spinelli, S.4    Tremblay, D.5    Moineau, S.6    Tegoni, M.7    Cambillau, C.8
  • 30
    • 77649224584 scopus 로고    scopus 로고
    • Genome organization and characterization of the virulent lactococcal phage 1358 and its similarities to Listeria phages
    • Dupuis ME, Moineau S. 2010. Genome organization and characterization of the virulent lactococcal phage 1358 and its similarities to Listeria phages. Appl. Environ. Microbiol. 76:1623-1632. http://dx.doi.org/10.1128/AEM.02173-09.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 1623-1632
    • Dupuis, M.E.1    Moineau, S.2
  • 31
    • 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 MJ. 2009. Comparative genome analysis of Listeria bacteriophages reveals extensive mosaicism, programmed translational frameshifting, and a novel prophage insertion site. J. Bacteriol. 191:7206-7215. http://dx.doi.org/10.1128/JB.01041-09.
    • (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
  • 32
    • 26844509944 scopus 로고    scopus 로고
    • Automated expression and solubility screening of His-tagged proteins in 96-well format
    • Vincentelli R, Canaan S, Offant J, Cambillau C, Bignon C. 2005. Automated expression and solubility screening of His-tagged proteins in 96-well format. Anal. Biochem. 346:77-84. http://dx.doi.org/10.1016/j.ab.2005.07.039.
    • (2005) Anal. Biochem. , vol.346 , pp. 77-84
    • Vincentelli, R.1    Canaan, S.2    Offant, J.3    Cambillau, C.4    Bignon, C.5
  • 34
    • 76449099287 scopus 로고    scopus 로고
    • Xds Acta Crystallogr.
    • Kabsch W. 2010. Xds. Acta Crystallogr. D Biol. Crystallogr. 66:125-132. http://dx.doi.org/10.1107/S0907444909047337.
    • (2010) D Biol. Crystallogr. , vol.66 , pp. 125-132
    • Kabsch, W.1
  • 37
    • 77950798648 scopus 로고    scopus 로고
    • Recent developments in classical density modification
    • Cowtan K. 2010. Recent developments in classical density modification. Acta Crystallogr. D Biol. Crystallogr. 66:470-478. http://dx.doi.org/10.1107/S090744490903947X.
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 470-478
    • Cowtan, K.1
  • 38
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr
    • Cowtan K. 2006. The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr. D Biol. Crystallogr. 62:1002-1011. http://dx.doi.org/10.1107/S0907444906022116.
    • (2006) D Biol. Crystallogr. , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 42
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G, Vagin AA, Dodson EJ. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53:240-255. http://dx.doi.org/10.1107/S0907444996012255.
    • (1997) Acta Crystallogr. D Biol. Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.1    Vagin, A.A.2    Dodson, E.J.3
  • 43
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Soding J, Biegert A, Lupas AN. 2005. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res. 33:W244-W248. http://dx.doi.org/10.1093/nar/gki408.
    • (2005) Nucleic Acids Res. , vol.33
    • Soding, J.1    Biegert, A.2    Lupas, A.N.3
  • 45
    • 0037164098 scopus 로고    scopus 로고
    • How proteins bind carbohydrates: lessons from legume lectins
    • Sharon N, Lis H. 2002. How proteins bind carbohydrates: lessons from legume lectins. J. Agric. Food Chem. 50:6586-6591. http://dx.doi.org/10.1021/jf020190s.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 6586-6591
    • Sharon, N.1    Lis, H.2
  • 46
    • 0028773158 scopus 로고
    • Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety
    • Bourne Y, Mazurier J, Legrand D, Rouge P, Montreuil J, Spik G, Cambillau C. 1994. Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety. Structure 2:209-219. http://dx.doi.org/10.1016/S0969-2126(00)00022-8.
    • (1994) Structure , vol.2 , pp. 209-219
    • Bourne, Y.1    Mazurier, J.2    Legrand, D.3    Rouge, P.4    Montreuil, J.5    Spik, G.6    Cambillau, C.7
  • 47
    • 0021095302 scopus 로고
    • Conformations in solution of α,α-trehalose, α-D-glucopyranosyl α-D-mannopyranoside, and their 1-thioglycosyl analogs, and a tentative correlation of their behaviour with respect to the enzyme trehalase
    • Bock K, Defaye J, Driguez H, Bar-Guilloux E. 1983. Conformations in solution of α,α-trehalose, α-D-glucopyranosyl α-D-mannopyranoside, and their 1-thioglycosyl analogs, and a tentative correlation of their behaviour with respect to the enzyme trehalase. Eur. J. Biochem. 131:595-600. http://dx.doi.org/10.1111/j.1432-1033.1983.tb07304.x.
    • (1983) Eur. J. Biochem. , vol.131 , pp. 595-600
    • Bock, K.1    Defaye, J.2    Driguez, H.3    Bar-Guilloux, E.4
  • 48
    • 84879826974 scopus 로고    scopus 로고
    • Structural studies of the cell wall polysaccharides from three strains of Lactobacillus helveticus with different autolytic properties: DPC4571, BROI, and LH1
    • Vinogradov E, Valence F, Maes E, Jebava I, Chuat V, Lortal S, Grard T, Guerardel Y, Sadovskaya I. 2013. Structural studies of the cell wall polysaccharides from three strains of Lactobacillus helveticus with different autolytic properties: DPC4571, BROI, and LH1. Carbohydr. Res. 379:7-12. http://dx.doi.org/10.1016/j.carres.2013.05.020.
    • (2013) Carbohydr. Res. , vol.379 , pp. 7-12
    • Vinogradov, E.1    Valence, F.2    Maes, E.3    Jebava, I.4    Chuat, V.5    Lortal, S.6    Grard, T.7    Guerardel, Y.8    Sadovskaya, I.9
  • 49
    • 71449123158 scopus 로고    scopus 로고
    • Furanose-specific sugar transport: characterization of a bacterial galactofuranose-binding protein
    • Horler RS, Muller A, Williamson DC, Potts JR, Wilson KS, Thomas GH. 2009. Furanose-specific sugar transport: characterization of a bacterial galactofuranose-binding protein. J. Biol. Chem. 284:31156-31163. http://dx.doi.org/10.1074/jbc. M109.054296.
    • (2009) J. Biol. Chem. , vol.284 , pp. 31156-31163
    • Horler, R.S.1    Muller, A.2    Williamson, D.C.3    Potts, J.R.4    Wilson, K.S.5    Thomas, G.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.