메뉴 건너뛰기




Volumn 326, Issue 2, 2012, Pages 151-160

Listeria monocytogenes tyrosine phosphatases affect wall teichoic acid composition and phage resistance

Author keywords

Listeria monocytogenes; Phage resistance; Tyrosine phosphatase

Indexed keywords

N ACETYLGLUCOSAMINE; PROTEIN TYROSINE PHOSPHATASE; TEICHOIC ACID;

EID: 83855163568     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2011.02445.x     Document Type: Article
Times cited : (11)

References (42)
  • 1
    • 43049181499 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis virulence is mediated by PtpA dephosphorylation of human vacuolar protein sorting 33B
    • Bach H, Papavinasasundaram KG, Wong D, Hmama Z & Av-Gay Y (2008) Mycobacterium tuberculosis virulence is mediated by PtpA dephosphorylation of human vacuolar protein sorting 33B. Cell Host Microbe 3: 316-322.
    • (2008) Cell Host Microbe , vol.3 , pp. 316-322
    • Bach, H.1    Papavinasasundaram, K.G.2    Wong, D.3    Hmama, Z.4    Av-Gay, Y.5
  • 2
    • 66549090908 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis PtkA is a novel protein tyrosine kinase whose substrate is PtpA
    • Bach H, Wong D & Av-Gay Y (2009) Mycobacterium tuberculosis PtkA is a novel protein tyrosine kinase whose substrate is PtpA. Biochem J 420: 155-160.
    • (2009) Biochem J , vol.420 , pp. 155-160
    • Bach, H.1    Wong, D.2    Av-Gay, Y.3
  • 3
    • 69249225578 scopus 로고    scopus 로고
    • Tyrosine-kinases in bacteria: from a matter of controversy to the status of key regulatory enzymes
    • Bechet E, Guiral S, Torres S, Mijakovic I, Cozzone AJ & Grangeasse C (2009) Tyrosine-kinases in bacteria: from a matter of controversy to the status of key regulatory enzymes. Amino Acids 37: 499-507.
    • (2009) Amino Acids , vol.37 , pp. 499-507
    • Bechet, E.1    Guiral, S.2    Torres, S.3    Mijakovic, I.4    Cozzone, A.J.5    Grangeasse, C.6
  • 4
    • 64649095990 scopus 로고    scopus 로고
    • Inhibition of MptpB phosphatase from Mycobacterium tuberculosis impairs mycobacterial survival in macrophages
    • Beresford NJ, Mulhearn D, Szczepankiewicz B et al. (2009) Inhibition of MptpB phosphatase from Mycobacterium tuberculosis impairs mycobacterial survival in macrophages. J Antimicrob Chemother 63: 928-936.
    • (2009) J Antimicrob Chemother , vol.63 , pp. 928-936
    • Beresford, N.J.1    Mulhearn, D.2    Szczepankiewicz, B.3
  • 5
    • 77955081657 scopus 로고    scopus 로고
    • A new family of phosphoinositide phosphatases in microorganisms: identification and biochemical analysis
    • Beresford NJ, Saville C, Bennett HJ, Roberts IS & Tabernero L (2010) A new family of phosphoinositide phosphatases in microorganisms: identification and biochemical analysis. BMC Genomics 11: 457.
    • (2010) BMC Genomics , vol.11 , pp. 457
    • Beresford, N.J.1    Saville, C.2    Bennett, H.J.3    Roberts, I.S.4    Tabernero, L.5
  • 6
    • 0027476804 scopus 로고
    • Dual roles of plcA in Listeria monocytogenes pathogenesis
    • Camilli A, Tilney LG & Portnoy DA (1993) Dual roles of plcA in Listeria monocytogenes pathogenesis. Mol Microbiol 8: 143-157.
    • (1993) Mol Microbiol , vol.8 , pp. 143-157
    • Camilli, A.1    Tilney, L.G.2    Portnoy, D.A.3
  • 7
    • 75349083412 scopus 로고    scopus 로고
    • Protein kinase and phosphatase signaling in Mycobacterium tuberculosis physiology and pathogenesis
    • Chao J, Wong D, Zheng X, Poirier V, Bach H, Hmama Z & Av-Gay Y (2010) Protein kinase and phosphatase signaling in Mycobacterium tuberculosis physiology and pathogenesis. Biochim Biophys Acta 1804: 620-627.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 620-627
    • Chao, J.1    Wong, D.2    Zheng, X.3    Poirier, V.4    Bach, H.5    Hmama, Z.6    Av-Gay, Y.7
  • 8
    • 30744478198 scopus 로고    scopus 로고
    • Role of protein phosphorylation on serine/threonine and tyrosine in the virulence of bacterial pathogens
    • Cozzone AJ (2005) Role of protein phosphorylation on serine/threonine and tyrosine in the virulence of bacterial pathogens. J Mol Microbiol Biotechnol 9: 198-213.
    • (2005) J Mol Microbiol Biotechnol , vol.9 , pp. 198-213
    • Cozzone, A.J.1
  • 9
    • 79959732255 scopus 로고    scopus 로고
    • Rapid analysis of Listeria monocytogenes cell wall teichoic acid carbohydrates by ESI-MS/MS
    • Eugster MR & Loessner MJ (2011) Rapid analysis of Listeria monocytogenes cell wall teichoic acid carbohydrates by ESI-MS/MS. PLoS ONE 6: e21500.
    • (2011) PLoS ONE , vol.6
    • Eugster, M.R.1    Loessner, M.J.2
  • 10
    • 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 MR, Haug MC, Huwiler SG & Loessner MJ (2011) The cell wall binding domain of Listeria bacteriophage endolysin PlyP35 recognizes terminal GlcNAc residues in cell wall teichoic acid. Mol Microbiol 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
  • 12
    • 0141574316 scopus 로고    scopus 로고
    • Autophosphorylation of the Escherichia coli protein kinase Wzc regulates tyrosine phosphorylation of Ugd, a UDP-glucose dehydrogenase
    • Grangeasse C, Obadia B, Mijakovic I, Deutscher J, Cozzone AJ & Doublet P (2003) Autophosphorylation of the Escherichia coli protein kinase Wzc regulates tyrosine phosphorylation of Ugd, a UDP-glucose dehydrogenase. J Biol Chem 278: 39323-39329.
    • (2003) J Biol Chem , vol.278 , pp. 39323-39329
    • Grangeasse, C.1    Obadia, B.2    Mijakovic, I.3    Deutscher, J.4    Cozzone, A.J.5    Doublet, P.6
  • 13
    • 33846683630 scopus 로고    scopus 로고
    • Tyrosine phosphorylation: an emerging regulatory device of bacterial physiology
    • Grangeasse C, Cozzone AJ, Deutscher J & Mijakovic I (2007) Tyrosine phosphorylation: an emerging regulatory device of bacterial physiology. Trends Biochem Sci 32: 86-94.
    • (2007) Trends Biochem Sci , vol.32 , pp. 86-94
    • Grangeasse, C.1    Cozzone, A.J.2    Deutscher, J.3    Mijakovic, I.4
  • 14
    • 34047255891 scopus 로고    scopus 로고
    • Structural basis for selective inhibition of Mycobacterium tuberculosis protein tyrosine phosphatase PtpB
    • Grundner C, Perrin D, Hooft van Huijsduijnen R et al. (2007) Structural basis for selective inhibition of Mycobacterium tuberculosis protein tyrosine phosphatase PtpB. Structure 15: 499-509.
    • (2007) Structure , vol.15 , pp. 499-509
    • Grundner, C.1    Perrin, D.2    Hooft van Huijsduijnen, R.3
  • 15
    • 66949133937 scopus 로고    scopus 로고
    • Risk factors for mortality among patients with nonperinatal listeriosis in Los Angeles County, 1992-2004
    • Guevara RE, Mascola L & Sorvillo F (2009) Risk factors for mortality among patients with nonperinatal listeriosis in Los Angeles County, 1992-2004. Clin Infect Dis 48: 1507-1515.
    • (2009) Clin Infect Dis , vol.48 , pp. 1507-1515
    • Guevara, R.E.1    Mascola, L.2    Sorvillo, F.3
  • 16
    • 0033977642 scopus 로고    scopus 로고
    • Generalized transduction of serotype 1/2 and serotype 4b strains of Listeria monocytogenes
    • Hodgson DA (2000) Generalized transduction of serotype 1/2 and serotype 4b strains of Listeria monocytogenes. Mol Microbiol 35: 312-323.
    • (2000) Mol Microbiol , vol.35 , pp. 312-323
    • Hodgson, D.A.1
  • 18
    • 0033806882 scopus 로고    scopus 로고
    • Cloning and characterization of secretory tyrosine phosphatases of Mycobacterium tuberculosis
    • Koul A, Choidas A, Treder M, Tyagi AK, Drlica K, Singh Y & Ullrich A (2000) Cloning and characterization of secretory tyrosine phosphatases of Mycobacterium tuberculosis. J Bacteriol 182: 5425-5432.
    • (2000) J Bacteriol , vol.182 , pp. 5425-5432
    • Koul, A.1    Choidas, A.2    Treder, M.3    Tyagi, A.K.4    Drlica, K.5    Singh, Y.6    Ullrich, A.7
  • 19
    • 52449096930 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the UDP-glucose dehydrogenase of Escherichia coli is at the crossroads of colanic acid synthesis and polymyxin resistance
    • Lacour S, Bechet E, Cozzone AJ, Mijakovic I & Grangeasse C (2008) Tyrosine phosphorylation of the UDP-glucose dehydrogenase of Escherichia coli is at the crossroads of colanic acid synthesis and polymyxin resistance. PLoS ONE 3: e3053.
    • (2008) PLoS ONE , vol.3
    • Lacour, S.1    Bechet, E.2    Cozzone, A.J.3    Mijakovic, I.4    Grangeasse, C.5
  • 20
    • 0036062278 scopus 로고    scopus 로고
    • Construction, characterization, and use of two Listeria monocytogenes site-specific phage integration vectors
    • Lauer P, Chow MY, Loessner MJ, Portnoy DA & Calendar R (2002) Construction, characterization, and use of two Listeria monocytogenes site-specific phage integration vectors. J Bacteriol 184: 4177-4186.
    • (2002) J Bacteriol , vol.184 , pp. 4177-4186
    • Lauer, P.1    Chow, M.Y.2    Loessner, M.J.3    Portnoy, D.A.4    Calendar, R.5
  • 21
    • 0028821725 scopus 로고
    • Organization and transcriptional analysis of the Listeria phage A511 late gene region comprising the major capsid and tail sheath protein genes cps and tsh
    • Loessner MJ & Scherer S (1995) Organization and transcriptional analysis of the Listeria phage A511 late gene region comprising the major capsid and tail sheath protein genes cps and tsh. J Bacteriol 177: 6601-6609.
    • (1995) J Bacteriol , vol.177 , pp. 6601-6609
    • Loessner, M.J.1    Scherer, S.2
  • 22
    • 0029783288 scopus 로고    scopus 로고
    • Modified Listeria bacteriophage lysin genes (ply) allow efficient overexpression and one-step purification of biochemically active fusion proteins
    • Loessner MJ, Schneider A & Scherer S (1996) Modified Listeria bacteriophage lysin genes (ply) allow efficient overexpression and one-step purification of biochemically active fusion proteins. Appl Environ Microbiol 62: 3057-3060.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 3057-3060
    • Loessner, M.J.1    Schneider, A.2    Scherer, S.3
  • 23
    • 0033959106 scopus 로고    scopus 로고
    • Complete nucleotide sequence, molecular analysis and genome structure of bacteriophage A118 of Listeria monocytogenes: implications for phage evolution
    • Loessner MJ, Inman RB, Lauer P & Calendar R (2000) Complete nucleotide sequence, molecular analysis and genome structure of bacteriophage A118 of Listeria monocytogenes: implications for phage evolution. Mol Microbiol 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
  • 24
    • 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 MJ, Kramer K, Ebel F & Scherer S (2002) C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high-affinity binding to bacterial cell wall carbohydrates. Mol Microbiol 44: 335-349.
    • (2002) Mol Microbiol , vol.44 , pp. 335-349
    • Loessner, M.J.1    Kramer, K.2    Ebel, F.3    Scherer, S.4
  • 25
    • 0016699858 scopus 로고
    • Interaction of wheat-germ agglutinin with bacterial cells and cell-wall polymers
    • Lotan R, Sharon N & Mirelman D (1975) Interaction of wheat-germ agglutinin with bacterial cells and cell-wall polymers. Eur J Biochem 55: 257-262.
    • (1975) Eur J Biochem , vol.55 , pp. 257-262
    • Lotan, R.1    Sharon, N.2    Mirelman, D.3
  • 26
    • 39749166860 scopus 로고    scopus 로고
    • Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation
    • Macek B, Gnad F, Soufi B, Kumar C, Olsen JV, Mijakovic I & Mann M (2008) Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol Cell Proteomics 7: 299-307.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 299-307
    • Macek, B.1    Gnad, F.2    Soufi, B.3    Kumar, C.4    Olsen, J.V.5    Mijakovic, I.6    Mann, M.7
  • 27
    • 0036134946 scopus 로고    scopus 로고
    • Streptococcus pneumoniae capsule biosynthesis protein CpsB is a novel manganese-dependent phosphotyrosine-protein phosphatase
    • Morona JK, Morona R, Miller DC & Paton JC (2002) Streptococcus pneumoniae capsule biosynthesis protein CpsB is a novel manganese-dependent phosphotyrosine-protein phosphatase. J Bacteriol 184: 577-583.
    • (2002) J Bacteriol , vol.184 , pp. 577-583
    • Morona, J.K.1    Morona, R.2    Miller, D.C.3    Paton, J.C.4
  • 28
    • 0035214193 scopus 로고    scopus 로고
    • Role of tyrosine kinases and the tyrosine phosphatase SptP in the interaction of Salmonella with host cells
    • Murli S, Watson RO & Galan JE (2001) Role of tyrosine kinases and the tyrosine phosphatase SptP in the interaction of Salmonella with host cells. Cell Microbiol 3: 795-810.
    • (2001) Cell Microbiol , vol.3 , pp. 795-810
    • Murli, S.1    Watson, R.O.2    Galan, J.E.3
  • 29
    • 21844476149 scopus 로고    scopus 로고
    • Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis
    • Musumeci L, Bongiorni C, Tautz L et al. (2005) Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis. J Bacteriol 187: 4945-4956.
    • (2005) J Bacteriol , vol.187 , pp. 4945-4956
    • Musumeci, L.1    Bongiorni, C.2    Tautz, L.3
  • 30
    • 0037310572 scopus 로고    scopus 로고
    • Involvement of a protein tyrosine kinase in production of the polymeric bioemulsifier emulsan from the oil-degrading strain Acinetobacter lwoffii RAG-1
    • Nakar D & Gutnick DL (2003) Involvement of a protein tyrosine kinase in production of the polymeric bioemulsifier emulsan from the oil-degrading strain Acinetobacter lwoffii RAG-1. J Bacteriol 185: 1001-1009.
    • (2003) J Bacteriol , vol.185 , pp. 1001-1009
    • Nakar, D.1    Gutnick, D.L.2
  • 31
    • 33847037161 scopus 로고    scopus 로고
    • Influence of tyrosine-kinase Wzc activity on colanic acid production in Escherichia coli K12 cells
    • Obadia B, Lacour S, Doublet P, Baubichon-Cortay H, Cozzone AJ & Grangeasse C (2007) Influence of tyrosine-kinase Wzc activity on colanic acid production in Escherichia coli K12 cells. J Mol Biol 367: 42-53.
    • (2007) J Mol Biol , vol.367 , pp. 42-53
    • Obadia, B.1    Lacour, S.2    Doublet, P.3    Baubichon-Cortay, H.4    Cozzone, A.J.5    Grangeasse, C.6
  • 32
    • 45849125779 scopus 로고    scopus 로고
    • Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus
    • Olivares-Illana V, Meyer P, Bechet E et al. (2008) Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus. PLoS Biol 6: e143.
    • (2008) PLoS Biol , vol.6
    • Olivares-Illana, V.1    Meyer, P.2    Bechet, E.3
  • 33
    • 22544486262 scopus 로고    scopus 로고
    • Identification of an Escherichia coli operon required for formation of the O-antigen capsule
    • Peleg A, Shifrin Y, Ilan O et al. (2005) Identification of an Escherichia coli operon required for formation of the O-antigen capsule. J Bacteriol 187: 5259-5266.
    • (2005) J Bacteriol , vol.187 , pp. 5259-5266
    • Peleg, A.1    Shifrin, Y.2    Ilan, O.3
  • 34
    • 0023898917 scopus 로고
    • Role of hemolysin for the intracellular growth of Listeria monocytogenes
    • Portnoy DA, Jacks PS & Hinrichs DJ (1988) Role of hemolysin for the intracellular growth of Listeria monocytogenes. J Exp Med 167: 1459-1471.
    • (1988) J Exp Med , vol.167 , pp. 1459-1471
    • Portnoy, D.A.1    Jacks, P.S.2    Hinrichs, D.J.3
  • 36
    • 0036199352 scopus 로고    scopus 로고
    • Listeria monocytogenes infection in Israel and review of cases worldwide
    • Siegman-Igra Y, Levin R, Weinberger M et al. (2002) Listeria monocytogenes infection in Israel and review of cases worldwide. Emerg Infect Dis 8: 305-310.
    • (2002) Emerg Infect Dis , vol.8 , pp. 305-310
    • Siegman-Igra, Y.1    Levin, R.2    Weinberger, M.3
  • 37
    • 0036723797 scopus 로고    scopus 로고
    • Staphylococcus aureus contains two low-molecular-mass phosphotyrosine protein phosphatases
    • Soulat D, Vaganay E, Duclos B, Genestier AL, Etienne J & Cozzone AJ (2002) Staphylococcus aureus contains two low-molecular-mass phosphotyrosine protein phosphatases. J Bacteriol 184: 5194-5199.
    • (2002) J Bacteriol , vol.184 , pp. 5194-5199
    • Soulat, D.1    Vaganay, E.2    Duclos, B.3    Genestier, A.L.4    Etienne, J.5    Cozzone, A.J.6
  • 38
    • 0025295647 scopus 로고
    • The bacteriophage kh receptor of Lactococcus lactis subsp. cremoris KH is the rhamnose of the extracellular wall polysaccharide
    • Valyasevi R, Sandine WE & Geller BL (1990) The bacteriophage kh receptor of Lactococcus lactis subsp. cremoris KH is the rhamnose of the extracellular wall polysaccharide. Appl Environ Microbiol 56: 1882-1889.
    • (1990) Appl Environ Microbiol , vol.56 , pp. 1882-1889
    • Valyasevi, R.1    Sandine, W.E.2    Geller, B.L.3
  • 39
    • 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 MJ & Scherer S (1996) Bacteriophage receptors on Listeria monocytogenes cells are the N-acetylglucosamine and rhamnose substituents of teichoic acids or the peptidoglycan itself. Microbiology 142(Pt 4): 985-992.
    • (1996) Microbiology , vol.142 , Issue.PART 4 , pp. 985-992
    • Wendlinger, G.1    Loessner, M.J.2    Scherer, S.3
  • 40
    • 0021755746 scopus 로고
    • Structural comparison of the two distinct sugar binding sites in wheat germ agglutinin isolectin II
    • Wright CS (1984) Structural comparison of the two distinct sugar binding sites in wheat germ agglutinin isolectin II. J Mol Biol 178: 91-104.
    • (1984) J Mol Biol , vol.178 , pp. 91-104
    • Wright, C.S.1
  • 41
    • 30744457819 scopus 로고    scopus 로고
    • Interaction between the Yersinia tyrosine phosphatase YopH and its macrophage substrate, Fyn-binding protein, Fyb
    • Yuan M, Deleuil F & Fallman M (2005) Interaction between the Yersinia tyrosine phosphatase YopH and its macrophage substrate, Fyn-binding protein, Fyb. J Mol Microbiol Biotechnol 9: 214-223.
    • (2005) J Mol Microbiol Biotechnol , vol.9 , pp. 214-223
    • Yuan, M.1    Deleuil, F.2    Fallman, M.3
  • 42
    • 77949536564 scopus 로고    scopus 로고
    • Targeting mycobacterium protein tyrosine phosphatase B for antituberculosis agents
    • Zhou B, He Y, Zhang X et al. (2010) Targeting mycobacterium protein tyrosine phosphatase B for antituberculosis agents. P Natl Acad Sci USA 107: 4573-4578.
    • (2010) P Natl Acad Sci USA , vol.107 , pp. 4573-4578
    • Zhou, B.1    He, Y.2    Zhang, X.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.