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Volumn 68, Issue , 2014, Pages 81-100

Lipoteichoic acid synthesis and function in gram-positive bacteria

Author keywords

Bacterial cell wall; Cholination; d alanylation; Glycosylation; Lipid turnover; Osmoregulated periplasmic glucans

Indexed keywords

GLUCAN; LIPOPOLYSACCHARIDE; LIPOTEICHOIC ACID; LIPOTEICHOIC ACID VACCINE; PHOSPHORYLCHOLINE; POLYMER; PROBIOTIC AGENT; UNCLASSIFIED DRUG; VACCINE; VANCOMYCIN; BACTERIAL PROTEIN; TEICHOIC ACID;

EID: 84907487882     PISSN: 00664227     EISSN: 15453251     Source Type: Book Series    
DOI: 10.1146/annurev-micro-091213-112949     Document Type: Review
Times cited : (311)

References (135)
  • 1
    • 0036192372 scopus 로고    scopus 로고
    • Formation of D-alanyl-lipoteichoic acid is required for adhesion and virulence of Listeria monocytogenes
    • Abachin E, Poyart C, Pellegrini E, Milohanic E, Fiedler F, et al. 2002. Formation of D-alanyl-lipoteichoic acid is required for adhesion and virulence of Listeria monocytogenes. Mol. Microbiol. 43:1-14
    • (2002) Mol. Microbiol. , vol.43 , pp. 1-14
    • Abachin, E.1    Poyart, C.2    Pellegrini, E.3    Milohanic, E.4    Fiedler, F.5
  • 2
    • 70350452559 scopus 로고    scopus 로고
    • The dlt operon of Bacillus cereus is required for resistance to cationic antimicrobial peptides and for virulence in insects
    • Abi Khattar Z, Rejasse A, Destoumieux-Garz on D, Escoubas JM, Sanchis V, et al. 2009. The dlt operon of Bacillus cereus is required for resistance to cationic antimicrobial peptides and for virulence in insects. J. Bacteriol. 191:7063-73
    • (2009) J. Bacteriol. , vol.191 , pp. 7063-7073
    • Abi Khattar, Z.1    Rejasse, A.2    Destoumieux-Garzon, D.3    Escoubas, J.M.4    Sanchis, V.5
  • 3
    • 79952211396 scopus 로고    scopus 로고
    • The C-terminal domain of the arabinosyltransferase Mycobacterium tuberculosisEmbCis a lectin-like carbohydrate bindingmodule
    • Alderwick LJ, Lloyd GS, Ghadbane H, May JW, Bhatt A, et al. 2011. The C-terminal domain of the arabinosyltransferase Mycobacterium tuberculosisEmbCis a lectin-like carbohydrate bindingmodule. PLoS Pathog. 7:e1001299
    • (2011) PLoS Pathog. , vol.7 , pp. e1001299
    • Alderwick, L.J.1    Lloyd, G.S.2    Ghadbane, H.3    May, J.W.4    Bhatt, A.5
  • 4
    • 0019858145 scopus 로고
    • Occurrence of ribitol-containing lipoteichoic acid in Staphylococcus aureus H and its glycosylation
    • Arakawa H, Shimada A, Ishimoto N, Ito E. 1981. Occurrence of ribitol-containing lipoteichoic acid in Staphylococcus aureus H and its glycosylation. J. Biochem. 89:1555-63
    • (1981) J. Biochem. , vol.89 , pp. 1555-1563
    • Arakawa, H.1    Shimada, A.2    Ishimoto, N.3    Ito, E.4
  • 5
    • 0015926870 scopus 로고
    • The alanine ester content and magnesium binding capacity of walls of Staphylococcus aureus H grown at different pH values
    • Archibald AR, Baddiley J, Heptinstall S. 1973. The alanine ester content and magnesium binding capacity of walls of Staphylococcus aureus H grown at different pH values. Biochim. Biophys. Acta 291:629-34
    • (1973) Biochim. Biophys. Acta , vol.291 , pp. 629-634
    • Archibald, A.R.1    Baddiley, J.2    Heptinstall, S.3
  • 8
    • 0015464726 scopus 로고
    • Teichoic acids in cell walls and membranes of bacteria
    • Baddiley J. 1972. Teichoic acids in cell walls and membranes of bacteria. Essays Biochem. 8:35-77
    • (1972) Essays Biochem. , vol.8 , pp. 35-77
    • Baddiley, J.1
  • 9
    • 84892404829 scopus 로고    scopus 로고
    • Cyclic di-AMP impairs potassium uptake mediated by a cyclic di-AMP binding protein in Streptococcus pneumoniae
    • Bai Y, Yang J, Zarrella TM, Zhang Y, Metzger DW, Bai G. 2013. Cyclic di-AMP impairs potassium uptake mediated by a cyclic di-AMP binding protein in Streptococcus pneumoniae. J. Bacteriol. 196:614-23
    • (2013) J. Bacteriol. , vol.196 , pp. 614-623
    • Bai, Y.1    Yang, J.2    Zarrella, T.M.3    Zhang, Y.4    Metzger, D.W.5    Bai, G.6
  • 10
    • 60849110560 scopus 로고    scopus 로고
    • Synthesis of CDP-activated ribitol for teichoic acid precursors in Streptococcus pneumoniae
    • Baur S, Marles-Wright J, Buckenmaier S, Lewis RJ, Vollmer W. 2009. Synthesis of CDP-activated ribitol for teichoic acid precursors in Streptococcus pneumoniae. J. Bacteriol. 191:1200-10
    • (2009) J. Bacteriol. , vol.191 , pp. 1200-1210
    • Baur, S.1    Marles-Wright, J.2    Buckenmaier, S.3    Lewis, R.J.4    Vollmer, W.5
  • 11
    • 34447312195 scopus 로고    scopus 로고
    • The glycosyltransferases of Mycobacterium tuberculosis- roles in the synthesis of arabinogalactan, lipoarabinomannan, and other glycoconjugates
    • Berg S, Kaur D, Jackson M, Brennan PJ. 2007. The glycosyltransferases of Mycobacterium tuberculosis- roles in the synthesis of arabinogalactan, lipoarabinomannan, and other glycoconjugates. Glycobiology 17:35R-56R
    • (2007) Glycobiology , vol.17 , pp. 35R-56R
    • Berg, S.1    Kaur, D.2    Jackson, M.3    Brennan, P.J.4
  • 12
    • 0034531018 scopus 로고    scopus 로고
    • Structures of two cell wall-associated polysaccharides of a Streptococcus mitis biovar 1 strain: A unique teichoic acid-like polysaccharide and the group O antigen which is a C-polysaccharide in common with pneumococci
    • Bergstrom N, Jansson PE, Kilian M, Skov Sorensen UB. 2000. Structures of two cell wall-associated polysaccharides of a Streptococcus mitis biovar 1 strain: a unique teichoic acid-like polysaccharide and the group O antigen which is a C-polysaccharide in common with pneumococci. Eur. J. Biochem. 267:7147-57
    • (2000) Eur. J. Biochem. , vol.267 , pp. 7147-7157
    • Bergstrom, N.1    Jansson, P.E.2    Kilian, M.3    Skov Sorensen, U.B.4
  • 13
    • 84861182186 scopus 로고    scopus 로고
    • Clostridium difficile carbohydrates: Glucan in spores, PSII common antigen in cells, immunogenicity of PSII in swine and synthesis of a dual C difficile-ETEC conjugate vaccine
    • Bertolo L, Boncheff AG, Ma Z, Chen YH, Wakeford T, et al. 2012. Clostridium difficile carbohydrates: glucan in spores, PSII common antigen in cells, immunogenicity of PSII in swine and synthesis of a dual C. difficile-ETEC conjugate vaccine. Carbohydr. Res. 354:79-86
    • (2012) Carbohydr. Res. , vol.354 , pp. 79-86
    • Bertolo, L.1    Boncheff, A.G.2    Ma, Z.3    Chen, Y.H.4    Wakeford, T.5
  • 14
    • 59349108944 scopus 로고    scopus 로고
    • Osmoregulated periplasmic glucans of Salmonella enterica serovar Typhimurium are required for optimal virulence in mice
    • Bhagwat AA, Jun W, Liu L, Kannan P, Dharne M, et al. 2009. Osmoregulated periplasmic glucans of Salmonella enterica serovar Typhimurium are required for optimal virulence in mice. Microbiology 155:229-37
    • (2009) Microbiology , vol.155 , pp. 229-237
    • Bhagwat, A.A.1    Jun, W.2    Liu, L.3    Kannan, P.4    Dharne, M.5
  • 15
    • 84887426625 scopus 로고    scopus 로고
    • Biosynthesis of osmoregulated periplasmic glucans in Escherichia coli: The phosphoethanolamine transferase is encoded by opgE
    • Bontemps-Gallo S, Cogez V, Robbe-Masselot C, Quintard K, Dondeyne J, et al. 2013. Biosynthesis of osmoregulated periplasmic glucans in Escherichia coli: The phosphoethanolamine transferase is encoded by opgE. BioMed. Res. Int. 2013:371429
    • (2013) BioMed. Res. Int. , vol.2013 , pp. 371429
    • Bontemps-Gallo, S.1    Cogez, V.2    Robbe-Masselot, C.3    Quintard, K.4    Dondeyne, J.5
  • 16
    • 16844384914 scopus 로고    scopus 로고
    • A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-amino-4-deoxy-L-arabinose: Identification and function of UDP-4-deoxy-4-formamido-L-arabinose
    • Breazeale SD, Ribeiro AA, McClerren AL, Raetz CR. 2005. A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-amino-4-deoxy-L-arabinose: identification and function of UDP-4-deoxy-4-formamido-L-arabinose. J. Biol. Chem. 280:14154-67
    • (2005) J. Biol. Chem. , vol.280 , pp. 14154-14167
    • Breazeale, S.D.1    Ribeiro, A.A.2    McClerren, A.L.3    Raetz, C.R.4
  • 18
    • 84879430573 scopus 로고    scopus 로고
    • Novel synthetic (poly)glycerolphosphatebased antistaphylococcal conjugate vaccine
    • Chen Q, Dintaman J, Lees A, Sen G, Schwartz D, et al. 2013. Novel synthetic (poly)glycerolphosphatebased antistaphylococcal conjugate vaccine. Infect. Immun. 81:2554-61
    • (2013) Infect. Immun. , vol.81 , pp. 2554-2561
    • Chen, Q.1    Dintaman, J.2    Lees, A.3    Sen, G.4    Schwartz, D.5
  • 19
    • 84868146980 scopus 로고    scopus 로고
    • Changes in the oligomerization potential of the division inhibitor UgtP co-ordinate Bacillus subtilis cell size with nutrient availability
    • Chien AC, Zareh SK, Wang YM, Levin PA. 2012. Changes in the oligomerization potential of the division inhibitor UgtP co-ordinate Bacillus subtilis cell size with nutrient availability. Mol. Microbiol. 86:594-610
    • (2012) Mol. Microbiol. , vol.86 , pp. 594-610
    • Chien, A.C.1    Zareh, S.K.2    Wang, Y.M.3    Levin, P.A.4
  • 20
    • 0019310087 scopus 로고
    • Biosynthesis of D-alanyl-lipoteichoic acid: Characterization of esterlinked D-alanine in the in vitro-synthesized product
    • ChildsWC III, Neuhaus FC. 1980. Biosynthesis of D-alanyl-lipoteichoic acid: characterization of esterlinked D-alanine in the in vitro-synthesized product. J. Bacteriol. 143:293-301
    • (1980) J. Bacteriol. , vol.143 , pp. 293-301
    • Childs, W.C.1    Neuhaus, F.C.2
  • 21
    • 0037099263 scopus 로고    scopus 로고
    • Staphylococcus aureus strains lacking D-alaninemodifications of teichoic acids are highly susceptible to human neutrophil killing and are virulence attenuated in mice
    • Collins LV, Kristian SA, Weidenmaier C, Faigle M, Van Kessel KP, et al. 2002. Staphylococcus aureus strains lacking D-alaninemodifications of teichoic acids are highly susceptible to human neutrophil killing and are virulence attenuated in mice. J. Infect. Dis. 186:214-19
    • (2002) J. Infect. Dis. , vol.186 , pp. 214-219
    • Collins, L.V.1    Kristian, S.A.2    Weidenmaier, C.3    Faigle, M.4    Van Kessel, K.P.5
  • 22
    • 80053436395 scopus 로고    scopus 로고
    • C-di-AMP is a new second messenger in Staphylococcus aureus with a role in controlling cell size and envelope stress
    • Corrigan RM, Abbott JC, Burhenne H, Kaever V, Grundling A. 2011. c-di-AMP is a new second messenger in Staphylococcus aureus with a role in controlling cell size and envelope stress. PLoS Pathog. 7:e1002217
    • (2011) PLoS Pathog. , vol.7 , pp. e1002217
    • Corrigan, R.M.1    Abbott, J.C.2    Burhenne, H.3    Kaever, V.4    Grundling, A.5
  • 24
    • 84880508942 scopus 로고    scopus 로고
    • Cyclic di-AMP: Another second messenger enters the fray
    • Corrigan RM, Grundling A. 2013. Cyclic di-AMP: another second messenger enters the fray. Nat. Rev. Microbiol. 11:513-24
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 513-524
    • Corrigan, R.M.1    Grundling, A.2
  • 25
    • 84887990533 scopus 로고    scopus 로고
    • Investigating the candidacy of a lipoteichoic acid-based glycoconjugate as a vaccine to combat Clostridium difficile infection
    • Cox AD, St. Michael F, Aubry A, Cairns CM, Strong PC, et al. 2013. Investigating the candidacy of a lipoteichoic acid-based glycoconjugate as a vaccine to combat Clostridium difficile infection. Glycoconj. J. 30:843-55
    • (2013) Glycoconj. J. , vol.30 , pp. 843-855
    • Cox, A.D.1    St. Michael, F.2    Aubry, A.3    Cairns, C.M.4    Strong, P.C.5
  • 26
    • 34948850302 scopus 로고    scopus 로고
    • The essential tacF gene is responsible for the choline-dependent growth phenotype of Streptococcus pneumoniae
    • Damjanovic M, Kharat AS, Eberhardt A, Tomasz A, Vollmer W. 2007. The essential tacF gene is responsible for the choline-dependent growth phenotype of Streptococcus pneumoniae. J. Bacteriol. 189:7105-11
    • (2007) J. Bacteriol. , vol.189 , pp. 7105-7111
    • Damjanovic, M.1    Kharat, A.S.2    Eberhardt, A.3    Tomasz, A.4    Vollmer, W.5
  • 27
    • 0034055890 scopus 로고    scopus 로고
    • Biosynthesis of lipoteichoic acid in Lactobacillus rhamnosus: Role of DltD in D-alanylation
    • Debabov DV, Kiriukhin MY, Neuhaus FC. 2000. Biosynthesis of lipoteichoic acid in Lactobacillus rhamnosus: role of DltD in D-alanylation. J. Bacteriol. 182:2855-64
    • (2000) J. Bacteriol. , vol.182 , pp. 2855-2864
    • Debabov, D.V.1    Kiriukhin, M.Y.2    Neuhaus, F.C.3
  • 28
    • 78649528250 scopus 로고    scopus 로고
    • Growth temperaturedependent expression of structural variants of Listeria monocytogenes lipoteichoic acid
    • Dehus O, Pfitzenmaier M, Stuebs G, Fischer N, Schwaeble W, et al. 2011. Growth temperaturedependent expression of structural variants of Listeria monocytogenes lipoteichoic acid. Immunobiology 216:24-31
    • (2011) Immunobiology , vol.216 , pp. 24-31
    • Dehus, O.1    Pfitzenmaier, M.2    Stuebs, G.3    Fischer, N.4    Schwaeble, W.5
  • 29
    • 84862018744 scopus 로고    scopus 로고
    • Biosynthesis of teichoic acids in Streptococcus pneumoniae and closely related species: Lessons from genomes
    • DenapaiteD, Br uckner R, Hakenbeck R, Vollmer W. 2012. Biosynthesis of teichoic acids in Streptococcus pneumoniae and closely related species: lessons from genomes. Microb. Drug Resist. 18:344-58
    • (2012) Microb. Drug Resist. , vol.18 , pp. 344-358
    • Denapaite, D.1    Bruckner, R.2    Hakenbeck, R.3    Vollmer, W.4
  • 30
    • 55249096220 scopus 로고    scopus 로고
    • Crystal structure and enantiomer selection by D-alanyl carrier protein ligase DltA from Bacillus cereus
    • Du L, He Y, Luo Y. 2008. Crystal structure and enantiomer selection by D-alanyl carrier protein ligase DltA from Bacillus cereus. Biochemistry 47:11473-80
    • (2008) Biochemistry , vol.47 , pp. 11473-11480
    • Du, L.1    He, Y.2    Luo, Y.3
  • 31
    • 70349920678 scopus 로고    scopus 로고
    • Cellular localization of cholineutilization proteins in Streptococcus pneumoniae using novel fluorescent reporter systems
    • Eberhardt A, Wu LJ, Errington J, Vollmer W, Veening JW. 2009. Cellular localization of cholineutilization proteins in Streptococcus pneumoniae using novel fluorescent reporter systems. Mol. Microbiol. 74:395-408
    • (2009) Mol. Microbiol. , vol.74 , pp. 395-408
    • Eberhardt, A.1    Wu, L.J.2    Errington, J.3    Vollmer, W.4    Veening, J.W.5
  • 32
    • 33745625880 scopus 로고    scopus 로고
    • Alanine esters of enterococcal lipoteichoic acid play a role in biofilm formation and resistance to antimicrobial peptides
    • Fabretti F, Theilacker C, Baldassarri L, Kaczynski Z, Kropec A, et al. 2006. Alanine esters of enterococcal lipoteichoic acid play a role in biofilm formation and resistance to antimicrobial peptides. Infect. Immun. 74:4164-71
    • (2006) Infect. Immun. , vol.74 , pp. 4164-4171
    • Fabretti, F.1    Theilacker, C.2    Baldassarri, L.3    Kaczynski, Z.4    Kropec, A.5
  • 33
    • 0000705051 scopus 로고
    • Bacterial phosphoglycolipids and lipoteichoic acids
    • ed. D Hanahan New York: Plenum
    • FischerW. 1990. Bacterial phosphoglycolipids and lipoteichoic acids. In Handbook of Lipid Research, ed. D Hanahan, pp. 123-234. New York: Plenum
    • (1990) Handbook of Lipid Research , pp. 123-234
    • Fischer, W.1
  • 34
    • 0028244076 scopus 로고
    • Lipoteichoic acid and lipids in the membrane of Staphylococcus aureus
    • Fischer W. 1994. Lipoteichoic acid and lipids in the membrane of Staphylococcus aureus. Med. Microbiol. Immunol. 183:61-76
    • (1994) Med. Microbiol. Immunol. , vol.183 , pp. 61-76
    • Fischer, W.1
  • 35
    • 0001575327 scopus 로고
    • Lipoteichoic acids and lipoglycans
    • ed. JM Ghuysen, R Hackenbeck. Amsterdam: Elsevier Science
    • Fischer W. 1994. Lipoteichoic acids and lipoglycans. In Bacterial Cell Wall, ed. JM Ghuysen, R Hackenbeck, pp. 199-214. Amsterdam: Elsevier Science
    • (1994) Bacterial Cell Wall , pp. 199-214
    • Fischer, W.1
  • 36
    • 0033863915 scopus 로고    scopus 로고
    • Phosphocholine of pneumococcal teichoic acids: Role in bacterial physiology and pneumococcal infection
    • Fischer W. 2000. Phosphocholine of pneumococcal teichoic acids: role in bacterial physiology and pneumococcal infection. Res. Microbiol. 151:421-27
    • (2000) Res. Microbiol. , vol.151 , pp. 421-427
    • Fischer, W.1
  • 37
    • 0019256630 scopus 로고
    • The alanine ester substitution of lipoteichoic acid (LTA) in Staphylococcus aureus
    • Fischer W, Rosel P. 1980. The alanine ester substitution of lipoteichoic acid (LTA) in Staphylococcus aureus. FEBS Lett. 119:224-26
    • (1980) FEBS Lett. , vol.119 , pp. 224-226
    • Fischer, W.1    Rosel, P.2
  • 40
    • 84878405643 scopus 로고    scopus 로고
    • Structural reevaluation of Streptococcus pneumoniae lipoteichoic acid and new insights into its immunostimulatory potency
    • Gisch N, Kohler T, Ulmer AJ, Muthing J, Pribyl T, et al. 2013. Structural reevaluation of Streptococcus pneumoniae lipoteichoic acid and new insights into its immunostimulatory potency. J. Biol. Chem. 288:15654-67
    • (2013) J. Biol. Chem. , vol.288 , pp. 15654-15667
    • Gisch, N.1    Kohler, T.2    Ulmer, A.J.3    Muthing, J.4    Pribyl, T.5
  • 41
    • 85005514846 scopus 로고
    • The immunological properties of the heterophile antigen and somatic polysaccharide of pneumococcus
    • Goebel WF, Adams MH. 1943. The immunological properties of the heterophile antigen and somatic polysaccharide of pneumococcus. J. Exp. Med. 77:435-49
    • (1943) J. Exp. Med. , vol.77 , pp. 435-449
    • Goebel, W.F.1    Adams, M.H.2
  • 42
    • 0019849998 scopus 로고
    • Biosynthesis of membrane-derived oligosaccharides: A periplasmic phosphoglyceroltransferase
    • Goldberg DE, Rumley MK, Kennedy EP. 1981. Biosynthesis of membrane-derived oligosaccharides: a periplasmic phosphoglyceroltransferase. Proc. Natl. Acad. Sci. USA 78:5513-17
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 5513-5517
    • Goldberg, D.E.1    Rumley, M.K.2    Kennedy, E.P.3
  • 43
    • 33947170440 scopus 로고    scopus 로고
    • Genes required for glycolipid synthesis and lipoteichoic acid anchoring in Staphylococcus aureus
    • Grundling A, Schneewind O. 2007. Genes required for glycolipid synthesis and lipoteichoic acid anchoring in Staphylococcus aureus. J. Bacteriol. 189:2521-30
    • (2007) J. Bacteriol. , vol.189 , pp. 2521-2530
    • Grundling, A.1    Schneewind, O.2
  • 44
    • 34347269622 scopus 로고    scopus 로고
    • Synthesis of glycerol phosphate lipoteichoic acid in Staphylococcus aureus
    • Grundling A, Schneewind O. 2007. Synthesis of glycerol phosphate lipoteichoic acid in Staphylococcus aureus. Proc. Natl. Acad. Sci. USA 104:8478-83
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 8478-8483
    • Grundling, A.1    Schneewind, O.2
  • 45
    • 84861879646 scopus 로고    scopus 로고
    • Amino acid addition to Vibrio cholerae LPS establishes a link between surface remodeling in gram-positive and gram-negative bacteria
    • Hankins JV, Madsen JA, Giles DK, Brodbelt JS, Trent MS. 2012. Amino acid addition to Vibrio cholerae LPS establishes a link between surface remodeling in gram-positive and gram-negative bacteria. Proc. Natl. Acad. Sci. USA 109:8722-27
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 8722-8727
    • Hankins, J.V.1    Madsen, J.A.2    Giles, D.K.3    Brodbelt, J.S.4    Trent, M.S.5
  • 46
    • 0026659616 scopus 로고
    • Biosynthesis of D-alanyl-lipoteichoic acid: Cloning, nucleotide sequence, and expression of the Lactobacillus casei gene for the D-alanine-activating enzyme
    • Heaton MP, Neuhaus FC. 1992. Biosynthesis of D-alanyl-lipoteichoic acid: cloning, nucleotide sequence, and expression of the Lactobacillus casei gene for the D-alanine-activating enzyme. J. Bacteriol. 174:4707-17
    • (1992) J. Bacteriol. , vol.174 , pp. 4707-4717
    • Heaton, M.P.1    Neuhaus, F.C.2
  • 47
    • 22444442099 scopus 로고    scopus 로고
    • Insights into pneumococcal pathogenesis from the crystal structure of the modular teichoic acid phosphorylcholine esterase Pce
    • Hermoso JA, Lagartera L, Gonzalez A, Stelter M, Garcia P, et al. 2005. Insights into pneumococcal pathogenesis from the crystal structure of the modular teichoic acid phosphorylcholine esterase Pce. Nat. Struct. Mol. Biol. 12:533-38
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 533-538
    • Hermoso, J.A.1    Lagartera, L.2    Gonzalez, A.3    Stelter, M.4    Garcia, P.5
  • 48
    • 0021014488 scopus 로고
    • Lipoteichoic acid from Listeria monocytogenes
    • Hether NW, Jackson LL. 1983. Lipoteichoic acid from Listeria monocytogenes. J. Bacteriol. 156:809-17
    • (1983) J. Bacteriol. , vol.156 , pp. 809-817
    • Hether, N.W.1    Jackson, L.L.2
  • 49
    • 84880834788 scopus 로고    scopus 로고
    • A moonlighting enzyme links Escherichia coli cell size with central metabolism
    • Hill NS, Buske PJ, Shi Y, Levin PA. 2013. A moonlighting enzyme links Escherichia coli cell size with central metabolism. PLoS Genet. 9:e1003663
    • (2013) PLoS Genet. , vol.9 , pp. e1003663
    • Hill, N.S.1    Buske, P.J.2    Shi, Y.3    Levin, P.A.4
  • 50
    • 0034161499 scopus 로고    scopus 로고
    • A superfamily of membrane-bound O-acyltransferases with implications for Wnt signaling
    • Hofmann K. 2000. A superfamily of membrane-bound O-acyltransferases with implications for Wnt signaling. Trends Biochem. Sci. 25:111-12
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 111-112
    • Hofmann, K.1
  • 51
    • 0016685679 scopus 로고
    • Loss of D-alanine during sublethal heating of Staphylococcus aureus S6 and magnesium binding during repair
    • Hurst A, Hughes A, Duckworth M, Baddiley J. 1975. Loss of D-alanine during sublethal heating of Staphylococcus aureus S6 and magnesium binding during repair. J. Gen. Microbiol. 89:277-84
    • (1975) J. Gen. Microbiol. , vol.89 , pp. 277-284
    • Hurst, A.1    Hughes, A.2    Duckworth, M.3    Baddiley, J.4
  • 52
    • 0024110267 scopus 로고
    • Membrane-bound phosphatases in Escherichia coli: Sequence of the pgpB gene and dual subcellular localization of the pgpB product
    • Icho T. 1988. Membrane-bound phosphatases in Escherichia coli: sequence of the pgpB gene and dual subcellular localization of the pgpB product. J. Bacteriol. 170:5117-24
    • (1988) J. Bacteriol. , vol.170 , pp. 5117-5124
    • Icho, T.1
  • 53
    • 0020657183 scopus 로고
    • Multiple genes for membrane-bound phosphatases in Escherichia coli and their action on phospholipid precursors
    • Icho T, Raetz CR. 1983. Multiple genes for membrane-bound phosphatases in Escherichia coli and their action on phospholipid precursors. J. Bacteriol. 153:722-30
    • (1983) J. Bacteriol. , vol.153 , pp. 722-730
    • Icho, T.1    Raetz, C.R.2
  • 54
    • 0022543504 scopus 로고
    • Comparative studies of lipoteichoic acids from several Bacillus strains
    • IwasakiH, Shimada A, Ito E. 1986. Comparative studies of lipoteichoic acids from several Bacillus strains. J. Bacteriol. 167:508-16
    • (1986) J. Bacteriol. , vol.167 , pp. 508-516
    • Iwasaki, H.1    Shimada, A.2    Ito, E.3
  • 55
    • 0024526129 scopus 로고
    • Structure and glycosylation of lipoteichoic acids in Bacillus strains
    • Iwasaki H, Shimada A, Yokoyama K, Ito E. 1989. Structure and glycosylation of lipoteichoic acids in Bacillus strains. J. Bacteriol. 171:424-29
    • (1989) J. Bacteriol. , vol.171 , pp. 424-429
    • Iwasaki, H.1    Shimada, A.2    Yokoyama, K.3    Ito, E.4
  • 56
    • 0021716448 scopus 로고
    • Biosynthesis of membrane-derived oligosaccharides: Characterization of mdoB mutants defective in phosphoglycerol transferase i activity
    • Jackson BJ, Bohin JP, Kennedy EP. 1984. Biosynthesis of membrane-derived oligosaccharides: characterization of mdoB mutants defective in phosphoglycerol transferase I activity. J. Bacteriol. 160:976-81
    • (1984) J. Bacteriol. , vol.160 , pp. 976-981
    • Jackson, B.J.1    Bohin, J.P.2    Kennedy, E.P.3
  • 57
    • 34547585389 scopus 로고    scopus 로고
    • Identification of a soluble diacylglycerol kinase required for lipoteichoic acid production in Bacillus subtilis
    • Jerga A, Lu YJ, Schujman GE, deMendoza D, Rock CO. 2007. Identification of a soluble diacylglycerol kinase required for lipoteichoic acid production in Bacillus subtilis. J. Biol. Chem. 282:21738-45
    • (2007) J. Biol. Chem. , vol.282 , pp. 21738-21745
    • Jerga, A.1    Lu, Y.J.2    Schujman, G.E.3    Demendoza, D.4    Rock, C.O.5
  • 58
    • 65449154391 scopus 로고    scopus 로고
    • Molecular determinants for interfacial binding and conformational change in a soluble diacylglycerol kinase
    • Jerga A, Miller DJ, White SW, Rock CO. 2009. Molecular determinants for interfacial binding and conformational change in a soluble diacylglycerol kinase. J. Biol. Chem. 284:7246-54
    • (2009) J. Biol. Chem. , vol.284 , pp. 7246-7254
    • Jerga, A.1    Miller, D.J.2    White, S.W.3    Rock, C.O.4
  • 59
    • 0033944623 scopus 로고    scopus 로고
    • Novel processive and nonprocessive glycosyltransferases from Staphylococcus aureus and Arabidopsis thaliana synthesize glycoglycerolipids, glycophospholipids, glycosphingolipids and glycosylsterols
    • Jorasch P, Warnecke DC, Lindner B, Zähringer U, Heinz E. 2000. Novel processive and nonprocessive glycosyltransferases from Staphylococcus aureus and Arabidopsis thaliana synthesize glycoglycerolipids, glycophospholipids, glycosphingolipids and glycosylsterols. Eur. J. Biochem. 267:3770-83
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3770-3783
    • Jorasch, P.1    Warnecke, D.C.2    Lindner, B.3    Zähringer, U.4    Heinz, E.5
  • 60
    • 0031848910 scopus 로고    scopus 로고
    • A UDP glucosyltransferase from Bacillus subtilis successively transfers up to four glucose residues to 1,2-diacylglycerol: Expression of ypfP in Escherichia coli and structural analysis of its reaction products
    • Jorasch P, Wolter FP, Zähringer U, Heinz E. 1998. A UDP glucosyltransferase from Bacillus subtilis successively transfers up to four glucose residues to 1,2-diacylglycerol: expression of ypfP in Escherichia coli and structural analysis of its reaction products. Mol. Microbiol. 29:419-30
    • (1998) Mol. Microbiol. , vol.29 , pp. 419-430
    • Jorasch, P.1    Wolter, F.P.2    Zähringer, U.3    Heinz, E.4
  • 61
    • 77957827858 scopus 로고    scopus 로고
    • In vitro analysis of the Staphylococcus aureus lipoteichoic acid synthase enzyme using fluorescently labeled lipids
    • Karatsa-Dodgson M, Wörmann ME, Gr undling A. 2010. In vitro analysis of the Staphylococcus aureus lipoteichoic acid synthase enzyme using fluorescently labeled lipids. J. Bacteriol. 192:5341-49
    • (2010) J. Bacteriol. , vol.192 , pp. 5341-5349
    • Karatsa-Dodgson, M.1    Wörmann, M.E.2    Grundling, A.3
  • 63
    • 0001223159 scopus 로고    scopus 로고
    • Membrane-derived oligosaccharides (periplasmic β-D-glucans) of Escherichia coli
    • ed. FC Neidhardt Washington, DC: ASM
    • Kennedy EP. 1996. Membrane-derived oligosaccharides (periplasmic β-D-glucans) of Escherichia coli. In Escherichia coli and Salmonella, ed. FC Neidhardt, pp. 1064-71. Washington, DC: ASM
    • (1996) Escherichia Coli and Salmonella , pp. 1064-1071
    • Kennedy, E.P.1
  • 64
    • 33644844445 scopus 로고    scopus 로고
    • Drastic reduction in the virulence of Streptococcus pneumoniae expressing type 2 capsular polysaccharide but lacking choline residues in the cell wall
    • Kharat AS, Tomasz A. 2006. Drastic reduction in the virulence of Streptococcus pneumoniae expressing type 2 capsular polysaccharide but lacking choline residues in the cell wall. Mol. Biol. 60:93-107
    • (2006) Mol. Biol. , vol.60 , pp. 93-107
    • Kharat, A.S.1    Tomasz, A.2
  • 65
    • 84862992817 scopus 로고    scopus 로고
    • Abating colon cancer polyposis by Lactobacillus acidophilus deficient in lipoteichoic acid
    • Khazaie K, Zadeh M, Khan MW, Bere P, Gounari F, et al. 2012. Abating colon cancer polyposis by Lactobacillus acidophilus deficient in lipoteichoic acid. Proc. Natl. Acad. Sci. USA 109:10462-67
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 10462-10467
    • Khazaie, K.1    Zadeh, M.2    Khan, M.W.3    Bere, P.4    Gounari, F.5
  • 66
    • 0035026895 scopus 로고    scopus 로고
    • Biosynthesis of the glycolipid anchor in lipoteichoic acid of Staphylococcus aureus RN4220: Role of YpfP, the diglucosyldiacylglycerol synthase
    • KiriukhinMY, Debabov DV, Shinabarger DL,Neuhaus FC. 2001. Biosynthesis of the glycolipid anchor in lipoteichoic acid of Staphylococcus aureus RN4220: role of YpfP, the diglucosyldiacylglycerol synthase. J. Bacteriol. 183:3506-14
    • (2001) J. Bacteriol. , vol.183 , pp. 3506-3514
    • Kiriukhin, M.Y.1    Debabov, D.V.2    Shinabarger, D.L.3    Neuhaus, F.C.4
  • 67
    • 0015837746 scopus 로고
    • Immunological properties of teichoic acids
    • Knox KW, Wicken AJ. 1973. Immunological properties of teichoic acids. Bacteriol. Rev. 37:215-57
    • (1973) Bacteriol. Rev. , vol.37 , pp. 215-257
    • Knox, K.W.1    Wicken, A.J.2
  • 68
    • 0018127729 scopus 로고
    • Acyldiglucosyldiacylglycerol-containing lipoteichoic acid with a poly(3-Ogalabiosyl-2-O-galactosyl-sn-glycero-1-phosphate) chain from Streptococcus lactis Kiel 42172
    • Koch HU, Fischer W. 1978. Acyldiglucosyldiacylglycerol-containing lipoteichoic acid with a poly(3-Ogalabiosyl- 2-O-galactosyl-sn-glycero-1-phosphate) chain from Streptococcus lactis Kiel 42172. Biochemistry 17:5275-81
    • (1978) Biochemistry , vol.17 , pp. 5275-5281
    • Koch, H.U.1    Fischer, W.2
  • 69
    • 0021765004 scopus 로고
    • The role of lipoteichoic acid biosynthesis in membrane lipid metabolism of growing Staphylococcus aureus
    • Koch HU, Haas R, Fischer W. 1984. The role of lipoteichoic acid biosynthesis in membrane lipid metabolism of growing Staphylococcus aureus. Eur. J. Biochem. 138:357-63
    • (1984) Eur. J. Biochem. , vol.138 , pp. 357-363
    • Koch, H.U.1    Haas, R.2    Fischer, W.3
  • 71
    • 33748670479 scopus 로고    scopus 로고
    • A functional dlt operon, encoding proteins required for incorporation of D-alanine in teichoic acids in gram-positive bacteria, confers resistance to cationic antimicrobial peptides in Streptococcus pneumoniae
    • Kovacs M, Halfmann A, Fedtke I, Heintz M, Peschel A, et al. 2006. A functional dlt operon, encoding proteins required for incorporation of D-alanine in teichoic acids in gram-positive bacteria, confers resistance to cationic antimicrobial peptides in Streptococcus pneumoniae. J. Bacteriol. 188:5797-805
    • (2006) J. Bacteriol. , vol.188 , pp. 5797-5805
    • Kovacs, M.1    Halfmann, A.2    Fedtke, I.3    Heintz, M.4    Peschel, A.5
  • 72
    • 25144519572 scopus 로고    scopus 로고
    • D-Alanylation of teichoic acids promotes group A Streptococcus antimicrobial peptide resistance, neutrophil survival, and epithelial cell invasion
    • Kristian SA, Datta V, Weidenmaier C, Kansal R, Fedtke I, et al. 2005. D-Alanylation of teichoic acids promotes group A Streptococcus antimicrobial peptide resistance, neutrophil survival, and epithelial cell invasion. J. Bacteriol. 187:6719-25
    • (2005) J. Bacteriol. , vol.187 , pp. 6719-6725
    • Kristian, S.A.1    Datta, V.2    Weidenmaier, C.3    Kansal, R.4    Fedtke, I.5
  • 74
    • 39749173102 scopus 로고    scopus 로고
    • Biosynthesis of osmoregulated periplasmic glucans in Escherichia coli: The membrane-bound and the soluble periplasmic phosphoglycerol transferases are encoded by the same gene
    • Lequette Y, Lanfroy E, Cogez V, Bohin JP, Lacroix JM. 2008. Biosynthesis of osmoregulated periplasmic glucans in Escherichia coli: The membrane-bound and the soluble periplasmic phosphoglycerol transferases are encoded by the same gene. Microbiology 154:476-83
    • (2008) Microbiology , vol.154 , pp. 476-483
    • Lequette, Y.1    Lanfroy, E.2    Cogez, V.3    Bohin, J.P.4    Lacroix, J.M.5
  • 75
    • 84878676002 scopus 로고    scopus 로고
    • Tailoring gut immune responseswith lipoteichoic acid-deficient Lactobacillus acidophilus
    • Lightfoot YL, Mohamadzadeh M. 2013. Tailoring gut immune responseswith lipoteichoic acid-deficient Lactobacillus acidophilus. Front. Immunol. 4:25
    • (2013) Front. Immunol. , vol.4 , pp. 25
    • Lightfoot, Y.L.1    Mohamadzadeh, M.2
  • 76
    • 0038309565 scopus 로고    scopus 로고
    • Three monophyletic superfamilies account for the majority of the known glycosyltransferases
    • Liu J, Mushegian A. 2003. Three monophyletic superfamilies account for the majority of the known glycosyltransferases. Protein Sci. 12:1418-31
    • (2003) Protein Sci. , vol.12 , pp. 1418-1431
    • Liu, J.1    Mushegian, A.2
  • 78
    • 79953159519 scopus 로고    scopus 로고
    • Three phosphatidylglycerol-phosphate phosphatases in the inner membrane of Escherichia coli
    • Lu YH, Guan Z, Zhao J, Raetz CR. 2011. Three phosphatidylglycerol-phosphate phosphatases in the inner membrane of Escherichia coli. J. Biol. Chem. 286:5506-18
    • (2011) J. Biol. Chem. , vol.286 , pp. 5506-5518
    • Lu, Y.H.1    Guan, Z.2    Zhao, J.3    Raetz, C.R.4
  • 79
    • 0021685778 scopus 로고
    • Effect of culture pH on the D-alanine ester content of lipoteichoic acid in Staphylococcus aureus
    • MacArthur AE, Archibald AR. 1984. Effect of culture pH on the D-alanine ester content of lipoteichoic acid in Staphylococcus aureus. J. Bacteriol. 160:792-93
    • (1984) J. Bacteriol. , vol.160 , pp. 792-793
    • Macarthur, A.E.1    Archibald, A.R.2
  • 80
    • 33846028166 scopus 로고    scopus 로고
    • Inhibition of pneumococcal choline-binding proteins and cell growth by esters of bicyclic amines
    • Maestro B, Gonzalez A, Garcia P, Sanz JM. 2007. Inhibition of pneumococcal choline-binding proteins and cell growth by esters of bicyclic amines. FEBS J. 274:364-76
    • (2007) FEBS J. , vol.274 , pp. 364-376
    • Maestro, B.1    Gonzalez, A.2    Garcia, P.3    Sanz, J.M.4
  • 81
    • 0020455389 scopus 로고
    • Biosynthesis of glucosyl monophosphoryl undecaprenol and its role in lipoteichoic acid biosynthesis
    • Mancuso DJ, Chiu TH. 1982. Biosynthesis of glucosyl monophosphoryl undecaprenol and its role in lipoteichoic acid biosynthesis. J. Bacteriol. 152:616-25
    • (1982) J. Bacteriol. , vol.152 , pp. 616-625
    • Mancuso, D.J.1    Chiu, T.H.2
  • 82
    • 31844451911 scopus 로고    scopus 로고
    • Multifunctional role of choline binding protein G in pneumococcal pathogenesis
    • Mann B, Orihuela C, Antikainen J, Gao G, Sublett J, et al. 2006. Multifunctional role of choline binding protein G in pneumococcal pathogenesis. Infect. Immun. 74:821-29
    • (2006) Infect. Immun. , vol.74 , pp. 821-829
    • Mann, B.1    Orihuela, C.2    Antikainen, J.3    Gao, G.4    Sublett, J.5
  • 83
    • 84885070749 scopus 로고    scopus 로고
    • Crystal structures of CbpF complexed with atropine and ipratropium reveal clues for the design of novel antimicrobials against Streptococcus pneumoniae
    • Martin NS, Retamosa MG, Maestro B, Bartual SG, Rodes MJ, et al. 2013. Crystal structures of CbpF complexed with atropine and ipratropium reveal clues for the design of novel antimicrobials against Streptococcus pneumoniae. Biochim. Biophys. Acta 1840:129-35
    • (2013) Biochim. Biophys. Acta , vol.1840 , pp. 129-135
    • Martin, N.S.1    Retamosa, M.G.2    Maestro, B.3    Bartual, S.G.4    Rodes, M.J.5
  • 84
    • 16244387909 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals native polymeric cell wall structure in Bacillus subtilis 168 and the existence of a periplasmic space
    • Matias VR, Beveridge TJ. 2005. Cryo-electron microscopy reveals native polymeric cell wall structure in Bacillus subtilis 168 and the existence of a periplasmic space. Mol. Microbiol. 56:240-51
    • (2005) Mol. Microbiol. , vol.56 , pp. 240-251
    • Matias, V.R.1    Beveridge, T.J.2
  • 85
    • 31344459535 scopus 로고    scopus 로고
    • Native cell wall organization shown by cryo-electron microscopy confirms the existence of a periplasmic space in Staphylococcus aureus
    • Matias VR, Beveridge TJ. 2006. Native cell wall organization shown by cryo-electron microscopy confirms the existence of a periplasmic space in Staphylococcus aureus. J. Bacteriol. 188:1011-21
    • (2006) J. Bacteriol. , vol.188 , pp. 1011-1021
    • Matias, V.R.1    Beveridge, T.J.2
  • 86
    • 55549101913 scopus 로고    scopus 로고
    • Lipoteichoic acid is a major component of the Bacillus subtilis periplasm
    • Matias VR, Beveridge TJ. 2008. Lipoteichoic acid is a major component of the Bacillus subtilis periplasm. J. Bacteriol. 190:7414-18
    • (2008) J. Bacteriol. , vol.190 , pp. 7414-7418
    • Matias, V.R.1    Beveridge, T.J.2
  • 87
    • 84859129089 scopus 로고    scopus 로고
    • The Bacillus subtilis essential gene dgkB is dispensable inmutants with defective lipoteichoic acid synthesis
    • Matsuoka S, Hashimoto M, Kamiya Y, Miyazawa T, Ishikawa K, et al. 2011. The Bacillus subtilis essential gene dgkB is dispensable inmutants with defective lipoteichoic acid synthesis. GenesGenet. Syst. 86:365-76
    • (2011) GenesGenet. Syst. , vol.86 , pp. 365-376
    • Matsuoka, S.1    Hashimoto, M.2    Kamiya, Y.3    Miyazawa, T.4    Ishikawa, K.5
  • 88
    • 21344450057 scopus 로고    scopus 로고
    • Inhibition of the D-alanine: DAlanyl carrier protein ligase from Bacillus subtilis increases the bacteriums susceptibility to antibiotics that target the cell wall
    • May JJ, Finking R, Wiegeshoff F, Weber TT, Bandur N, et al. 2005. Inhibition of the D-alanine: DAlanyl carrier protein ligase from Bacillus subtilis increases the bacteriums susceptibility to antibiotics that target the cell wall. FEBS J. 272:2993-3003
    • (2005) FEBS J. , vol.272 , pp. 2993-3003
    • May, J.J.1    Finking, R.2    Wiegeshoff, F.3    Weber, T.T.4    Bandur, N.5
  • 89
    • 79961063575 scopus 로고    scopus 로고
    • Regulation of D-alanylation of lipoteichoic acid in Streptococcus gordonii
    • McCormick NE, Halperin SA, Lee SF. 2011. Regulation of D-alanylation of lipoteichoic acid in Streptococcus gordonii. Microbiology 157:2248-56
    • (2011) Microbiology , vol.157 , pp. 2248-2256
    • McCormick, N.E.1    Halperin, S.A.2    Lee, S.F.3
  • 90
    • 46049087721 scopus 로고    scopus 로고
    • Analysis of the Staphylococcus aureus DgkB structure reveals a common catalytic mechanism for the soluble diacylglycerol kinases
    • Miller DJ, Jerga A, Rock CO, White SW. 2008. Analysis of the Staphylococcus aureus DgkB structure reveals a common catalytic mechanism for the soluble diacylglycerol kinases. Structure 16:1036-46
    • (2008) Structure , vol.16 , pp. 1036-1046
    • Miller, D.J.1    Jerga, A.2    Rock, C.O.3    White, S.W.4
  • 91
    • 79952664813 scopus 로고    scopus 로고
    • Regulation of induced colonic inflammation by Lactobacillus acidophilus deficient in lipoteichoic acid
    • Mohamadzadeh M, Pfeiler EA, Brown JB, Zadeh M, Gramarossa M, et al. 2011. Regulation of induced colonic inflammation by Lactobacillus acidophilus deficient in lipoteichoic acid. Proc. Natl. Acad. Sci. USA 108(Suppl. 1):4623-30
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , Issue.SUPPL. 1 , pp. 4623-4630
    • Mohamadzadeh, M.1    Pfeiler, E.A.2    Brown, J.B.3    Zadeh, M.4    Gramarossa, M.5
  • 92
    • 61849105426 scopus 로고    scopus 로고
    • Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae
    • Molina R, Gonzalez A, Stelter M, Perez-Dorado I, Kahn R, et al. 2009. Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae. EMBO Rep. 10:246-51
    • (2009) EMBO Rep. , vol.10 , pp. 246-251
    • Molina, R.1    Gonzalez, A.2    Stelter, M.3    Perez-Dorado, I.4    Kahn, R.5
  • 93
    • 84869752136 scopus 로고    scopus 로고
    • Pneumococcal surface protein A inhibits complement deposition on the pneumococcal surface by competing with the binding of Creactive protein to cell-surface phosphocholine
    • Mukerji R, Mirza S, Roche AM, Widener RW, Croney CM, et al. 2012. Pneumococcal surface protein A inhibits complement deposition on the pneumococcal surface by competing with the binding of Creactive protein to cell-surface phosphocholine. J. Immunobiol. 189:5327-35
    • (2012) J. Immunobiol. , vol.189 , pp. 5327-5335
    • Mukerji, R.1    Mirza, S.2    Roche, A.M.3    Widener, R.W.4    Croney, C.M.5
  • 95
    • 0347479228 scopus 로고    scopus 로고
    • A continuum of anionic charge: Structures and functions of D-alanylteichoic acids in gram-positive bacteria
    • Neuhaus FC, Baddiley J. 2003. A continuum of anionic charge: structures and functions of D-alanylteichoic acids in gram-positive bacteria. Microbiol. Mol. Biol. Rev. 67:686-723
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 686-723
    • Neuhaus, F.C.1    Baddiley, J.2
  • 96
    • 34147146425 scopus 로고    scopus 로고
    • Contributions of pneumolysin, pneumococcal surface protein A (PspA), and PspC to pathogenicity of Streptococcus pneumoniae D39 in a mouse model
    • Ogunniyi AD, LeMessurier KS, Graham RM, Watt JM, Briles DE, et al. 2007. Contributions of pneumolysin, pneumococcal surface protein A (PspA), and PspC to pathogenicity of Streptococcus pneumoniae D39 in a mouse model. Infect. Immunol. 75:1843-51
    • (2007) Infect. Immunol. , vol.75 , pp. 1843-1851
    • Ogunniyi, A.D.1    Lemessurier, K.S.2    Graham, R.M.3    Watt, J.M.4    Briles, D.E.5
  • 97
    • 58149479227 scopus 로고    scopus 로고
    • Pleiotropic roles of polyglycerolphosphate synthase of lipoteichoic acid in growth of Staphylococcus aureus cells
    • Oku Y, Kurokawa K, Matsuo M, Yamada S, Lee BL, Sekimizu K. 2009. Pleiotropic roles of polyglycerolphosphate synthase of lipoteichoic acid in growth of Staphylococcus aureus cells. J. Bacteriol. 191:141-51
    • (2009) J. Bacteriol. , vol.191 , pp. 141-151
    • Oku, Y.1    Kurokawa, K.2    Matsuo, M.3    Yamada, S.4    Lee, B.L.5    Sekimizu, K.6
  • 98
    • 64049096534 scopus 로고    scopus 로고
    • Crystal structure of Bacillus cereus D-alanyl carrier protein ligase (DltA) in complex with ATP
    • Osman KT, Du L, He Y, Luo Y. 2009. Crystal structure of Bacillus cereus D-alanyl carrier protein ligase (DltA) in complex with ATP. J. Mol. Biol. 388:345-55
    • (2009) J. Mol. Biol. , vol.388 , pp. 345-355
    • Osman, K.T.1    Du, L.2    He, Y.3    Luo, Y.4
  • 99
    • 34249888506 scopus 로고    scopus 로고
    • Functional analysis of D-alanylation of lipoteichoic acid in the probiotic strain Lactobacillus rhamnosus GG
    • PereaVelez M, Verhoeven TL, DraingC,Von Aulock S, PfitzenmaierM, et al. 2007. Functional analysis of D-alanylation of lipoteichoic acid in the probiotic strain Lactobacillus rhamnosus GG. Appl. Environ. Microbiol. 73:3595-604
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 3595-3604
    • Pereavelez, M.1    Verhoeven, T.L.2    Draing, C.3    Von Aulock, S.4    Pfitzenmaier, M.5
  • 100
    • 0028982844 scopus 로고
    • Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis. Identification of genes and regulation
    • Perego M, Glaser P, Minutello A, StrauchMA, Leopold K, Fischer W. 1995. Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis. Identification of genes and regulation. J. Biol. Chem. 270:15598-606
    • (1995) J. Biol. Chem. , vol.270 , pp. 15598-15606
    • Perego, M.1    Glaser, P.2    Minutello, A.3    Strauch, M.A.4    Leopold, K.5    Fischer, W.6
  • 101
    • 77951978074 scopus 로고    scopus 로고
    • Insights into pneumococcal fratricide from the crystal structures of the modular killing factor LytC
    • Perez-Dorado I, Gonzalez A, Morales M, Sanles R, Striker W, et al. 2010. Insights into pneumococcal fratricide from the crystal structures of the modular killing factor LytC. Nat. Struct. Mol. Biol. 17:576-81
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 576-581
    • Perez-Dorado, I.1    Gonzalez, A.2    Morales, M.3    Sanles, R.4    Striker, W.5
  • 102
    • 0033605557 scopus 로고    scopus 로고
    • Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides
    • Peschel A, Otto M, Jack RW, Kalbacher H, Jung G, Gotz F. 1999. Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides. J. Biol. Chem. 274:8405-10
    • (1999) J. Biol. Chem. , vol.274 , pp. 8405-8410
    • Peschel, A.1    Otto, M.2    Jack, R.W.3    Kalbacher, H.4    Jung, G.5    Gotz, F.6
  • 103
    • 0035685114 scopus 로고    scopus 로고
    • Regulation of D-alanyl-lipoteichoic acid biosynthesis in Streptococcus agalactiae involves a novel two-component regulatory system
    • Poyart C, Lamy MC, Boumaila C, Fiedler F, Trieu-Cuot P. 2001. Regulation of D-alanyl-lipoteichoic acid biosynthesis in Streptococcus agalactiae involves a novel two-component regulatory system. J. Bacteriol. 183:6324-34
    • (2001) J. Bacteriol. , vol.183 , pp. 6324-6334
    • Poyart, C.1    Lamy, M.C.2    Boumaila, C.3    Fiedler, F.4    Trieu-Cuot, P.5
  • 104
    • 84883364968 scopus 로고    scopus 로고
    • Revised mechanism of D-alanine incorporation into cell wall polymers in gram-positive bacteria
    • Reichmann NT, Cassona CP, Gr undling A. 2013. Revised mechanism of D-alanine incorporation into cell wall polymers in gram-positive bacteria. Microbiology 159:1868-77
    • (2013) Microbiology , vol.159 , pp. 1868-1877
    • Reichmann, N.T.1    Cassona, C.P.2    Grundling, A.3
  • 105
    • 84897957160 scopus 로고    scopus 로고
    • Differential localization of LTA synthesis proteins and their interaction with the cell division machinery in Staphylococcus aureus
    • Reichmann NT, Cassona CP, Monteiro JM, Bottomley AL, Corrigan RM, et al. 2014. Differential localization of LTA synthesis proteins and their interaction with the cell division machinery in Staphylococcus aureus. Mol. Microbiol. 92:273-86
    • (2014) Mol. Microbiol. , vol.92 , pp. 273-286
    • Reichmann, N.T.1    Cassona, C.P.2    Monteiro, J.M.3    Bottomley, A.L.4    Corrigan, R.M.5
  • 106
    • 79956141388 scopus 로고    scopus 로고
    • Location, synthesis and function of glycolipids and polyglycerolphosphate lipoteichoic acid in gram-positive bacteria of the phylum Firmicutes
    • Reichmann NT, Gr undling A. 2011. Location, synthesis and function of glycolipids and polyglycerolphosphate lipoteichoic acid in gram-positive bacteria of the phylum Firmicutes. FEMS Microbiol. Lett. 319:97-105
    • (2011) FEMS Microbiol. Lett. , vol.319 , pp. 97-105
    • Reichmann, N.T.1    Grundling, A.2
  • 108
    • 84874472480 scopus 로고    scopus 로고
    • Small molecule inhibitor of lipoteichoic acid synthesis is an antibiotic for gram-positive bacteria
    • Richter SG, Elli D, KimHK, Hendrickx AP, Sorg JA, et al. 2013. Small molecule inhibitor of lipoteichoic acid synthesis is an antibiotic for gram-positive bacteria. Proc. Natl. Acad. Sci. USA 110:3531-36
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 3531-3536
    • Richter, S.G.1    Elli, D.2    Kim, H.K.3    Hendrickx, A.P.4    Sorg, J.A.5
  • 109
    • 84866951984 scopus 로고    scopus 로고
    • D-Alanylation of lipoteichoic acids confers resistance to cationic peptides in group B Streptococcus by increasing the cell wall density
    • Saar-Dover R, Bitler A, Nezer R, Shmuel-Galia L, Firon A, et al. 2012. D-Alanylation of lipoteichoic acids confers resistance to cationic peptides in group B Streptococcus by increasing the cell wall density. PLoS Pathog. 8:e1002891
    • (2012) PLoS Pathog. , vol.8 , pp. e1002891
    • Saar-Dover, R.1    Bitler, A.2    Nezer, R.3    Shmuel-Galia, L.4    Firon, A.5
  • 110
    • 65449173646 scopus 로고    scopus 로고
    • Distinct and essential morphogenic functions for wall- and lipo-teichoic acids in Bacillus subtilis
    • Schirner K, Marles-Wright J, Lewis RJ, Errington J. 2009. Distinct and essential morphogenic functions for wall- and lipo-teichoic acids in Bacillus subtilis. EMBO J. 28:830-42
    • (2009) EMBO J. , vol.28 , pp. 830-842
    • Schirner, K.1    Marles-Wright, J.2    Lewis, R.J.3    Errington, J.4
  • 111
    • 41549141383 scopus 로고    scopus 로고
    • A new model of pneumococcal lipoteichoic acid structure resolves biochemical, biosynthetic, and serologic inconsistencies of the current model
    • Seo HS, Cartee RT, Pritchard DG, Nahm MH. 2008. A new model of pneumococcal lipoteichoic acid structure resolves biochemical, biosynthetic, and serologic inconsistencies of the current model. J. Bacteriol. 190:2379-87
    • (2008) J. Bacteriol. , vol.190 , pp. 2379-2387
    • Seo, H.S.1    Cartee, R.T.2    Pritchard, D.G.3    Nahm, M.H.4
  • 112
    • 66349088254 scopus 로고    scopus 로고
    • Recent progress on acylCoA: Lysophospholipid acyltransferase research
    • Shindou H, Hishikawa D, HarayamaT,YukiK, Shimizu T. 2009. Recent progress on acylCoA: lysophospholipid acyltransferase research. J. Lipid Res. 50(Suppl.):S46-51
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL. , pp. S46-51
    • Shindou, H.1    Hishikawa, D.2    Harayama, T.3    Yuki, K.4    Shimizu, T.5
  • 113
    • 11144322172 scopus 로고    scopus 로고
    • Autolysis of Lactococcus lactis is increased upon D-alanine depletion of peptidoglycan and lipoteichoic acids
    • Steen A, Palumbo E, Deghorain M, Cocconcelli PS, Delcour J, et al. 2005. Autolysis of Lactococcus lactis is increased upon D-alanine depletion of peptidoglycan and lipoteichoic acids. J. Bacteriol. 187:114-24
    • (2005) J. Bacteriol. , vol.187 , pp. 114-124
    • Steen, A.1    Palumbo, E.2    Deghorain, M.3    Cocconcelli, P.S.4    Delcour, J.5
  • 114
    • 0025708583 scopus 로고
    • Polysaccharides from Peptostreptococcus anaerobius and structure of the species-specific antigen
    • Stortz CA, Cherniak R, Jones RG, Treber TD, Reinhardt DJ. 1990. Polysaccharides from Peptostreptococcus anaerobius and structure of the species-specific antigen. Carbohydr. Res. 207:101-20
    • (1990) Carbohydr. Res. , vol.207 , pp. 101-120
    • Stortz, C.A.1    Cherniak, R.2    Jones, R.G.3    Treber, T.D.4    Reinhardt, D.J.5
  • 116
    • 0020533106 scopus 로고
    • Biosynthesis of D-alanyl-lipoteichoic acid: Role of diglyceride kinase in the synthesis of phosphatidylglycerol for chain elongation
    • Taron DJ, ChildsWC III, Neuhaus FC. 1983. Biosynthesis of D-alanyl-lipoteichoic acid: role of diglyceride kinase in the synthesis of phosphatidylglycerol for chain elongation. J. Bacteriol. 154:1110-16
    • (1983) J. Bacteriol. , vol.154 , pp. 1110-1116
    • Taron, D.J.1    Childs, W.C.2    Neuhaus, F.C.3
  • 117
    • 33749266224 scopus 로고    scopus 로고
    • Opsonic antibodies to Enterococcus faecalis strain 12030 are directed against lipoteichoic acid
    • Theilacker C, Kaczynski Z, Kropec A, Fabretti F, SangeT, et al. 2006. Opsonic antibodies to Enterococcus faecalis strain 12030 are directed against lipoteichoic acid. Infec. Immun. 74:5703-12
    • (2006) Infec. Immun. , vol.74 , pp. 5703-5712
    • Theilacker, C.1    Kaczynski, Z.2    Kropec, A.3    Fabretti, F.4    Sange, T.5
  • 118
    • 84858224547 scopus 로고    scopus 로고
    • Protection against Staphylococcus aureus by antibody to the polyglycerolphosphate backbone of heterologous lipoteichoic acid
    • Theilacker C, Kropec A, Hammer F, Sava I, Wobser D, et al. 2012. Protection against Staphylococcus aureus by antibody to the polyglycerolphosphate backbone of heterologous lipoteichoic acid. J. Infect. Dis. 205:1076-85
    • (2012) J. Infect. Dis. , vol.205 , pp. 1076-1085
    • Theilacker, C.1    Kropec, A.2    Hammer, F.3    Sava, I.4    Wobser, D.5
  • 119
    • 7344250495 scopus 로고
    • Chemical and immunological properties of a species-specific carbohydrate of pneumococci
    • Tillett WS, GoebelWF, Avery OT. 1930. Chemical and immunological properties of a species-specific carbohydrate of pneumococci. J. Exp. Med. 52:895-900
    • (1930) J. Exp. Med. , vol.52 , pp. 895-900
    • Tillett, W.S.1    Goebel, W.F.2    Avery, O.T.3
  • 120
    • 0014200202 scopus 로고
    • Choline in the cell wall of a bacterium: Novel type of polymer-linked choline in Pneumococcus
    • Tomasz A. 1967. Choline in the cell wall of a bacterium: novel type of polymer-linked choline in Pneumococcus. Science 157:694-97
    • (1967) Science , vol.157 , pp. 694-697
    • Tomasz, A.1
  • 121
    • 0014227389 scopus 로고
    • Biological consequences of the replacement of choline by ethanolamine in the cell wall of Pneumococcus: Chain formation, loss of transformability, and loss of autolysis
    • Tomasz A. 1968. Biological consequences of the replacement of choline by ethanolamine in the cell wall of Pneumococcus: chain formation, loss of transformability, and loss of autolysis. Proc. Natl. Acad. Sci. USA 59:86-93
    • (1968) Proc. Natl. Acad. Sci. USA , vol.59 , pp. 86-93
    • Tomasz, A.1
  • 122
    • 0015156375 scopus 로고
    • Abnormal autolytic enzyme in a pneumococcus with altered teichoic acid composition
    • Tomasz A, Westphal M. 1971. Abnormal autolytic enzyme in a pneumococcus with altered teichoic acid composition. Proc. Natl. Acad. Sci. USA 68:2627-30
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 2627-2630
    • Tomasz, A.1    Westphal, M.2
  • 123
    • 0022513681 scopus 로고
    • Structural studies on lipoteichoic acids from four Listeria strains
    • Uchikawa K, Sekikawa I, Azuma I. 1986. Structural studies on lipoteichoic acids from four Listeria strains. J. Bacteriol. 168:115-22
    • (1986) J. Bacteriol. , vol.168 , pp. 115-122
    • Uchikawa, K.1    Sekikawa, I.2    Azuma, I.3
  • 124
    • 0035838447 scopus 로고    scopus 로고
    • Biosynthesis of D-alanyl-lipoteichoic acid: The tertiary structure of apo-D-alanyl carrier protein
    • Volkman BF, Zhang Q, Debabov DV, Rivera E, Kresheck GC, Neuhaus FC. 2001. Biosynthesis of D-alanyl-lipoteichoic acid: the tertiary structure of apo-D-alanyl carrier protein. Biochemistry 40:7964-72
    • (2001) Biochemistry , vol.40 , pp. 7964-7972
    • Volkman, B.F.1    Zhang, Q.2    Debabov, D.V.3    Rivera, E.4    Kresheck, G.C.5    Neuhaus, F.C.6
  • 125
    • 0035061124 scopus 로고    scopus 로고
    • Identification of the teichoic acid phosphorylcholine esterase in Streptococcus pneumoniae
    • Vollmer W, Tomasz A. 2001. Identification of the teichoic acid phosphorylcholine esterase in Streptococcus pneumoniae. Mol. Microbiol. 39:1610-22
    • (2001) Mol. Microbiol. , vol.39 , pp. 1610-1622
    • Vollmer, W.1    Tomasz, A.2
  • 126
    • 84878392079 scopus 로고    scopus 로고
    • The choline-binding protein PspC of Streptococcus pneumoniae interacts with the C-terminal heparin-binding domain of vitronectin
    • Voss S, Hallstrom T, Saleh M, Burchhardt G, Pribyl T, et al. 2013. The choline-binding protein PspC of Streptococcus pneumoniae interacts with the C-terminal heparin-binding domain of vitronectin. J. Biol. Chem. 288:15614-27
    • (2013) J. Biol. Chem. , vol.288 , pp. 15614-15627
    • Voss, S.1    Hallstrom, T.2    Saleh, M.3    Burchhardt, G.4    Pribyl, T.5
  • 128
    • 70349900174 scopus 로고    scopus 로고
    • Two-enzyme systems for glycolipid and polyglycerolphosphate lipoteichoic acid synthesis in Listeria monocytogenes
    • Webb AJ, Karatsa-Dodgson M, Grundling A. 2009. Two-enzyme systems for glycolipid and polyglycerolphosphate lipoteichoic acid synthesis in Listeria monocytogenes. Mol. Microbiol. 74:299-314
    • (2009) Mol. Microbiol. , vol.74 , pp. 299-314
    • Webb, A.J.1    Karatsa-Dodgson, M.2    Grundling, A.3
  • 129
    • 67650000573 scopus 로고    scopus 로고
    • Phase 1/2 doubleblind, placebo-controlled, dose escalation, safety, and pharmacokinetic study of pagibaximab (BSYXA110), an antistaphylococcal monoclonal antibody for the prevention of staphylococcal bloodstream infections, in very-low-birth-weight neonates
    • Weisman LE, Thackray HM, Garcia-Prats JA, Nesin M, Schneider JH, et al. 2009. Phase 1/2 doubleblind, placebo-controlled, dose escalation, safety, and pharmacokinetic study of pagibaximab (BSYXA110), an antistaphylococcal monoclonal antibody for the prevention of staphylococcal bloodstream infections, in very-low-birth-weight neonates. Antimicrob. Agents Chemother. 53:2879-86
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 2879-2886
    • Weisman, L.E.1    Thackray, H.M.2    Garcia-Prats, J.A.3    Nesin, M.4    Schneider, J.H.5
  • 130
    • 80051494427 scopus 로고    scopus 로고
    • A randomized study of a monoclonal antibody (pagibaximab) to prevent staphylococcal sepsis
    • Weisman LE, Thackray HM, Steinhorn RH, WalshWF, Lassiter HA, et al. 2011. A randomized study of a monoclonal antibody (pagibaximab) to prevent staphylococcal sepsis. Pediatrics 128:271-79
    • (2011) Pediatrics , vol.128 , pp. 271-279
    • Weisman, L.E.1    Thackray, H.M.2    Steinhorn, R.H.3    Walsh, W.F.4    Lassiter, H.A.5
  • 131
    • 78751681333 scopus 로고    scopus 로고
    • Enzymatic activities and functional interdependencies of Bacillus subtilis lipoteichoic acid synthesis enzymes
    • Wörmann ME, Corrigan RM, Simpson PJ, Matthews SJ, Grundling A. 2011. Enzymatic activities and functional interdependencies of Bacillus subtilis lipoteichoic acid synthesis enzymes. Mol. Microbiol. 79:566-83
    • (2011) Mol. Microbiol. , vol.79 , pp. 566-583
    • Wörmann, M.E.1    Corrigan, R.M.2    Simpson, P.J.3    Matthews, S.J.4    Grundling, A.5
  • 133
    • 0023923648 scopus 로고
    • The function of galactosyl phosphorylpolyprenol in biosynthesis of lipoteichoic acid in Bacillus coagulans
    • Yokoyama K, Araki Y, Ito E. 1988. The function of galactosyl phosphorylpolyprenol in biosynthesis of lipoteichoic acid in Bacillus coagulans. Eur. J. Biochem. 173:453-58
    • (1988) Eur. J. Biochem. , vol.173 , pp. 453-458
    • Yokoyama, K.1    Araki, Y.2    Ito, E.3
  • 134
    • 57749097690 scopus 로고    scopus 로고
    • Crystal structure of DltA: Implications for the reactionmechanism of non-ribosomal peptide synthetase adenylation domains
    • Yonus H, Neumann P, Zimmermann S, May JJ, Marahiel MA, Stubbs MT. 2008. Crystal structure of DltA: implications for the reactionmechanism of non-ribosomal peptide synthetase adenylation domains. J. Biol. Chem. 283:32484-91
    • (2008) J. Biol. Chem. , vol.283 , pp. 32484-32491
    • Yonus, H.1    Neumann, P.2    Zimmermann, S.3    May, J.J.4    Marahiel, M.A.5    Stubbs, M.T.6


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