메뉴 건너뛰기




Volumn 197, Issue 6, 2015, Pages 1075-1082

Small-molecule inhibitors of gram-negative lipoprotein trafficking discovered by phenotypic screening

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ABC TRANSPORTER LOLCDE; ANTIBIOTIC AGENT; BACTERIAL PROTEIN; DOXYCYCLINE; IMIDAZOLE DERIVATIVE; LIPOPROTEIN; MEROPENEM; NALIDIXIC ACID; POLYMYXIN B; RIFAMPICIN; UNCLASSIFIED DRUG; VANCOMYCIN; ANTIFUNGAL AGENT; ANTIINFECTIVE AGENT;

EID: 84923286190     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.02352-14     Document Type: Article
Times cited : (65)

References (46)
  • 1
    • 80053280679 scopus 로고    scopus 로고
    • Lipoprotein sorting in bacteria
    • Okuda S, Tokuda H. 2011. Lipoprotein sorting in bacteria. Annu Rev Microbiol 65:239-259. http://dx.doi.org/10.1146/annurev-micro-090110-102859.
    • (2011) Annu Rev Microbiol , vol.65 , pp. 239-259
    • Okuda, S.1    Tokuda, H.2
  • 2
    • 0028981022 scopus 로고
    • A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane
    • Matsuyama S, Tajima T, Tokuda H. 1995. A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane. EMBO J 14:3365-3372.
    • (1995) EMBO J , vol.14 , pp. 3365-3372
    • Matsuyama, S.1    Tajima, T.2    Tokuda, H.3
  • 3
    • 0033787084 scopus 로고    scopus 로고
    • A new ABC transporter mediating the detachment of lipid-modified proteins from membranes
    • Yakushi T, Masuda K, Narita S, Matsuyama S, Tokuda H. 2000. A new ABC transporter mediating the detachment of lipid-modified proteins from membranes. Nat Cell Biol 2:212-218. http://dx.doi.org/10.1038/35008635.
    • (2000) Nat Cell Biol , vol.2 , pp. 212-218
    • Yakushi, T.1    Masuda, K.2    Narita, S.3    Matsuyama, S.4    Tokuda, H.5
  • 4
    • 0030663775 scopus 로고    scopus 로고
    • A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli
    • Matsuyama S, Yokota N, Tokuda H. 1997. A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli. EMBO J 16:6947-6955. http://dx.doi.org/10.1093/emboj/16.23.6947.
    • (1997) EMBO J , vol.16 , pp. 6947-6955
    • Matsuyama, S.1    Yokota, N.2    Tokuda, H.3
  • 5
    • 84902276774 scopus 로고    scopus 로고
    • Secretion of bacterial lipoproteins: through the cytoplasmic membrane, the periplasm and beyond
    • Zuckert WR. 2014. Secretion of bacterial lipoproteins: through the cytoplasmic membrane, the periplasm and beyond. Biochim Biophys Acta 1843:1509-1516. http://dx.doi.org/10.1016/j.bbamcr.2014.04.022.
    • (2014) Biochim Biophys Acta , vol.1843 , pp. 1509-1516
    • Zuckert, W.R.1
  • 7
    • 42549171131 scopus 로고    scopus 로고
    • Federal funding for the study of antimicrobial resistance in nosocomial pathogens: no ESKAPE
    • Rice LB. 2008. Federal funding for the study of antimicrobial resistance in nosocomial pathogens: no ESKAPE. J Infect Dis 197:1079-1081. http://dx.doi.org/10.1086/533452.
    • (2008) J Infect Dis , vol.197 , pp. 1079-1081
    • Rice, L.B.1
  • 8
    • 39449103059 scopus 로고    scopus 로고
    • The epidemic of antibiotic-resistant infections: a call to action for the medical community from the Infectious Diseases Society of America
    • Spellberg B, Guidos R, Gilbert D, Bradley J, Boucher HW, Scheld WM, Bartlett JG, Edwards J, Jr. 2008. The epidemic of antibiotic-resistant infections: a call to action for the medical community from the Infectious Diseases Society of America. Clin Infect Dis 46:155-164. http://dx.doi.org/10.1086/524891.
    • (2008) Clin Infect Dis , vol.46 , pp. 155-164
    • Spellberg, B.1    Guidos, R.2    Gilbert, D.3    Bradley, J.4    Boucher, H.W.5    Scheld, W.M.6    Bartlett, J.G.7    Edwards, J.8
  • 9
    • 0036175948 scopus 로고    scopus 로고
    • Disruption of lolCDE, encoding an ATP-binding cassette transporter, is lethal for Escherichia coli and prevents release of lipoproteins from the inner membrane
    • Narita S, Tanaka K, Matsuyama S, Tokuda H. 2002. Disruption of lolCDE, encoding an ATP-binding cassette transporter, is lethal for Escherichia coli and prevents release of lipoproteins from the inner membrane. J Bacteriol 184:1417-1422. http://dx.doi.org/10.1128/JB.184.5.1417-1422.2002.
    • (2002) J Bacteriol , vol.184 , pp. 1417-1422
    • Narita, S.1    Tanaka, K.2    Matsuyama, S.3    Tokuda, H.4
  • 10
    • 0032515174 scopus 로고    scopus 로고
    • Genetic analyses of the in vivo function of LolA, a periplasmic chaperone involved in the outer membrane localization of Escherichia coli lipoproteins
    • Tajima T, Yokota N, Matsuyama S, Tokuda H. 1998. Genetic analyses of the in vivo function of LolA, a periplasmic chaperone involved in the outer membrane localization of Escherichia coli lipoproteins. FEBS Lett 439:51-54. http://dx.doi.org/10.1016/S0014-5793(98)01334-9.
    • (1998) FEBS Lett , vol.439 , pp. 51-54
    • Tajima, T.1    Yokota, N.2    Matsuyama, S.3    Tokuda, H.4
  • 11
    • 0034750231 scopus 로고    scopus 로고
    • Deletion of lolB, encoding an outer membrane lipoprotein, is lethal for Escherichia coli and causes accumulation of lipoprotein localization intermediates in the periplasm
    • Tanaka K, Matsuyama SI, Tokuda H. 2001. Deletion of lolB, encoding an outer membrane lipoprotein, is lethal for Escherichia coli and causes accumulation of lipoprotein localization intermediates in the periplasm. J Bacteriol 183:6538-6542. http://dx.doi.org/10.1128/JB.183.22.6538-6542.2001.
    • (2001) J Bacteriol , vol.183 , pp. 6538-6542
    • Tanaka, K.1    Matsuyama, S.I.2    Tokuda, H.3
  • 12
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci U S A 97:6640-6645. http://dx.doi.org/10.1073/pnas.120163297.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 14
    • 0035997382 scopus 로고    scopus 로고
    • Lipopolysaccharide endotoxins
    • Raetz CR, Whitfield C. 2002. Lipopolysaccharide endotoxins. Annu Rev Biochem 71:635-700. http://dx.doi.org/10.1146/annurev.biochem.71.110601.135414.
    • (2002) Annu Rev Biochem , vol.71 , pp. 635-700
    • Raetz, C.R.1    Whitfield, C.2
  • 15
    • 72949111486 scopus 로고    scopus 로고
    • Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically: approved standard
    • 9th ed, M07-A8, vol 29, no 2. Clinical and Laboratory Standards Institute, Wayne, PA
    • Clinical and Laboratory Standards Institute. 2009. Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically: approved standard, 9th ed, M07-A8, vol 29, no 2. Clinical and Laboratory Standards Institute, Wayne, PA.
    • (2009)
  • 17
    • 29944445261 scopus 로고    scopus 로고
    • Different modes of action of naphthyridones in Gram-positive and Gram-negative bacteria
    • Buurman ET, Johnson KD, Kelly RK, MacCormack K. 2006. Different modes of action of naphthyridones in Gram-positive and Gram-negative bacteria. Antimicrob Agents Chemother 50:385-387. http://dx.doi.org/10.1128/AAC.50.1.385-387.2006.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 385-387
    • Buurman, E.T.1    Johnson, K.D.2    Kelly, R.K.3    MacCormack, K.4
  • 18
    • 0022341427 scopus 로고
    • Kinetics of uptake and incorporation of meso-diaminopimelic acid in different Escherichia coli strains
    • Wientjes FB, Pas E, Taschner PE, Woldringh CL. 1985. Kinetics of uptake and incorporation of meso-diaminopimelic acid in different Escherichia coli strains. J Bacteriol 164:331-337.
    • (1985) J Bacteriol , vol.164 , pp. 331-337
    • Wientjes, F.B.1    Pas, E.2    Taschner, P.E.3    Woldringh, C.L.4
  • 19
    • 0014465913 scopus 로고
    • Improved agar gradient-plate technique
    • Hunt DE, Sandham HJ. 1969. Improved agar gradient-plate technique. Appl Microbiol 17:329-330.
    • (1969) Appl Microbiol , vol.17 , pp. 329-330
    • Hunt, D.E.1    Sandham, H.J.2
  • 20
    • 84885081302 scopus 로고    scopus 로고
    • Bacterial cytological profiling rapidly identifies the cellular pathways targeted by antibacterial molecules
    • Nonejuie P, Burkart M, Pogliano K, Pogliano J. 2013. Bacterial cytological profiling rapidly identifies the cellular pathways targeted by antibacterial molecules. Proc Natl Acad SciUS A 110:16169-16174. http://dx.doi.org/10.1073/pnas.1311066110.
    • (2013) Proc Natl Acad SciUS A , vol.110 , pp. 16169-16174
    • Nonejuie, P.1    Burkart, M.2    Pogliano, K.3    Pogliano, J.4
  • 22
    • 0022999829 scopus 로고
    • Trimeric structure and localization of the major lipoprotein in the cell surface of Escherichia coli
    • Choi DS, Yamada H, Mizuno T, Mizushima S. 1986. Trimeric structure and localization of the major lipoprotein in the cell surface of Escherichia coli. J Biol Chem 261:8953-8957.
    • (1986) J Biol Chem , vol.261 , pp. 8953-8957
    • Choi, D.S.1    Yamada, H.2    Mizuno, T.3    Mizushima, S.4
  • 23
    • 0015524158 scopus 로고
    • The assembly of a structural lipoprotein in the envelope of Escherichia coli
    • Inouye M, Shaw J, Shen C. 1972. The assembly of a structural lipoprotein in the envelope of Escherichia coli. J Biol Chem 247:8154-8159.
    • (1972) J Biol Chem , vol.247 , pp. 8154-8159
    • Inouye, M.1    Shaw, J.2    Shen, C.3
  • 24
    • 0018608655 scopus 로고
    • Existence of the bound form of prolipoprotein in Escherichia coli B cells treated with globomycin
    • Inukai M, Takeuchi M, Shimizu K, Arai M. 1979. Existence of the bound form of prolipoprotein in Escherichia coli B cells treated with globomycin. J Bacteriol 140:1098-1101.
    • (1979) J Bacteriol , vol.140 , pp. 1098-1101
    • Inukai, M.1    Takeuchi, M.2    Shimizu, K.3    Arai, M.4
  • 25
    • 0031002073 scopus 로고    scopus 로고
    • Lethality of the covalent linkage between mislocalized major outer membrane lipoprotein and the peptidoglycan of Escherichia coli
    • Yakushi T, Tajima T, Matsuyama S, Tokuda H. 1997. Lethality of the covalent linkage between mislocalized major outer membrane lipoprotein and the peptidoglycan of Escherichia coli. J Bacteriol 179:2857-2862.
    • (1997) J Bacteriol , vol.179 , pp. 2857-2862
    • Yakushi, T.1    Tajima, T.2    Matsuyama, S.3    Tokuda, H.4
  • 26
    • 84858650670 scopus 로고    scopus 로고
    • Myxobacterium-produced antibiotic TA (myxovirescin) inhibits type II signal peptidase
    • Xiao Y, Gerth K, Muller R, Wall D. 2012. Myxobacterium-produced antibiotic TA (myxovirescin) inhibits type II signal peptidase. Antimicrob Agents Chemother 56:2014-2021. http://dx.doi.org/10.1128/AAC.06148-11.
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 2014-2021
    • Xiao, Y.1    Gerth, K.2    Muller, R.3    Wall, D.4
  • 27
    • 0019351717 scopus 로고
    • Preferential selection of deletion mutations of the outer membrane lipoprotein gene of Escherichia coli by globomycin
    • Zwiebel LJ, Inukai M, Nakamura K, Inouye M. 1981. Preferential selection of deletion mutations of the outer membrane lipoprotein gene of Escherichia coli by globomycin. J Bacteriol 145:654-656.
    • (1981) J Bacteriol , vol.145 , pp. 654-656
    • Zwiebel, L.J.1    Inukai, M.2    Nakamura, K.3    Inouye, M.4
  • 28
    • 0018242617 scopus 로고
    • Mechanism of action of globomycin
    • Inukai M, Takeuchi M, Shimizu K, Arai M. 1978. Mechanism of action of globomycin. J Antibiot (Tokyo) 31:1203-1205. http://dx.doi.org/10.7164/antibiotics.31.1203.
    • (1978) J Antibiot (Tokyo) , vol.31 , pp. 1203-1205
    • Inukai, M.1    Takeuchi, M.2    Shimizu, K.3    Arai, M.4
  • 29
    • 77952363712 scopus 로고    scopus 로고
    • Reconstitution of outer membrane protein assembly from purified components
    • Hagan CL, Kim S, Kahne D. 2010. Reconstitution of outer membrane protein assembly from purified components. Science 328:890-892. http://dx.doi.org/10.1126/science.1188919.
    • (2010) Science , vol.328 , pp. 890-892
    • Hagan, C.L.1    Kim, S.2    Kahne, D.3
  • 30
    • 33745202589 scopus 로고    scopus 로고
    • YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli
    • Malinverni JC, Werner J, Kim S, Sklar JG, Kahne D, Misra R, Silhavy TJ. 2006. YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli. Mol Microbiol 61:151-164. http://dx.doi.org/10.1111/j.1365-2958.2006.05211.x.
    • (2006) Mol Microbiol , vol.61 , pp. 151-164
    • Malinverni, J.C.1    Werner, J.2    Kim, S.3    Sklar, J.G.4    Kahne, D.5    Misra, R.6    Silhavy, T.J.7
  • 31
    • 17444381980 scopus 로고    scopus 로고
    • Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli
    • Wu T, Malinverni J, Ruiz N, Kim S, Silhavy TJ, Kahne D. 2005. Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 121:235-245. http://dx.doi.org/10.1016/j.cell.2005.02.015.
    • (2005) Cell , vol.121 , pp. 235-245
    • Wu, T.1    Malinverni, J.2    Ruiz, N.3    Kim, S.4    Silhavy, T.J.5    Kahne, D.6
  • 32
    • 77950438894 scopus 로고    scopus 로고
    • Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane
    • Chng SS, Ruiz N, Chimalakonda G, Silhavy TJ, Kahne D. 2010. Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane. Proc Natl Acad Sci U S A 107:5363-5368. http://dx.doi.org/10.1073/pnas.0912872107.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 5363-5368
    • Chng, S.S.1    Ruiz, N.2    Chimalakonda, G.3    Silhavy, T.J.4    Kahne, D.5
  • 33
    • 69249230732 scopus 로고    scopus 로고
    • Transport of lipopolysaccharide across the cell envelope: the long road of discovery
    • Ruiz N, Kahne D, Silhavy TJ. 2009. Transport of lipopolysaccharide across the cell envelope: the long road of discovery. Nat Rev Microbiol 7:677-683. http://dx.doi.org/10.1038/nrmicro2184.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 677-683
    • Ruiz, N.1    Kahne, D.2    Silhavy, T.J.3
  • 34
    • 33746852673 scopus 로고    scopus 로고
    • Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli
    • Wu T, McCandlish AC, Gronenberg LS, Chng SS, Silhavy TJ, Kahne D. 2006. Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli. Proc Natl Acad Sci U S A 103:11754-11759. http://dx.doi.org/10.1073/pnas.0604744103.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11754-11759
    • Wu, T.1    McCandlish, A.C.2    Gronenberg, L.S.3    Chng, S.S.4    Silhavy, T.J.5    Kahne, D.6
  • 35
    • 78650497005 scopus 로고    scopus 로고
    • Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases
    • Paradis-Bleau C, Markovski M, Uehara T, Lupoli TJ, Walker S, Kahne DE, Bernhardt TG. 2010. Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases. Cell 143:1110-1120. http://dx.doi.org/10.1016/j.cell.2010.11.037.
    • (2010) Cell , vol.143 , pp. 1110-1120
    • Paradis-Bleau, C.1    Markovski, M.2    Uehara, T.3    Lupoli, T.J.4    Walker, S.5    Kahne, D.E.6    Bernhardt, T.G.7
  • 37
    • 79959539151 scopus 로고    scopus 로고
    • ABC transporters involved in the biogenesis of the outer membrane in Gram-negative bacteria
    • Narita S. 2011. ABC transporters involved in the biogenesis of the outer membrane in Gram-negative bacteria. Biosci Biotechnol Biochem 75:1044-1054. http://dx.doi.org/10.1271/bbb.110115.
    • (2011) Biosci Biotechnol Biochem , vol.75 , pp. 1044-1054
    • Narita, S.1
  • 38
    • 70350446622 scopus 로고    scopus 로고
    • Membrane topology and functional importance of the periplasmic region of ABC transporter LolCDE
    • Yasuda M, Iguchi-Yokoyama A, Matsuyama S, Tokuda H, Narita S. 2009. Membrane topology and functional importance of the periplasmic region of ABC transporter LolCDE. Biosci Biotechnol Biochem 73:2310-2316. http://dx.doi.org/10.1271/bbb.90451.
    • (2009) Biosci Biotechnol Biochem , vol.73 , pp. 2310-2316
    • Yasuda, M.1    Iguchi-Yokoyama, A.2    Matsuyama, S.3    Tokuda, H.4    Narita, S.5
  • 39
    • 84871722765 scopus 로고    scopus 로고
    • Functional differentiation of structurally similar membrane subunits of the ABC transporter LolCDE complex
    • Mizutani M, Mukaiyama K, Xiao J, Mori M, Satou R, Narita S, Okuda S, Tokuda H. 2013. Functional differentiation of structurally similar membrane subunits of the ABC transporter LolCDE complex. FEBS Lett 587:23-29. http://dx.doi.org/10.1016/j.febslet.2012.11.009.
    • (2013) FEBS Lett , vol.587 , pp. 23-29
    • Mizutani, M.1    Mukaiyama, K.2    Xiao, J.3    Mori, M.4    Satou, R.5    Narita, S.6    Okuda, S.7    Tokuda, H.8
  • 40
    • 65249085615 scopus 로고    scopus 로고
    • Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB
    • Okuda S, Tokuda H. 2009. Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB. Proc Natl Acad Sci U S A 106:5877-5882. http://dx.doi.org/10.1073/pnas.0900896106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 5877-5882
    • Okuda, S.1    Tokuda, H.2
  • 41
    • 0035782884 scopus 로고    scopus 로고
    • Preventing drug access to targets: cell surface permeability barriers and active efflux in bacteria
    • Nikaido H. 2001. Preventing drug access to targets: cell surface permeability barriers and active efflux in bacteria. Semin Cell Dev Biol 12:215-223. http://dx.doi.org/10.1006/scdb.2000.0247.
    • (2001) Semin Cell Dev Biol , vol.12 , pp. 215-223
    • Nikaido, H.1
  • 44
    • 84455161855 scopus 로고    scopus 로고
    • Colistin-resistant, lipopolysaccharide-deficient Acinetobacter baumannii responds to lipopolysaccharide loss through increased expression of genes involved in the synthesis and transport of lipoproteins, phospholipids, and poly-beta-1,6-N-acetylglucosamine
    • Henry R, Vithanage N, Harrison P, Seemann T, Coutts S, Moffatt JH, Nation RL, Li J, Harper M, Adler B, Boyce JD. 2012. Colistin-resistant, lipopolysaccharide-deficient Acinetobacter baumannii responds to lipopolysaccharide loss through increased expression of genes involved in the synthesis and transport of lipoproteins, phospholipids, and poly-beta-1,6-N-acetylglucosamine. Antimicrob Agents Chemother 56:59-69. http://dx.doi.org/10.1128/AAC.05191-11.
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 59-69
    • Henry, R.1    Vithanage, N.2    Harrison, P.3    Seemann, T.4    Coutts, S.5    Moffatt, J.H.6    Nation, R.L.7    Li, J.8    Harper, M.9    Adler, B.10    Boyce, J.D.11
  • 45
    • 34250353151 scopus 로고    scopus 로고
    • Characterization of the Pseudomonas aeruginosa Lol system as a lipoprotein sorting mechanism
    • Tanaka SY, Narita S, Tokuda H. 2007. Characterization of the Pseudomonas aeruginosa Lol system as a lipoprotein sorting mechanism. J Biol Chem 282:13379-13384. http://dx.doi.org/10.1074/jbc.M611840200.
    • (2007) J Biol Chem , vol.282 , pp. 13379-13384
    • Tanaka, S.Y.1    Narita, S.2    Tokuda, H.3
  • 46
    • 34250351484 scopus 로고    scopus 로고
    • Amino acids at positions 3 and 4 determine the membrane specificity of Pseudomonas aeruginosa lipoproteins
    • Narita S, Tokuda H. 2007. Amino acids at positions 3 and 4 determine the membrane specificity of Pseudomonas aeruginosa lipoproteins. J Biol Chem 282:13372-13378. http://dx.doi.org/10.1074/jbc.M611839200.
    • (2007) J Biol Chem , vol.282 , pp. 13372-13378
    • Narita, S.1    Tokuda, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.