메뉴 건너뛰기




Volumn 13, Issue 1, 2013, Pages

Lipoproteins of slow-growing Mycobacteria carry three fatty acids and are N-acylated by Apolipoprotein N-Acyltransferase BCG-2070c

Author keywords

Apolipoprotein N acyltransferase; Lipidation; Lipoprotein; Mycobacteria; Tuberculosis

Indexed keywords

ACYLTRANSFERASE; APOLIPOPROTEIN N ACYLTRANSFERASE; BCG VACCINE; FATTY ACID; LIPOPROTEIN; UNCLASSIFIED DRUG; APOLIPOPROTEIN N-ACYLTRANSFERASE;

EID: 84884966147     PISSN: None     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-13-223     Document Type: Article
Times cited : (25)

References (68)
  • 1
    • 7944226058 scopus 로고    scopus 로고
    • Lipoproteins of Mycobacterium tuberculosis: An abundant and functionally diverse class of cell envelope components
    • DOI 10.1016/j.femsre.2004.06.002, PII S0168644504000476
    • Lipoproteins of Mycobacterium tuberculosis: an abundant and functionally diverse class of cell envelope components. Sutcliffe IC, Harrington DJ, FEMS Microbiol Rev 2004 28 5 645 659 10.1016/j.femsre.2004.06.002 15539077 (Pubitemid 39469923)
    • (2004) FEMS Microbiology Reviews , vol.28 , Issue.5 , pp. 645-659
    • Sutcliffe, I.C.1    Harrington, D.J.2
  • 2
    • 33645972887 scopus 로고    scopus 로고
    • A database of bacterial lipoproteins (DOLOP) with functional assignments to predicted lipoproteins
    • 10.1128/JB.188.8.2761-2773.2006 16585737
    • A database of bacterial lipoproteins (DOLOP) with functional assignments to predicted lipoproteins. Babu MM, Priya ML, Selvan AT, Madera M, Gough J, Aravind L, Sankaran K, J Bacteriol 2006 188 8 2761 2773 10.1128/JB.188.8.2761- 2773.2006 16585737
    • (2006) J Bacteriol , vol.188 , Issue.8 , pp. 2761-2773
    • Babu, M.M.1    Priya, M.L.2    Selvan, A.T.3    Madera, M.4    Gough, J.5    Aravind, L.6    Sankaran, K.7
  • 3
    • 79251472718 scopus 로고    scopus 로고
    • Lipoproteins of bacterial pathogens
    • 10.1128/IAI.00682-10 20974828
    • Lipoproteins of bacterial pathogens. Kovacs-Simon A, Titball RW, Michell SL, Infect Immun 2011 79 2 548 561 10.1128/IAI.00682-10 20974828
    • (2011) Infect Immun , vol.79 , Issue.2 , pp. 548-561
    • Kovacs-Simon, A.1    Titball, R.W.2    Michell, S.L.3
  • 4
    • 27744493918 scopus 로고    scopus 로고
    • The twin-arginine translocation pathway of Mycobacterium smegmatis is functional and required for the export of mycobacterial β-lactamases
    • DOI 10.1128/JB.187.22.7667-7679.2005
    • The twin-arginine translocation pathway of Mycobacterium smegmatis is functional and required for the export of mycobacterial beta-lactamases. McDonough JA, Hacker KE, Flores AR, Pavelka MS Jr, Braunstein M, J Bacteriol 2005 187 22 7667 7679 10.1128/JB.187.22.7667-7679.2005 16267291 (Pubitemid 41587705)
    • (2005) Journal of Bacteriology , vol.187 , Issue.22 , pp. 7667-7679
    • McDonough, J.A.1    Hacker, K.E.2    Flores, A.R.3    Pavelka Jr., M.S.4    Braunstein, M.5
  • 6
    • 80053280679 scopus 로고    scopus 로고
    • Lipoprotein sorting in bacteria
    • 10.1146/annurev-micro-090110-102859 21663440
    • Lipoprotein sorting in bacteria. Okuda S, Tokuda H, Annu Rev Microbiol 2011 65 239 259 10.1146/annurev-micro-090110-102859 21663440
    • (2011) Annu Rev Microbiol , vol.65 , pp. 239-259
    • Okuda, S.1    Tokuda, H.2
  • 7
    • 33947413501 scopus 로고    scopus 로고
    • Lipoprotein synthesis in mycobacteria
    • DOI 10.1099/mic.0.2006/000216-0
    • Lipoprotein synthesis in mycobacteria. Rezwan M, Grau T, Tschumi A, Sander P, Microbiology 2007 153 Pt 3 652 658 17322184 (Pubitemid 46444362)
    • (2007) Microbiology , vol.153 , Issue.3 , pp. 652-658
    • Rezwan, M.1    Grau, T.2    Tschumi, A.3    Sander, P.4
  • 8
    • 0033787084 scopus 로고    scopus 로고
    • A new ABC transporter mediating the detachment of lipid-modified proteins from membranes
    • 10.1038/35008635 10783239
    • A new ABC transporter mediating the detachment of lipid-modified proteins from membranes. Yakushi T, Masuda K, Narita S, Matsuyama S, Tokuda H, Nat Cell Biol 2000 2 4 212 218 10.1038/35008635 10783239
    • (2000) Nat Cell Biol , vol.2 , Issue.4 , pp. 212-218
    • Yakushi, T.1    Masuda, K.2    Narita, S.3    Matsuyama, S.4    Tokuda, H.5
  • 9
    • 80052551712 scopus 로고    scopus 로고
    • Overexpression of LolCDE allows deletion of the Escherichia coli gene encoding apolipoprotein N-acyltransferase
    • 10.1128/JB.05013-11 21742870
    • Overexpression of LolCDE allows deletion of the Escherichia coli gene encoding apolipoprotein N-acyltransferase. Narita S, Tokuda H, J Bacteriol 2011 193 18 4832 4840 10.1128/JB.05013-11 21742870
    • (2011) J Bacteriol , vol.193 , Issue.18 , pp. 4832-4840
    • Narita, S.1    Tokuda, H.2
  • 10
    • 0000587078 scopus 로고    scopus 로고
    • Biosynthesis of lipoproteins
    • Washington, DC: American Society for Microbiology: Neidhardt FC, 2, 2nd edn
    • Biosynthesis of lipoproteins. Wu HC, Escherichia coli and Salmonella typhimurium: cellular and molecular biology Washington, DC: American Society for Microbiology: Neidhardt FC, vol. 2, 2nd edn 1996 1005 1014
    • (1996) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 1005-1014
    • Wu, H.C.1
  • 11
    • 34250303119 scopus 로고    scopus 로고
    • Identification of essential residues in apolipoprotein N-acyl transferase, a member of the CN hydrolase family
    • DOI 10.1128/JB.00099-07
    • Identification of essential residues in apolipoprotein N-acyl transferase, a member of the CN hydrolase family. Vidal-Ingigliardi D, Lewenza S, Buddelmeijer N, J Bacteriol 2007 189 12 4456 4464 10.1128/JB.00099-07 17416655 (Pubitemid 46919633)
    • (2007) Journal of Bacteriology , vol.189 , Issue.12 , pp. 4456-4464
    • Vidal-Ingigliardi, D.1    Lewenza, S.2    Buddelmeijer, N.3
  • 12
    • 70350437568 scopus 로고    scopus 로고
    • Identification of apolipoprotein N-acyltransferase (Lnt) in mycobacteria
    • 10.1074/jbc.M109.022715 19661058
    • Identification of apolipoprotein N-acyltransferase (Lnt) in mycobacteria. Tschumi A, Nai C, Auchli Y, Hunziker P, Gehrig P, Keller P, Grau T, Sander P, J Biol Chem 2009 284 40 27146 27156 10.1074/jbc.M109.022715 19661058
    • (2009) J Biol Chem , vol.284 , Issue.40 , pp. 27146-27156
    • Tschumi, A.1    Nai, C.2    Auchli, Y.3    Hunziker, P.4    Gehrig, P.5    Keller, P.6    Grau, T.7    Sander, P.8
  • 16
    • 84867033119 scopus 로고    scopus 로고
    • The ppm operon is essential for acylation and glycosylation of lipoproteins in Corynebacterium glutamicum
    • 10.1371/journal.pone.0046225 23029442
    • The ppm operon is essential for acylation and glycosylation of lipoproteins in Corynebacterium glutamicum. Mohiman N, Argentini M, Batt SM, Cornu D, Masi M, Eggeling L, Besra G, Bayan N, PLoS One 2012 7 9 46225 10.1371/journal.pone.0046225 23029442
    • (2012) PLoS One , vol.7 , Issue.9 , pp. 546225
    • Mohiman, N.1    Argentini, M.2    Batt, S.M.3    Cornu, D.4    Masi, M.5    Eggeling, L.6    Besra, G.7    Bayan, N.8
  • 17
    • 0021789468 scopus 로고
    • Modification and processing of internalized signal sequences of prolipoprotein in Escherichia coli and in Bacillus subtilis
    • Modification and processing of internalized signal sequences of prolipoprotein in Escherichia coli and in Bacillus subtilis. Hayashi S, Chang SY, Chang S, Giam CZ, Wu HC, J Biol Chem 1985 260 9 5753 5759 2985611 (Pubitemid 15001138)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.9 , pp. 5753-5759
    • Hayashi, S.1    Chang, S.-Y.2    Chang, S.3
  • 18
    • 67649763474 scopus 로고    scopus 로고
    • The Triacylated ATP Binding Cluster Transporter Substrate-binding Lipoprotein of Staphylococcus aureus Functions as a Native Ligand for Toll-like Receptor 2
    • 19139093
    • The Triacylated ATP Binding Cluster Transporter Substrate-binding Lipoprotein of Staphylococcus aureus Functions as a Native Ligand for Toll-like Receptor 2. Kurokawa K, Lee H, Roh KB, Asanuma M, Kim YS, Nakayama H, Shiratsuchi A, Choi Y, Takeuchi O, Kang HJ, et al. J Biol Chem 2009 284 13 8406 8411 19139093
    • (2009) J Biol Chem , vol.284 , Issue.13 , pp. 8406-8411
    • Kurokawa, K.1    Lee, H.2    Roh, K.B.3    Asanuma, M.4    Kim, Y.S.5    Nakayama, H.6    Shiratsuchi, A.7    Choi, Y.8    Takeuchi, O.9    Kang, H.J.10
  • 19
    • 66149125243 scopus 로고    scopus 로고
    • Characterization of N-terminal structure of TLR2-activating lipoprotein in Staphylococcus aureus
    • 10.1074/jbc.M900429200 19218237
    • Characterization of N-terminal structure of TLR2-activating lipoprotein in Staphylococcus aureus. Tawaratsumida K, Furuyashiki M, Katsumoto M, Fujimoto Y, Fukase K, Suda Y, Hashimoto M, J Biol Chem 2009 284 14 9147 9152 10.1074/jbc.M900429200 19218237
    • (2009) J Biol Chem , vol.284 , Issue.14 , pp. 9147-9152
    • Tawaratsumida, K.1    Furuyashiki, M.2    Katsumoto, M.3    Fujimoto, Y.4    Fukase, K.5    Suda, Y.6    Hashimoto, M.7
  • 20
    • 84870061381 scopus 로고    scopus 로고
    • Lipoproteins in bacteria: Structures and biosynthetic pathways
    • 10.1111/febs.12041 23094979
    • Lipoproteins in bacteria: structures and biosynthetic pathways. Nakayama H, Kurokawa K, Lee BL, Febs J 2012 279 23 4247 4268 10.1111/febs.12041 23094979
    • (2012) Febs J , vol.279 , Issue.23 , pp. 4247-4268
    • Nakayama, H.1    Kurokawa, K.2    Lee, B.L.3
  • 21
    • 79959565162 scopus 로고    scopus 로고
    • The acylation state of surface lipoproteins of mollicute Acholeplasma laidlawii
    • 10.1074/jbc.M111.231316 21540185
    • The acylation state of surface lipoproteins of mollicute Acholeplasma laidlawii. Serebryakova MV, Demina IA, Galyamina MA, Kondratov IG, Ladygina VG, Govorun VM, J Biol Chem 2011 286 26 22769 22776 10.1074/jbc.M111.231316 21540185
    • (2011) J Biol Chem , vol.286 , Issue.26 , pp. 22769-22776
    • Serebryakova, M.V.1    Demina, I.A.2    Galyamina, M.A.3    Kondratov, I.G.4    Ladygina, V.G.5    Govorun, V.M.6
  • 22
    • 84859739265 scopus 로고    scopus 로고
    • Novel bacterial lipoprotein structures conserved in low-GC content gram-positive bacteria are recognized by Toll-like receptor 2
    • 10.1074/jbc.M111.292235 22303020
    • Novel bacterial lipoprotein structures conserved in low-GC content gram-positive bacteria are recognized by Toll-like receptor 2. Kurokawa K, Ryu KH, Ichikawa R, Masuda A, Kim MS, Lee H, Chae JH, Shimizu T, Saitoh T, Kuwano K, et al. J Biol Chem 2012 287 16 13170 13181 10.1074/jbc.M111.292235 22303020
    • (2012) J Biol Chem , vol.287 , Issue.16 , pp. 13170-13181
    • Kurokawa, K.1    Ryu, K.H.2    Ichikawa, R.3    Masuda, A.4    Kim, M.S.5    Lee, H.6    Chae, J.H.7    Shimizu, T.8    Saitoh, T.9    Kuwano, K.10
  • 24
    • 55549136412 scopus 로고    scopus 로고
    • LspA inactivation in Mycobacterium tuberculosis results in attenuation without affecting phagosome maturation arrest
    • 18832305
    • LspA inactivation in Mycobacterium tuberculosis results in attenuation without affecting phagosome maturation arrest. Rampini SK, Selchow P, Keller C, Ehlers S, Bottger EC, Sander P, Microbiology 2008 154 Pt 10 2991 3001 18832305
    • (2008) Microbiology , vol.154 , Issue.PART 10 , pp. 2991-3001
    • Rampini, S.K.1    Selchow, P.2    Keller, C.3    Ehlers, S.4    Bottger, E.C.5    Sander, P.6
  • 25
    • 84870526465 scopus 로고    scopus 로고
    • Bacterial cell wall macroamphiphiles: Pathogen-/microbe-associated molecular patterns detected by mammalian innate immune system
    • 10.1016/j.biochi.2012.06.007 22706280
    • Bacterial cell wall macroamphiphiles: pathogen-/microbe-associated molecular patterns detected by mammalian innate immune system. Ray A, Cot M, Puzo G, Gilleron M, Nigou J, Biochimie 2013 95 1 33 42 10.1016/j.biochi.2012.06. 007 22706280
    • (2013) Biochimie , vol.95 , Issue.1 , pp. 33-42
    • Ray, A.1    Cot, M.2    Puzo, G.3    Gilleron, M.4    Nigou, J.5
  • 26
    • 67349217383 scopus 로고    scopus 로고
    • TLR2 and its co-receptors determine responses of macrophages and dendritic cells to lipoproteins of Mycobacterium tuberculosis
    • 10.1016/j.cellimm.2009.03.008 19362712
    • TLR2 and its co-receptors determine responses of macrophages and dendritic cells to lipoproteins of Mycobacterium tuberculosis. Drage MG, Pecora ND, Hise AG, Febbraio M, Silverstein RL, Golenbock DT, Boom WH, Harding CV, Cell Immunol 2009 258 1 29 37 10.1016/j.cellimm.2009.03.008 19362712
    • (2009) Cell Immunol , vol.258 , Issue.1 , pp. 29-37
    • Drage, M.G.1    Pecora, N.D.2    Hise, A.G.3    Febbraio, M.4    Silverstein, R.L.5    Golenbock, D.T.6    Boom, W.H.7    Harding, C.V.8
  • 27
    • 77949550080 scopus 로고    scopus 로고
    • Regulation of antigen presentation by Mycobacterium tuberculosis: A role for Toll-like receptors
    • 10.1038/nrmicro2321 20234378
    • Regulation of antigen presentation by Mycobacterium tuberculosis: a role for Toll-like receptors. Harding CV, Boom WH, Nat Rev Microbiol 2010 8 4 296 307 10.1038/nrmicro2321 20234378
    • (2010) Nat Rev Microbiol , vol.8 , Issue.4 , pp. 296-307
    • Harding, C.V.1    Boom, W.H.2
  • 30
    • 84869887217 scopus 로고    scopus 로고
    • Recombinant live vaccine candidates against tuberculosis
    • 10.1016/j.copbio.2012.03.007 22483201
    • Recombinant live vaccine candidates against tuberculosis. Kaufmann SH, Gengenbacher M, Curr Opin Biotechnol 2012 23 6 900 907 10.1016/j.copbio.2012.03. 007 22483201
    • (2012) Curr Opin Biotechnol , vol.23 , Issue.6 , pp. 900-907
    • Kaufmann, S.H.1    Gengenbacher, M.2
  • 31
    • 0345576939 scopus 로고    scopus 로고
    • Gene Replacement in Mycobacterium tuberculosis and Mycobacterium bovis BCG Using rpsL as a Dominant Negative Selectable Marker
    • 21341071
    • Gene Replacement in Mycobacterium tuberculosis and Mycobacterium bovis BCG Using rpsL as a Dominant Negative Selectable Marker. Sander P, Springer B, Bottger EC, Methods Mol Med 2001 54 93 104 21341071
    • (2001) Methods Mol Med , vol.54 , pp. 93-104
    • Sander, P.1    Springer, B.2    Bottger, E.C.3
  • 32
    • 0028979580 scopus 로고
    • RpsL+: A dominant selectable marker for gene replacement in mycobacteria
    • 10.1111/j.1365-2958.1995.tb02324.x 7476195
    • rpsL+: a dominant selectable marker for gene replacement in mycobacteria. Sander P, Meier A, Bottger EC, Mol Microbiol 1995 16 5 991 1000 10.1111/j.1365-2958.1995.tb02324.x 7476195
    • (1995) Mol Microbiol , vol.16 , Issue.5 , pp. 991-1000
    • Sander, P.1    Meier, A.2    Bottger, E.C.3
  • 35
    • 39149101861 scopus 로고    scopus 로고
    • A method for analyzing lipid-modified proteins with mass spectrometry
    • 10.1016/j.ab.2007.11.014 18078799
    • A method for analyzing lipid-modified proteins with mass spectrometry. Ujihara T, Sakurai I, Mizusawa N, Wada H, Anal Biochem 2008 374 2 429 431 10.1016/j.ab.2007.11.014 18078799
    • (2008) Anal Biochem , vol.374 , Issue.2 , pp. 429-431
    • Ujihara, T.1    Sakurai, I.2    Mizusawa, N.3    Wada, H.4
  • 36
    • 33645737729 scopus 로고    scopus 로고
    • LppX is a lipoprotein required for the translocation of phthiocerol dimycocerosates to the surface of Mycobacterium tuberculosis
    • 10.1038/sj.emboj.7601048 16541102
    • LppX is a lipoprotein required for the translocation of phthiocerol dimycocerosates to the surface of Mycobacterium tuberculosis. Sulzenbacher G, Canaan S, Bordat Y, Neyrolles O, Stadthagen G, Roig-Zamboni V, Rauzier J, Maurin D, Laval F, Daffe M, et al. Embo J 2006 25 7 1436 1444 10.1038/sj.emboj.7601048 16541102
    • (2006) Embo J , vol.25 , Issue.7 , pp. 1436-1444
    • Sulzenbacher, G.1    Canaan, S.2    Bordat, Y.3    Neyrolles, O.4    Stadthagen, G.5    Roig-Zamboni, V.6    Rauzier, J.7    Maurin, D.8    Laval, F.9    Daffe, M.10
  • 37
    • 0037329291 scopus 로고    scopus 로고
    • Interaction of the sensor module of Mycobacterium tuberculosis H37Rv KdpD with members of the Lpr family
    • DOI 10.1046/j.1365-2958.2003.03356.x
    • Interaction of the sensor module of Mycobacterium tuberculosis H37Rv KdpD with members of the Lpr family. Steyn AJ, Joseph J, Bloom BR, Mol Microbiol 2003 47 4 1075 1089 10.1046/j.1365-2958.2003.03356.x 12581360 (Pubitemid 36232802)
    • (2003) Molecular Microbiology , vol.47 , Issue.4 , pp. 1075-1089
    • Steyn, A.J.C.1    Joseph, J.2    Bloom, B.R.3
  • 38
    • 23944479701 scopus 로고    scopus 로고
    • The 19-kDa antigen of Mycobacterium tuberculosis is a major adhesin that binds the mannose receptor of THP-1 monocytic cells and promotes phagocytosis of mycobacteria
    • DOI 10.1016/j.micpath.2005.06.002, PII S0882401005000781
    • The 19-kDa antigen of Mycobacterium tuberculosis is a major adhesin that binds the mannose receptor of THP-1 monocytic cells and promotes phagocytosis of mycobacteria. Diaz-Silvestre H, Espinosa-Cueto P, Sanchez-Gonzalez A, Esparza-Ceron MA, Pereira-Suarez AL, Bernal-Fernandez G, Espitia C, Mancilla R, Microb Pathog 2005 39 3 97 107 10.1016/j.micpath.2005.06.002 16098710 (Pubitemid 41207213)
    • (2005) Microbial Pathogenesis , vol.39 , Issue.3 , pp. 97-107
    • Diaz-Silvestre, H.1    Espinosa-Cueto, P.2    Sanchez-Gonzalez, A.3    Esparza-Ceron, M.A.4    Pereira-Suarez, A.L.5    Bernal-Fernandez, G.6    Espitia, C.7    Mancilla, R.8
  • 39
    • 0002725473 scopus 로고
    • Mycobacterial lipids: Chemistry and biological activities
    • The W. B. Saunders Co. Philadelphia, PA: Youmans GP
    • Mycobacterial lipids: chemistry and biological activities. Goren MB, Brennan PJ, Tuberculosis The W. B. Saunders Co., Philadelphia, PA: Youmans GP 1979 63 193
    • (1979) Tuberculosis , pp. 63-193
    • Goren, M.B.1    Brennan, P.J.2
  • 40
    • 0025871351 scopus 로고
    • Phosphatidylethanolamine is not essential for the N-acylation of apolipoprotein in Escherichia coli
    • Phosphatidylethanolamine is not essential for the N-acylation of apolipoprotein in Escherichia coli. Gupta SD, Dowhan W, Wu HC, J Biol Chem 1991 266 15 9983 9986 2033085 (Pubitemid 21906752)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.15 , pp. 9983-9986
    • Gupta, S.D.1    Dowhan, W.2    Wu, H.C.3
  • 41
    • 80051503015 scopus 로고    scopus 로고
    • Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase
    • 10.1074/jbc.M111.243519 21676878
    • Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase. Hillmann F, Argentini M, Buddelmeijer N, J Biol Chem 2011 286 32 27936 27946 10.1074/jbc.M111.243519 21676878
    • (2011) J Biol Chem , vol.286 , Issue.32 , pp. 27936-27946
    • Hillmann, F.1    Argentini, M.2    Buddelmeijer, N.3
  • 42
    • 0023032318 scopus 로고
    • Transfer of fatty acids from the 1-position of phosphatidylethanolamine to the major outer membrane lipoprotein of Escherichia coli
    • Transfer of fatty acids from the 1-position of phosphatidylethanolamine to the major outer membrane lipoprotein of Escherichia coli. Jackowski S, Rock CO, J Biol Chem 1986 261 24 11328 11333 3525566 (Pubitemid 17216742)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.24 , pp. 11328-11333
    • Jackowski, S.1    Rock, C.O.2
  • 43
    • 0019159584 scopus 로고
    • Incorporation of acyl moieties of phospholipids into murein lipoprotein in intact cells of Escherichia coli by phospholipid vesicle fusion
    • Incorporation of acyl moieties of phospholipids into murein lipoprotein in intact cells of Escherichia coli by phospholipid vesicle fusion. Lai JS, Wu HC, J Bacteriol 1980 144 1 451 453 6998965 (Pubitemid 11211073)
    • (1980) Journal of Bacteriology , vol.144 , Issue.1 , pp. 451-453
    • Lai, J.S.1    Wu, H.C.2
  • 44
    • 0018879508 scopus 로고
    • Assembly of outer membrane lipoprotein in an Escherichia coli mutant with a single amino acid replacement within the signal sequence of prolipoprotein
    • Assembly of outer membrane lipoprotein in an Escherichia coli mutant with a single amino acid replacement within the signal sequence of prolipoprotein. Lin JJ, Kanazawa H, Wu HC, J Bacteriol 1980 141 2 550 557 6154034 (Pubitemid 10110843)
    • (1980) Journal of Bacteriology , vol.141 , Issue.2 , pp. 550-557
    • Lin, J.J.C.1    Kanazawa, H.2    Wu, H.C.3
  • 45
    • 57649185429 scopus 로고    scopus 로고
    • N-Terminal clustering of the O-glycosylation sites in the Mycobacterium tuberculosis lipoprotein SodC
    • 18842962
    • N-Terminal clustering of the O-glycosylation sites in the Mycobacterium tuberculosis lipoprotein SodC. Sartain MJ, Belisle JT, Glycobiology 2009 19 1 38 51 18842962
    • (2009) Glycobiology , vol.19 , Issue.1 , pp. 38-51
    • Sartain, M.J.1    Belisle, J.T.2
  • 46
    • 0027514448 scopus 로고
    • Expression of the Mycobacterium tuberculosis 19-kilodalton antigen in Mycobacterium smegmatis: Immunological analysis and evidence of glycosylation
    • Expression of the Mycobacterium tuberculosis 19-kilodalton antigen in Mycobacterium smegmatis: immunological analysis and evidence of glycosylation. Garbe T, Harris D, Vordermeier M, Lathigra R, Ivanyi J, Young D, Infect Immun 1993 61 1 260 267 8418047 (Pubitemid 23015425)
    • (1993) Infection and Immunity , vol.61 , Issue.1 , pp. 260-267
    • Garbe, T.1    Harris, D.2    Vordermeier, M.3    Lathigra, R.4    Ivanyi, J.5    Young, D.6
  • 47
    • 75349096668 scopus 로고    scopus 로고
    • The essential Escherichia coli apolipoprotein N-acyltransferase (Lnt) exists as an extracytoplasmic thioester acyl-enzyme intermediate
    • The essential Escherichia coli apolipoprotein N-acyltransferase (Lnt) exists as an extracytoplasmic thioester acyl-enzyme intermediate. Buddelmeijer N, Young R, Biochemistry 2009 49 2 341 346
    • (2009) Biochemistry , vol.49 , Issue.2 , pp. 341-346
    • Buddelmeijer, N.1    Young, R.2
  • 48
    • 84866321497 scopus 로고    scopus 로고
    • Functional analyses of mycobacterial lipoprotein diacylglyceryl transferase and comparative secretome analysis of a mycobacterial lgt mutant
    • 10.1128/JB.00127-12 22609911
    • Functional analyses of mycobacterial lipoprotein diacylglyceryl transferase and comparative secretome analysis of a mycobacterial lgt mutant. Tschumi A, Grau T, Albrecht D, Rezwan M, Antelmann H, Sander P, J Bacteriol 2012 194 15 3938 3949 10.1128/JB.00127-12 22609911
    • (2012) J Bacteriol , vol.194 , Issue.15 , pp. 3938-3949
    • Tschumi, A.1    Grau, T.2    Albrecht, D.3    Rezwan, M.4    Antelmann, H.5    Sander, P.6
  • 50
    • 0000812428 scopus 로고    scopus 로고
    • Identification of a virulence gene cluster of Mycobacterium tuberculosis by signature-tagged transposon mutagenesis
    • DOI 10.1046/j.1365-2958.1999.01593.x
    • Identification of a virulence gene cluster of Mycobacterium tuberculosis by signature-tagged transposon mutagenesis. Camacho LR, Ensergueix D, Perez E, Gicquel B, Guilhot C, Mol Microbiol 1999 34 2 257 267 10.1046/j.1365-2958.1999. 01593.x 10564470 (Pubitemid 29486244)
    • (1999) Molecular Microbiology , vol.34 , Issue.2 , pp. 257-267
    • Camacho, L.R.1    Ensergueix, D.2    Perez, E.3    Gicquel, B.4    Guilhot, C.5
  • 52
    • 34648828887 scopus 로고    scopus 로고
    • A mutant of Mycobacterium tuberculosis lacking the 19-kDa lipoprotein Rv3763 is highly attenuated in vivo but retains potent vaccinogenic properties
    • DOI 10.1016/j.vaccine.2007.07.042, PII S0264410X0700833X
    • A mutant of Mycobacterium tuberculosis lacking the 19-kDa lipoprotein Rv3763 is highly attenuated in vivo but retains potent vaccinogenic properties. Henao-Tamayo M, Junqueira-Kipnis AP, Ordway D, Gonzales-Juarrero M, Stewart GR, Young DB, Wilkinson RJ, Basaraba RJ, Orme IM, Vaccine 2007 25 41 7153 7159 10.1016/j.vaccine.2007.07.042 17804126 (Pubitemid 47464672)
    • (2007) Vaccine , vol.25 , Issue.41 , pp. 7153-7159
    • Henao-Tamayo, M.1    Junqueira-Kipnis, A.P.2    Ordway, D.3    Gonzales-Juarrero, M.4    Stewart, G.R.5    Young, D.B.6    Wilkinson, R.J.7    Basaraba, R.J.8    Orme, I.M.9
  • 53
    • 84878505261 scopus 로고    scopus 로고
    • The lpqS knockout mutant of Mycobacterium tuberculosis is attenuated in Macrophages
    • The lpqS knockout mutant of Mycobacterium tuberculosis is attenuated in Macrophages. Sakthi S, Narayanan S, Microbiol Res 2013
    • (2013) Microbiol Res
    • Sakthi, S.1    Narayanan, S.2
  • 54
    • 84866900148 scopus 로고    scopus 로고
    • Lipidated promiscuous peptides vaccine for tuberculosis-endemic regions
    • 10.1016/j.molmed.2012.07.008 22939171
    • Lipidated promiscuous peptides vaccine for tuberculosis-endemic regions. Gowthaman U, Rai PK, Khan N, Jackson DC, Agrewala JN, Trends Mol Med 2012 18 10 607 614 10.1016/j.molmed.2012.07.008 22939171
    • (2012) Trends Mol Med , vol.18 , Issue.10 , pp. 607-614
    • Gowthaman, U.1    Rai, P.K.2    Khan, N.3    Jackson, D.C.4    Agrewala, J.N.5
  • 56
    • 84864009033 scopus 로고    scopus 로고
    • Environment-mediated accumulation of diacyl lipoproteins over their triacyl counterparts in Staphylococcus aureus
    • 10.1128/JB.00314-12 22467779
    • Environment-mediated accumulation of diacyl lipoproteins over their triacyl counterparts in Staphylococcus aureus. Kurokawa K, Kim MS, Ichikawa R, Ryu KH, Dohmae N, Nakayama H, Lee BL, J Bacteriol 2012 194 13 3299 3306 10.1128/JB.00314-12 22467779
    • (2012) J Bacteriol , vol.194 , Issue.13 , pp. 3299-3306
    • Kurokawa, K.1    Kim, M.S.2    Ichikawa, R.3    Ryu, K.H.4    Dohmae, N.5    Nakayama, H.6    Lee, B.L.7
  • 57
    • 0014101231 scopus 로고
    • Positional distribution of fatty acids in phospholipids from Mycobacteria
    • 4964827
    • Positional distribution of fatty acids in phospholipids from Mycobacteria. Okuyama H, Kankura T, Nojima S, J Biochem 1967 61 6 732 737 4964827
    • (1967) J Biochem , vol.61 , Issue.6 , pp. 732-737
    • Okuyama, H.1    Kankura, T.2    Nojima, S.3
  • 58
    • 34548608447 scopus 로고    scopus 로고
    • Crystal Structure of the TLR1-TLR2 Heterodimer Induced by Binding of a Tri-Acylated Lipopeptide
    • DOI 10.1016/j.cell.2007.09.008, PII S009286740701152X
    • Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide. Jin MS, Kim SE, Heo JY, Lee ME, Kim HM, Paik SG, Lee H, Lee JO, Cell 2007 130 6 1071 1082 10.1016/j.cell.2007.09.008 17889651 (Pubitemid 47410281)
    • (2007) Cell , vol.130 , Issue.6 , pp. 1071-1082
    • Jin, M.S.1    Kim, S.E.2    Heo, J.Y.3    Lee, M.E.4    Kim, H.M.5    Paik, S.-G.6    Lee, H.7    Lee, J.-O.8
  • 59
    • 71749118913 scopus 로고    scopus 로고
    • Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer
    • 10.1016/j.immuni.2009.09.018 19931471
    • Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer. Kang JY, Nan X, Jin MS, Youn SJ, Ryu YH, Mah S, Han SH, Lee H, Paik SG, Lee JO, Immunity 2009 31 6 873 884 10.1016/j.immuni.2009.09.018 19931471
    • (2009) Immunity , vol.31 , Issue.6 , pp. 873-884
    • Kang, J.Y.1    Nan, X.2    Jin, M.S.3    Youn, S.J.4    Ryu, Y.H.5    Mah, S.6    Han, S.H.7    Lee, H.8    Paik, S.G.9    Lee, J.O.10
  • 61
    • 84867619205 scopus 로고    scopus 로고
    • Innate immune gene polymorphisms in tuberculosis
    • 10.1128/IAI.00443-12 22825450
    • Innate immune gene polymorphisms in tuberculosis. Azad AK, Sadee W, Schlesinger LS, Infect Immun 2012 80 10 3343 3359 10.1128/IAI.00443-12 22825450
    • (2012) Infect Immun , vol.80 , Issue.10 , pp. 3343-3359
    • Azad, A.K.1    Sadee, W.2    Schlesinger, L.S.3
  • 62
    • 0029896457 scopus 로고    scopus 로고
    • Bacterial glycoproteins: A link between glycosylation and proteolytic cleavage of a 19 kDa antigen from Mycobacterium tuberculosis
    • Bacterial glycoproteins: a link between glycosylation and proteolytic cleavage of a 19 kDa antigen from Mycobacterium tuberculosis. Herrmann JL, O'Gaora P, Gallagher A, Thole JE, Young DB, Embo J 1996 15 14 3547 3554 8670858 (Pubitemid 26239767)
    • (1996) EMBO Journal , vol.15 , Issue.14 , pp. 3547-3554
    • Herrmann, J.L.1    O'Gaora, P.2    Gallagher, A.3    Thole, J.E.R.4    Young, D.B.5
  • 63
    • 28444440285 scopus 로고    scopus 로고
    • Proteomics-based consensus prediction of protein retention in a bacterial membrane
    • DOI 10.1002/pmic.200402080
    • Proteomics-based consensus prediction of protein retention in a bacterial membrane. Tjalsma H, van Dijl JM, Proteomics 2005 5 17 4472 4482 10.1002/pmic.200402080 16220534 (Pubitemid 41739924)
    • (2005) Proteomics , vol.5 , Issue.17 , pp. 4472-4482
    • Tjalsma, H.1    Van Dijl, J.M.2
  • 64
    • 84866887386 scopus 로고    scopus 로고
    • Global assessment of genomic regions required for growth in Mycobacterium tuberculosis
    • 10.1371/journal.ppat.1002946 23028335
    • Global assessment of genomic regions required for growth in Mycobacterium tuberculosis. Zhang YJ, Ioerger TR, Huttenhower C, Long JE, Sassetti CM, Sacchettini JC, Rubin EJ, PLoS Pathog 2012 8 9 1002946 10.1371/journal.ppat. 1002946 23028335
    • (2012) PLoS Pathog , vol.8 , Issue.9 , pp. 51002946
    • Zhang, Y.J.1    Ioerger, T.R.2    Huttenhower, C.3    Long, J.E.4    Sassetti, C.M.5    Sacchettini, J.C.6    Rubin, E.J.7
  • 65
    • 12544257510 scopus 로고    scopus 로고
    • Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli
    • 15513925
    • Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli. Robichon C, Vidal-Ingigliardi D, Pugsley AP, J Biol Chem 2005 280 2 974 983 15513925
    • (2005) J Biol Chem , vol.280 , Issue.2 , pp. 974-983
    • Robichon, C.1    Vidal-Ingigliardi, D.2    Pugsley, A.P.3
  • 66
    • 77649105362 scopus 로고    scopus 로고
    • Mycobacterial outer membranes: In search of proteins
    • 10.1016/j.tim.2009.12.005 20060722
    • Mycobacterial outer membranes: in search of proteins. Niederweis M, Danilchanka O, Huff J, Hoffmann C, Engelhardt H, Trends Microbiol 2010 18 3 109 116 10.1016/j.tim.2009.12.005 20060722
    • (2010) Trends Microbiol , vol.18 , Issue.3 , pp. 109-116
    • Niederweis, M.1    Danilchanka, O.2    Huff, J.3    Hoffmann, C.4    Engelhardt, H.5
  • 67
    • 77956988767 scopus 로고    scopus 로고
    • A phylum level perspective on bacterial cell envelope architecture
    • 10.1016/j.tim.2010.06.005 20637628
    • A phylum level perspective on bacterial cell envelope architecture. Sutcliffe IC, Trends Microbiol 2010 18 10 464 470 10.1016/j.tim.2010.06.005 20637628
    • (2010) Trends Microbiol , vol.18 , Issue.10 , pp. 464-470
    • Sutcliffe, I.C.1
  • 68
    • 49449107199 scopus 로고    scopus 로고
    • Direct visualization of the outer membrane of mycobacteria and corynebacteria in their native state
    • 10.1128/JB.01919-07 18567661
    • Direct visualization of the outer membrane of mycobacteria and corynebacteria in their native state. Zuber B, Chami M, Houssin C, Dubochet J, Griffiths G, Daffe M, J Bacteriol 2008 190 16 5672 5680 10.1128/JB.01919-07 18567661
    • (2008) J Bacteriol , vol.190 , Issue.16 , pp. 5672-5680
    • Zuber, B.1    Chami, M.2    Houssin, C.3    Dubochet, J.4    Griffiths, G.5    Daffe, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.