메뉴 건너뛰기




Volumn 3, Issue 9, 2017, Pages 624-633

Neisseria gonorrhoeae Lytic Transglycosylases LtgA and LtgD Reduce Host Innate Immune Signaling through TLR2 and NOD2

Author keywords

innate immunity; lysozyme; lytic transglycosylase; Neisseria gonorrhoeae; NOD2; peptidoglycan

Indexed keywords

CASPASE RECRUITMENT DOMAIN PROTEIN 15; GLYCOSYLTRANSFERASE; INTERLEUKIN 1BETA; LYSOZYME; LYTIC TRANSGLYCOSYLASE A; LYTIC TRANSGLYCOSYLASE D; MEMBRANE PROTEIN; MURAMIC ACID; PEPTIDOGLYCAN; TOLL LIKE RECEPTOR 2; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CYTOKINE; NOD2 PROTEIN, HUMAN; TLR2 PROTEIN, HUMAN;

EID: 85029219278     PISSN: None     EISSN: 23738227     Source Type: Journal    
DOI: 10.1021/acsinfecdis.6b00088     Document Type: Article
Times cited : (27)

References (49)
  • 1
    • 77950343791 scopus 로고    scopus 로고
    • Pattern Recognition Receptors and Inflammation
    • Takeuchi, O. and Akira, S. (2010) Pattern Recognition Receptors and Inflammation Cell 140 (6) 805-820 10.1016/j.cell.2010.01.022
    • (2010) Cell , vol.140 , Issue.6 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 2
    • 0020071653 scopus 로고
    • Detection, isolation, and analysis of a released Bordetella pertussis product toxic to cultured tracheal cells
    • Goldman, W. E., Klapper, D. G., and Baseman, J. B. (1982) Detection, isolation, and analysis of a released Bordetella pertussis product toxic to cultured tracheal cells Infect. Immun. 36 (2) 782-794
    • (1982) Infect. Immun. , vol.36 , Issue.2 , pp. 782-794
    • Goldman, W.E.1    Klapper, D.G.2    Baseman, J.B.3
  • 3
    • 0018948535 scopus 로고
    • Release of soluble peptidoglycan from growing gonococci: Demonstration of anhydro-muramyl-containing fragments
    • Sinha, R. K. and Rosenthal, R. S. (1980) Release of soluble peptidoglycan from growing gonococci: demonstration of anhydro-muramyl-containing fragments Infect. Immun. 29 (3) 914-925
    • (1980) Infect. Immun. , vol.29 , Issue.3 , pp. 914-925
    • Sinha, R.K.1    Rosenthal, R.S.2
  • 4
    • 0021326947 scopus 로고
    • Ability of monomeric peptidoglycan fragments from Neisseria gonorrhoeae to damage human fallopian-tube mucosa
    • Melly, M. A., McGee, Z. A., and Rosenthal, R. S. (1984) Ability of monomeric peptidoglycan fragments from Neisseria gonorrhoeae to damage human fallopian-tube mucosa J. Infect. Dis. 149 (3) 378-386 10.1093/infdis/149.3.378
    • (1984) J. Infect. Dis. , vol.149 , Issue.3 , pp. 378-386
    • Melly, M.A.1    McGee, Z.A.2    Rosenthal, R.S.3
  • 5
    • 50249175927 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae Uses Two Lytic Transglycosylases to Produce Cytotoxic Peptidoglycan Monomers
    • Cloud-Hansen, K. A., Hackett, K. T., Garcia, D. L., and Dillard, J. P. (2008) Neisseria gonorrhoeae Uses Two Lytic Transglycosylases To Produce Cytotoxic Peptidoglycan Monomers J. Bacteriol. 190 (17) 5989-5994 10.1128/JB.00506-08
    • (2008) J. Bacteriol. , vol.190 , Issue.17 , pp. 5989-5994
    • Cloud-Hansen, K.A.1    Hackett, K.T.2    Garcia, D.L.3    Dillard, J.P.4
  • 9
    • 0037458665 scopus 로고    scopus 로고
    • Host Recognition of Bacterial Muramyl Dipeptide Mediated through NOD2. Implications for Crohn's Disease
    • Inohara, N. (2003) Host Recognition of Bacterial Muramyl Dipeptide Mediated through NOD2. Implications for Crohn's Disease J. Biol. Chem. 278 (8) 5509-5512 10.1074/jbc.C200673200
    • (2003) J. Biol. Chem. , vol.278 , Issue.8 , pp. 5509-5512
    • Inohara, N.1
  • 10
    • 84855253242 scopus 로고    scopus 로고
    • Expression, purification, and characterization of recombinant NOD1 (NLRC1): A NLR family member
    • Askari, N., Correa, R. G., Zhai, D., and Reed, J. C. (2012) Expression, purification, and characterization of recombinant NOD1 (NLRC1): A NLR family member J. Biotechnol. 157 (1) 75-81 10.1016/j.jbiotec.2011.10.007
    • (2012) J. Biotechnol. , vol.157 , Issue.1 , pp. 75-81
    • Askari, N.1    Correa, R.G.2    Zhai, D.3    Reed, J.C.4
  • 11
    • 84865434771 scopus 로고    scopus 로고
    • The innate immune protein Nod2 binds directly to MDP, a bacterial cell wall fragment
    • Grimes, C. L., Ariyananda, L. D. Z., Melnyk, J. E., and O'Shea, E. K. (2012) The innate immune protein Nod2 binds directly to MDP, a bacterial cell wall fragment J. Am. Chem. Soc. 134 (33) 13535-13537 10.1021/ja303883c
    • (2012) J. Am. Chem. Soc. , vol.134 , Issue.33 , pp. 13535-13537
    • Grimes, C.L.1    Ariyananda, L.D.Z.2    Melnyk, J.E.3    O'Shea, E.K.4
  • 12
    • 84863336565 scopus 로고    scopus 로고
    • Pathogen sensing by nucleotide-binding oligomerization domain-containing protein 2 (NOD2) is mediated by direct binding to muramyl dipeptide and ATP
    • Mo, J., Boyle, J. P., Howard, C. B., Monie, T. P., Davis, B. K., and Duncan, J. A. (2012) Pathogen sensing by nucleotide-binding oligomerization domain-containing protein 2 (NOD2) is mediated by direct binding to muramyl dipeptide and ATP J. Biol. Chem. 287 (27) 23057-23067 10.1074/jbc.M112.344283
    • (2012) J. Biol. Chem. , vol.287 , Issue.27 , pp. 23057-23067
    • Mo, J.1    Boyle, J.P.2    Howard, C.B.3    Monie, T.P.4    Davis, B.K.5    Duncan, J.A.6
  • 13
    • 7944220803 scopus 로고    scopus 로고
    • Toll-like receptor 2-dependent bacterial sensing does not occur via peptidoglycan recognition
    • Travassos, L. H., Girardin, S. E., Philpott, D. J., Blanot, D., Nahori, M.-A., Werts, C., and Boneca, I. G. (2004) Toll-like receptor 2-dependent bacterial sensing does not occur via peptidoglycan recognition EMBO Rep. 5 (10) 1000-1006 10.1038/sj.embor.7400248
    • (2004) EMBO Rep. , vol.5 , Issue.10 , pp. 1000-1006
    • Travassos, L.H.1    Girardin, S.E.2    Philpott, D.J.3    Blanot, D.4    Nahori, M.-A.5    Werts, C.6    Boneca, I.G.7
  • 14
    • 0021836821 scopus 로고
    • Soluble non-cross-linked peptidoglycan polymers stimulate monocyte-macrophage inflammatory functions
    • Gold, M. R., Miller, C. L., and Mishell, R. I. (1985) Soluble non-cross-linked peptidoglycan polymers stimulate monocyte-macrophage inflammatory functions Infect. Immun. 49 (3) 731-741
    • (1985) Infect. Immun. , vol.49 , Issue.3 , pp. 731-741
    • Gold, M.R.1    Miller, C.L.2    Mishell, R.I.3
  • 15
    • 0018147421 scopus 로고
    • Activation of the alternate complement pathway by peptidoglycan from streptococcal cell wall
    • Greenblatt, J., Boackle, R. J., and Schwab, J. H. (1978) Activation of the alternate complement pathway by peptidoglycan from streptococcal cell wall Infect. Immun. 19 (1) 296-303
    • (1978) Infect. Immun. , vol.19 , Issue.1 , pp. 296-303
    • Greenblatt, J.1    Boackle, R.J.2    Schwab, J.H.3
  • 16
    • 0027159588 scopus 로고
    • Functional antagonism between vitamin D3 and retinoic acid in the regulation of CD14 and CD23 expression during monocytic differentiation of U-937 cells
    • Oberg, F., Botling, J., and Nilsson, K. (1993) Functional antagonism between vitamin D3 and retinoic acid in the regulation of CD14 and CD23 expression during monocytic differentiation of U-937 cells J. Immunol. 150 (8 Pt 1) 3487-3495
    • (1993) J. Immunol. , vol.150 , Issue.8 , pp. 3487-3495
    • Oberg, F.1    Botling, J.2    Nilsson, K.3
  • 17
    • 78049274222 scopus 로고    scopus 로고
    • Staphylococcal Peptidoglycan Co-Localizes with Nod2 and TLR2 and Activates Innate Immune Response via Both Receptors in Primary Murine Keratinocytes
    • Müller-Anstett, M. A., Müller, P., Albrecht, T., Nega, M., Wagener, J., Gao, Q., Kaesler, S., Schaller, M., Biedermann, T., and Götz, F. (2010) Staphylococcal Peptidoglycan Co-Localizes with Nod2 and TLR2 and Activates Innate Immune Response via Both Receptors in Primary Murine Keratinocytes PLoS One 5 (10) e13153 10.1371/journal.pone.0013153
    • (2010) PLoS One , vol.5 , Issue.10 , pp. e13153
    • Müller-Anstett, M.A.1    Müller, P.2    Albrecht, T.3    Nega, M.4    Wagener, J.5    Gao, Q.6    Kaesler, S.7    Schaller, M.8    Biedermann, T.9    Götz, F.10
  • 18
    • 77957827147 scopus 로고    scopus 로고
    • Natural Staphylococcus aureus-derived peptidoglycan fragments activate NOD2 and act as potent costimulators of the innate immune system exclusively in the presence of TLR signals
    • Volz, T., Nega, M., Buschmann, J., Kaesler, S., Guenova, E., Peschel, A., Rocken, M., Gotz, F., and Biedermann, T. (2010) Natural Staphylococcus aureus-derived peptidoglycan fragments activate NOD2 and act as potent costimulators of the innate immune system exclusively in the presence of TLR signals FASEB J. 24 (10) 4089-4102 10.1096/fj.09-151001
    • (2010) FASEB J. , vol.24 , Issue.10 , pp. 4089-4102
    • Volz, T.1    Nega, M.2    Buschmann, J.3    Kaesler, S.4    Guenova, E.5    Peschel, A.6    Rocken, M.7    Gotz, F.8    Biedermann, T.9
  • 19
    • 0344012591 scopus 로고    scopus 로고
    • The Lip Lipoprotein from Neisseria gonorrhoeae Stimulates Cytokine Release and NF-κB Activation in Epithelial Cells in a Toll-like Receptor 2-Dependent Manner
    • Fisette, P. L., Ram, S., Andersen, J. M., Guo, W., and Ingalls, R. R. (2003) The Lip Lipoprotein from Neisseria gonorrhoeae Stimulates Cytokine Release and NF-κB Activation in Epithelial Cells in a Toll-like Receptor 2-Dependent Manner J. Biol. Chem. 278 (47) 46252-46260 10.1074/jbc.M306587200
    • (2003) J. Biol. Chem. , vol.278 , Issue.47 , pp. 46252-46260
    • Fisette, P.L.1    Ram, S.2    Andersen, J.M.3    Guo, W.4    Ingalls, R.R.5
  • 20
    • 14844361310 scopus 로고    scopus 로고
    • Neisserial porin-induced dendritic cell activation is MyD88 and TLR2 dependent
    • Singleton, T. E., Massari, P., and Wetzler, L. M. (2005) Neisserial porin-induced dendritic cell activation is MyD88 and TLR2 dependent J. Immunol. 174 (6) 3545-3550 10.4049/jimmunol.174.6.3545
    • (2005) J. Immunol. , vol.174 , Issue.6 , pp. 3545-3550
    • Singleton, T.E.1    Massari, P.2    Wetzler, L.M.3
  • 21
    • 0037083638 scopus 로고    scopus 로고
    • Cutting edge: Immune stimulation by neisserial porins is Toll-like receptor 2 and MyD88 dependent
    • Massari, P., Henneke, P., Ho, Y., Latz, E., Golenbock, D. T., and Wetzler, L. M. (2002) Cutting edge: Immune stimulation by neisserial porins is Toll-like receptor 2 and MyD88 dependent J. Immunol. 168 (4) 1533-1537 10.4049/jimmunol.168.4.1533
    • (2002) J. Immunol. , vol.168 , Issue.4 , pp. 1533-1537
    • Massari, P.1    Henneke, P.2    Ho, Y.3    Latz, E.4    Golenbock, D.T.5    Wetzler, L.M.6
  • 22
    • 84899002698 scopus 로고    scopus 로고
    • Activation of NOD receptors by Neisseria gonorrhoeae modulates the innate immune response
    • Mavrogiorgos, N., Mekasha, S., Yang, Y., Kelliher, M. A., and Ingalls, R. R. (2013) Activation of NOD receptors by Neisseria gonorrhoeae modulates the innate immune response Innate Immunity 20, 377-389 10.1177/1753425913493453
    • (2013) Innate Immunity , vol.20 , pp. 377-389
    • Mavrogiorgos, N.1    Mekasha, S.2    Yang, Y.3    Kelliher, M.A.4    Ingalls, R.R.5
  • 23
    • 84996477451 scopus 로고    scopus 로고
    • Two lytic transglycosylases in Neisseria gonorrhoeae impart resistance to killing by lysozyme and human neutrophils
    • Ragland, S. A., Schaub, R. E., Hackett, K. T., Dillard, J. P., and Criss, A. K. (2017) Two lytic transglycosylases in Neisseria gonorrhoeae impart resistance to killing by lysozyme and human neutrophils Cell. Microbiol. 19, e12662 10.1111/cmi.12662
    • (2017) Cell. Microbiol. , vol.19 , pp. e12662
    • Ragland, S.A.1    Schaub, R.E.2    Hackett, K.T.3    Dillard, J.P.4    Criss, A.K.5
  • 24
    • 80052352663 scopus 로고    scopus 로고
    • Nod2 sensing of lysozyme-digested peptidoglycan promotes macrophage recruitment and clearance of S. pneumoniae colonization in mice
    • Davis, K. M., Nakamura, S., and Weiser, J. N. (2011) Nod2 sensing of lysozyme-digested peptidoglycan promotes macrophage recruitment and clearance of S. pneumoniae colonization in mice J. Clin. Invest. 121 (9) 3666-3676 10.1172/JCI57761
    • (2011) J. Clin. Invest. , vol.121 , Issue.9 , pp. 3666-3676
    • Davis, K.M.1    Nakamura, S.2    Weiser, J.N.3
  • 27
    • 84935837185 scopus 로고    scopus 로고
    • Peptidoglycan Modifications Tune the Stability and Function of the Innate Immune Receptor Nod2
    • Melnyk, J. E., Mohanan, V., Schaefer, A. K., Hou, C.-W., and Grimes, C. L. (2015) Peptidoglycan Modifications Tune the Stability and Function of the Innate Immune Receptor Nod2 J. Am. Chem. Soc. 137 (22) 6987-6990 10.1021/jacs.5b01607
    • (2015) J. Am. Chem. Soc. , vol.137 , Issue.22 , pp. 6987-6990
    • Melnyk, J.E.1    Mohanan, V.2    Schaefer, A.K.3    Hou, C.-W.4    Grimes, C.L.5
  • 28
    • 84938751186 scopus 로고    scopus 로고
    • Synthesis of Diverse N-Substituted Muramyl Dipeptide Derivatives and Their Use in a Study of Human NOD2 Stimulation Activity
    • Chen, K.-T., Huang, D.-Y., Chiu, C.-H., Lin, W.-W., Liang, P.-H., and Cheng, W.-C. (2015) Synthesis of Diverse N-Substituted Muramyl Dipeptide Derivatives and Their Use in a Study of Human NOD2 Stimulation Activity Chem.-Eur. J. 21 (34) 11984-11988 10.1002/chem.201501557
    • (2015) Chem. - Eur. J. , vol.21 , Issue.34 , pp. 11984-11988
    • Chen, K.-T.1    Huang, D.-Y.2    Chiu, C.-H.3    Lin, W.-W.4    Liang, P.-H.5    Cheng, W.-C.6
  • 29
    • 33746615159 scopus 로고    scopus 로고
    • The Presence of Peptidoglycan O-Acetyltransferase in Various Staphylococcal Species Correlates with Lysozyme Resistance and Pathogenicity
    • Bera, A., Biswas, R., Herbert, S., and Gotz, F. (2006) The Presence of Peptidoglycan O-Acetyltransferase in Various Staphylococcal Species Correlates with Lysozyme Resistance and Pathogenicity Infect. Immun. 74 (8) 4598-4604 10.1128/IAI.00301-06
    • (2006) Infect. Immun. , vol.74 , Issue.8 , pp. 4598-4604
    • Bera, A.1    Biswas, R.2    Herbert, S.3    Gotz, F.4
  • 30
    • 23944510740 scopus 로고    scopus 로고
    • Mutations Affecting Peptidoglycan Acetylation in Neisseria gonorrhoeae and Neisseria meningitidis
    • Dillard, J. P. and Hackett, K. T. (2005) Mutations Affecting Peptidoglycan Acetylation in Neisseria gonorrhoeae and Neisseria meningitidis Infect. Immun. 73 (9) 5697-5705 10.1128/IAI.73.9.5697-5705.2005
    • (2005) Infect. Immun. , vol.73 , Issue.9 , pp. 5697-5705
    • Dillard, J.P.1    Hackett, K.T.2
  • 31
    • 80255137078 scopus 로고    scopus 로고
    • O-Acetylated peptidoglycan: Controlling the activity of bacterial autolysins and lytic enzymes of innate immune systems
    • Moynihan, P. J. and Clarke, A. J. (2011) O-Acetylated peptidoglycan: Controlling the activity of bacterial autolysins and lytic enzymes of innate immune systems Int. J. Biochem. Cell Biol. 43 (12) 1655-1659 10.1016/j.biocel.2011.08.007
    • (2011) Int. J. Biochem. Cell Biol. , vol.43 , Issue.12 , pp. 1655-1659
    • Moynihan, P.J.1    Clarke, A.J.2
  • 32
    • 0020028114 scopus 로고
    • Strain-related differences in lysozyme sensitivity and extent of O-acetylation of gonococcal peptidoglycan
    • Rosenthal, R. S., Blundell, J. K., and Perkins, H. R. (1982) Strain-related differences in lysozyme sensitivity and extent of O-acetylation of gonococcal peptidoglycan Infect. Immun. 37 (2) 826-829
    • (1982) Infect. Immun. , vol.37 , Issue.2 , pp. 826-829
    • Rosenthal, R.S.1    Blundell, J.K.2    Perkins, H.R.3
  • 33
    • 0020632077 scopus 로고
    • Resistance of O-acetylated gonococcal peptidoglycan to human peptidoglycan-degrading enzymes
    • Rosenthal, R. S., Folkening, W. J., Miller, D. R., and Swim, S. C. (1983) Resistance of O-acetylated gonococcal peptidoglycan to human peptidoglycan-degrading enzymes Infect. Immun. 40 (3) 903-911
    • (1983) Infect. Immun. , vol.40 , Issue.3 , pp. 903-911
    • Rosenthal, R.S.1    Folkening, W.J.2    Miller, D.R.3    Swim, S.C.4
  • 34
    • 74049087445 scopus 로고    scopus 로고
    • Staphylococcus aureus Evades Lysozyme-Based Peptidoglycan Digestion that Links Phagocytosis, Inflammasome Activation, and IL-1β Secretion
    • Shimada, T., Park, B. G., Wolf, A. J., Brikos, C., Goodridge, H. S., Becker, C. A., Reyes, C. N., Miao, E. A., Aderem, A., and Götz, F. et al. 2010, Staphylococcus aureus Evades Lysozyme-Based Peptidoglycan Digestion that Links Phagocytosis, Inflammasome Activation, and IL-1β Secretion Cell Host Microbe 7 (1) 38-49 10.1016/j.chom.2009.12.008
    • (2010) Cell Host Microbe , vol.7 , Issue.1 , pp. 38-49
    • Shimada, T.1    Park, B.G.2    Wolf, A.J.3    Brikos, C.4    Goodridge, H.S.5    Becker, C.A.6    Reyes, C.N.7    Miao, E.A.8    Aderem, A.9    Götz, F.10
  • 38
    • 77950463821 scopus 로고    scopus 로고
    • The expression and function of Nod-like receptors in neutrophils
    • Ekman, A.-K. and Cardell, L. O. (2010) The expression and function of Nod-like receptors in neutrophils Immunology 130 (1) 55-63 10.1111/j.1365-2567.2009.03212.x
    • (2010) Immunology , vol.130 , Issue.1 , pp. 55-63
    • Ekman, A.-K.1    Cardell, L.O.2
  • 39
    • 33644849605 scopus 로고    scopus 로고
    • NOD2/CARD15 mediates induction of the antimicrobial peptide human beta-defensin-2
    • Voss, E., Wehkamp, J., Wehkamp, K., Stange, E. F., Schröder, J. M., and Harder, J. (2006) NOD2/CARD15 mediates induction of the antimicrobial peptide human beta-defensin-2 J. Biol. Chem. 281 (4) 2005-2011 10.1074/jbc.M511044200
    • (2006) J. Biol. Chem. , vol.281 , Issue.4 , pp. 2005-2011
    • Voss, E.1    Wehkamp, J.2    Wehkamp, K.3    Stange, E.F.4    Schröder, J.M.5    Harder, J.6
  • 40
    • 77950641148 scopus 로고    scopus 로고
    • MDP-NOD2 stimulation induces HNP-1 secretion, which contributes to NOD2 antibacterial function
    • Yamamoto-Furusho, J. K., Barnich, N., Hisamatsu, T., and Podolsky, D. K. (2010) MDP-NOD2 stimulation induces HNP-1 secretion, which contributes to NOD2 antibacterial function Inflamm. Bowel Dis. 16 (5) 736-742 10.1002/ibd.21144
    • (2010) Inflamm. Bowel Dis. , vol.16 , Issue.5 , pp. 736-742
    • Yamamoto-Furusho, J.K.1    Barnich, N.2    Hisamatsu, T.3    Podolsky, D.K.4
  • 41
    • 0032769613 scopus 로고    scopus 로고
    • Limited local and systemic antibody responses to Neisseria gonorrhoeae during uncomplicated genital infections
    • Hedges, S. R., Mayo, M. S., Mestecky, J., Hook, E. W., 3rd, and Russell, M. W. (1999) Limited local and systemic antibody responses to Neisseria gonorrhoeae during uncomplicated genital infections Infect. Immun. 67 (8) 3937-3946
    • (1999) Infect. Immun. , vol.67 , Issue.8 , pp. 3937-3946
    • Hedges, S.R.1    Mayo, M.S.2    Mestecky, J.3    Hook, E.W.4    Russell, M.W.5
  • 42
    • 0036259701 scopus 로고    scopus 로고
    • A Lytic Transglycosylase of Neisseria gonorrhoeae Is Involved in Peptidoglycan-Derived Cytotoxin Production
    • Cloud, K. A. and Dillard, J. P. (2002) A Lytic Transglycosylase of Neisseria gonorrhoeae Is Involved in Peptidoglycan-Derived Cytotoxin Production Infect. Immun. 70 (6) 2752-2757 10.1128/IAI.70.6.2752-2757.2002
    • (2002) Infect. Immun. , vol.70 , Issue.6 , pp. 2752-2757
    • Cloud, K.A.1    Dillard, J.P.2
  • 43
    • 34347404096 scopus 로고    scopus 로고
    • A fully defined, clear and protein-free liquid medium permitting dense growth of Neisseria gonorrhoeae from very low inocula
    • Wade, J. J. and Graver, M. A. (2007) A fully defined, clear and protein-free liquid medium permitting dense growth of Neisseria gonorrhoeae from very low inocula FEMS Microbiol. Lett. 273 (1) 35-37 10.1111/j.1574-6968.2007.00776.x
    • (2007) FEMS Microbiol. Lett. , vol.273 , Issue.1 , pp. 35-37
    • Wade, J.J.1    Graver, M.A.2
  • 44
    • 0028287439 scopus 로고
    • Isolation of peptidoglycan and soluble peptidoglycan fragments
    • Rosenthal, R. S. and Dziarski, R. (1994) Isolation of peptidoglycan and soluble peptidoglycan fragments Methods Enzymol. 235, 253-285 10.1016/0076-6879(94)35146-5
    • (1994) Methods Enzymol. , vol.235 , pp. 253-285
    • Rosenthal, R.S.1    Dziarski, R.2
  • 45
    • 44349179845 scopus 로고    scopus 로고
    • Mutations in ampG or ampD Affect Peptidoglycan Fragment Release from Neisseria gonorrhoeae
    • Garcia, D. L. and Dillard, J. P. (2008) Mutations in ampG or ampD Affect Peptidoglycan Fragment Release from Neisseria gonorrhoeae J. Bacteriol. 190 (11) 3799-3807 10.1128/JB.01194-07
    • (2008) J. Bacteriol. , vol.190 , Issue.11 , pp. 3799-3807
    • Garcia, D.L.1    Dillard, J.P.2
  • 46
    • 84988822553 scopus 로고    scopus 로고
    • Lytic transglycosylases LtgA and LtgD perform distinct roles in remodeling, recycling and releasing peptidoglycan in Neisseria gonorrhoeae
    • Schaub, R. E., Chan, Y. A., Lee, M., Hesek, D., Mobashery, S., and Dillard, J. P. (2016) Lytic transglycosylases LtgA and LtgD perform distinct roles in remodeling, recycling and releasing peptidoglycan in Neisseria gonorrhoeae Mol. Microbiol. 102, 865 10.1111/mmi.13496
    • (2016) Mol. Microbiol. , vol.102 , pp. 865
    • Schaub, R.E.1    Chan, Y.A.2    Lee, M.3    Hesek, D.4    Mobashery, S.5    Dillard, J.P.6
  • 47
    • 84979979880 scopus 로고    scopus 로고
    • Analysis of Peptidoglycan Fragment Release
    • Schaub, R. E., Lenz, J. D., and Dillard, J. P. (2016) Analysis of Peptidoglycan Fragment Release Methods Mol. Biol. 1440, 185-200 10.1007/978-1-4939-3676-2-14
    • (2016) Methods Mol. Biol. , vol.1440 , pp. 185-200
    • Schaub, R.E.1    Lenz, J.D.2    Dillard, J.P.3
  • 48
    • 84969194621 scopus 로고    scopus 로고
    • Amidase Activity of AmiC Controls Cell Separation and Stem Peptide Release and Is Enhanced by NlpD in Neisseria gonorrhoeae
    • Lenz, J. D., Stohl, E. A., Robertson, R. M., Hackett, K. T., Fisher, K., Xiong, K., Lee, M., Hesek, D., Mobashery, S., and Seifert, H. S. et al. 2016, Amidase Activity of AmiC Controls Cell Separation and Stem Peptide Release and Is Enhanced by NlpD in Neisseria gonorrhoeae J. Biol. Chem. 291 (20) 10916-10933 10.1074/jbc.M116.715573
    • (2016) J. Biol. Chem. , vol.291 , Issue.20 , pp. 10916-10933
    • Lenz, J.D.1    Stohl, E.A.2    Robertson, R.M.3    Hackett, K.T.4    Fisher, K.5    Xiong, K.6    Lee, M.7    Hesek, D.8    Mobashery, S.9    Seifert, H.S.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.