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Volumn 31, Issue 4, 2013, Pages 258-267

Exterior design: Strategies for redecorating the bacterial surface with small molecules

Author keywords

Bacterial envelope; Bioorthogonal chemistry; Metabolic labeling; Small molecule; Surface display; Surface engineering

Indexed keywords

BACTERIAL ENVELOPES; BIOORTHOGONAL CHEMISTRIES; METABOLIC LABELING; SMALL MOLECULES; SURFACE DISPLAYS; SURFACE ENGINEERING;

EID: 84875486336     PISSN: 01677799     EISSN: 18793096     Source Type: Journal    
DOI: 10.1016/j.tibtech.2013.01.012     Document Type: Review
Times cited : (36)

References (91)
  • 2
    • 69949158186 scopus 로고    scopus 로고
    • Sculpting the bacterial cell
    • Margolin W. Sculpting the bacterial cell. Curr. Biol. 2009, 19:R812-R822.
    • (2009) Curr. Biol. , vol.19
    • Margolin, W.1
  • 3
    • 84855889658 scopus 로고    scopus 로고
    • From the regulation of peptidoglycan synthesis to bacterial growth and morphology
    • Typas A., et al. From the regulation of peptidoglycan synthesis to bacterial growth and morphology. Nat. Rev. Microbiol. 2012, 10:123-136.
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 123-136
    • Typas, A.1
  • 4
    • 0023042026 scopus 로고
    • Cell surface exposure of the outer membrane protein OmpA of Escherichia coli K-12
    • Freudl R., et al. Cell surface exposure of the outer membrane protein OmpA of Escherichia coli K-12. J. Mol. Biol. 1986, 188:491-494.
    • (1986) J. Mol. Biol. , vol.188 , pp. 491-494
    • Freudl, R.1
  • 5
    • 0022814620 scopus 로고
    • Probing the topology of a bacterial membrane protein by genetic insertion of a foreign epitope; expression at the cell surface
    • Charbit A., et al. Probing the topology of a bacterial membrane protein by genetic insertion of a foreign epitope; expression at the cell surface. EMBO J. 1986, 5:3029-3037.
    • (1986) EMBO J. , vol.5 , pp. 3029-3037
    • Charbit, A.1
  • 6
    • 79957984059 scopus 로고    scopus 로고
    • Molecular design of the microbial cell surface toward the recovery of metal ions
    • Kuroda K., Ueda M. Molecular design of the microbial cell surface toward the recovery of metal ions. Curr. Opin. Biotechnol. 2011, 22:427-433.
    • (2011) Curr. Opin. Biotechnol. , vol.22 , pp. 427-433
    • Kuroda, K.1    Ueda, M.2
  • 7
    • 41549136380 scopus 로고    scopus 로고
    • Versatile microbial surface-display for environmental remediation and biofuels production
    • Wu C.H., et al. Versatile microbial surface-display for environmental remediation and biofuels production. Trends Microbiol. 2008, 16:181-188.
    • (2008) Trends Microbiol. , vol.16 , pp. 181-188
    • Wu, C.H.1
  • 8
    • 77955568982 scopus 로고    scopus 로고
    • Fluorescent and bioluminescent cell-based sensors: strategies for their preservation
    • Date A., et al. Fluorescent and bioluminescent cell-based sensors: strategies for their preservation. Adv. Biochem. Eng. Biotechnol. 2010, 117:57-75.
    • (2010) Adv. Biochem. Eng. Biotechnol. , vol.117 , pp. 57-75
    • Date, A.1
  • 9
    • 34548814155 scopus 로고    scopus 로고
    • Protein engineering with bacterial display
    • Daugherty P.S. Protein engineering with bacterial display. Curr. Opin. Struct. Biol. 2007, 17:474-480.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 474-480
    • Daugherty, P.S.1
  • 10
    • 77958488277 scopus 로고    scopus 로고
    • Engineering the perfect (bacterial) cancer therapy
    • Forbes N.S. Engineering the perfect (bacterial) cancer therapy. Nat. Rev. Cancer 2010, 10:785-794.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 785-794
    • Forbes, N.S.1
  • 11
    • 79955557064 scopus 로고    scopus 로고
    • Bacterial spores as platforms for bioanalytical and biomedical applications
    • Knecht L.D., et al. Bacterial spores as platforms for bioanalytical and biomedical applications. Anal. Bioanal. Chem. 2011, 400:977-989.
    • (2011) Anal. Bioanal. Chem. , vol.400 , pp. 977-989
    • Knecht, L.D.1
  • 12
    • 78751624924 scopus 로고    scopus 로고
    • Decorating microbes: surface display of proteins on Escherichia coli
    • van Bloois E., et al. Decorating microbes: surface display of proteins on Escherichia coli. Trends Biotechnol. 2011, 29:79-86.
    • (2011) Trends Biotechnol. , vol.29 , pp. 79-86
    • van Bloois, E.1
  • 13
    • 79960016255 scopus 로고    scopus 로고
    • Mucosal vaccination and therapy with genetically modified lactic acid bacteria
    • Wells J. Mucosal vaccination and therapy with genetically modified lactic acid bacteria. Annu. Rev. Food Sci. Technol. 2011, 2:423-445.
    • (2011) Annu. Rev. Food Sci. Technol. , vol.2 , pp. 423-445
    • Wells, J.1
  • 14
    • 84863100717 scopus 로고    scopus 로고
    • Bioengineered microbes in disease therapy
    • Paton A.W., et al. Bioengineered microbes in disease therapy. Trends Mol. Med. 2012, 18:417-425.
    • (2012) Trends Mol. Med. , vol.18 , pp. 417-425
    • Paton, A.W.1
  • 15
    • 67650474557 scopus 로고    scopus 로고
    • Click chemistry and bioorthogonal reactions: unprecedented selectivity in the labeling of biological molecules
    • Best M.D. Click chemistry and bioorthogonal reactions: unprecedented selectivity in the labeling of biological molecules. Biochemistry 2009, 48:6571-6584.
    • (2009) Biochemistry , vol.48 , pp. 6571-6584
    • Best, M.D.1
  • 16
    • 72449163625 scopus 로고    scopus 로고
    • Expanding the chemical biologist's tool kit: chemical labelling strategies and its applications
    • Chattopadhaya S., et al. Expanding the chemical biologist's tool kit: chemical labelling strategies and its applications. Curr. Med. Chem. 2009, 16:4527-4543.
    • (2009) Curr. Med. Chem. , vol.16 , pp. 4527-4543
    • Chattopadhaya, S.1
  • 17
    • 40949126564 scopus 로고    scopus 로고
    • Surface modification of tobacco mosaic virus with " click" chemistry
    • Bruckman M.A., et al. Surface modification of tobacco mosaic virus with " click" chemistry. Chembiochem 2008, 9:519-523.
    • (2008) Chembiochem , vol.9 , pp. 519-523
    • Bruckman, M.A.1
  • 18
    • 84868293654 scopus 로고    scopus 로고
    • Chemoselective modification of viral surfaces via bioorthogonal click chemistry
    • Rubino F.A., et al. Chemoselective modification of viral surfaces via bioorthogonal click chemistry. J. Vis. Exp. 2012, 66:e4246.
    • (2012) J. Vis. Exp. , vol.66
    • Rubino, F.A.1
  • 19
    • 43249099890 scopus 로고    scopus 로고
    • In vivo imaging of membrane-associated glycans in developing zebrafish
    • Laughlin S.T., et al. In vivo imaging of membrane-associated glycans in developing zebrafish. Science 2008, 320:664-667.
    • (2008) Science , vol.320 , pp. 664-667
    • Laughlin, S.T.1
  • 20
    • 4344704630 scopus 로고    scopus 로고
    • Chemical remodelling of cell surfaces in living animals
    • Prescher J.A., et al. Chemical remodelling of cell surfaces in living animals. Nature 2004, 430:873-877.
    • (2004) Nature , vol.430 , pp. 873-877
    • Prescher, J.A.1
  • 21
    • 70349320611 scopus 로고    scopus 로고
    • Discovery of Escherichia coli methionyl-tRNA synthetase mutants for efficient labeling of proteins with azidonorleucine in vivo
    • Tanrikulu I.C., et al. Discovery of Escherichia coli methionyl-tRNA synthetase mutants for efficient labeling of proteins with azidonorleucine in vivo. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:15285-15290.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 15285-15290
    • Tanrikulu, I.C.1
  • 22
    • 77953754676 scopus 로고    scopus 로고
    • Rapid visualization and large-scale profiling of bacterial lipoproteins with chemical reporters
    • Rangan K.J., et al. Rapid visualization and large-scale profiling of bacterial lipoproteins with chemical reporters. J. Am. Chem. Soc. 2010, 132:10628-10629.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 10628-10629
    • Rangan, K.J.1
  • 23
    • 33645859599 scopus 로고    scopus 로고
    • Promotion of opsonization by antibodies and phagocytosis of Gram-positive bacteria by a bifunctional polyacrylamide
    • Krishnamurthy V.M., et al. Promotion of opsonization by antibodies and phagocytosis of Gram-positive bacteria by a bifunctional polyacrylamide. Biomaterials 2006, 27:3663-3674.
    • (2006) Biomaterials , vol.27 , pp. 3663-3674
    • Krishnamurthy, V.M.1
  • 24
    • 79953029878 scopus 로고    scopus 로고
    • Multivalent artificial opsonin for the recognition and phagocytosis of Gram-positive bacteria by human phagocytes
    • Katzenmeyer K.N., Bryers J.D. Multivalent artificial opsonin for the recognition and phagocytosis of Gram-positive bacteria by human phagocytes. Biomaterials 2011, 32:4042-4051.
    • (2011) Biomaterials , vol.32 , pp. 4042-4051
    • Katzenmeyer, K.N.1    Bryers, J.D.2
  • 25
    • 80052486494 scopus 로고    scopus 로고
    • Chemical-biological studies of subcellular organization in bacteria
    • Foss M.H., et al. Chemical-biological studies of subcellular organization in bacteria. Biochemistry 2011, 50:7719-7734.
    • (2011) Biochemistry , vol.50 , pp. 7719-7734
    • Foss, M.H.1
  • 26
    • 79952952479 scopus 로고    scopus 로고
    • Uptake of unnatural trehalose analogs as a reporter for Mycobacterium tuberculosis
    • Backus K.M., et al. Uptake of unnatural trehalose analogs as a reporter for Mycobacterium tuberculosis. Nat. Chem. Biol. 2011, 7:228-235.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 228-235
    • Backus, K.M.1
  • 27
    • 0034581375 scopus 로고    scopus 로고
    • Metabolic labeling of glycoproteins with chemical tags through unnatural sialic acid biosynthesis
    • Jacobs C.L., et al. Metabolic labeling of glycoproteins with chemical tags through unnatural sialic acid biosynthesis. Methods Enzymol. 2000, 327:260-275.
    • (2000) Methods Enzymol. , vol.327 , pp. 260-275
    • Jacobs, C.L.1
  • 28
    • 84858785499 scopus 로고    scopus 로고
    • Click-mediated labeling of bacterial membranes through metabolic modification of the lipopolysaccharide inner core
    • Dumont A., et al. Click-mediated labeling of bacterial membranes through metabolic modification of the lipopolysaccharide inner core. Angew. Chem. Int. Ed. Engl. 2012, 51:3143-3146.
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 3143-3146
    • Dumont, A.1
  • 30
    • 0000096835 scopus 로고    scopus 로고
    • Click chemistry: diverse chemical function from a few good reactions
    • Kolb H.C., et al. Click chemistry: diverse chemical function from a few good reactions. Angew. Chem. Int. Ed. Engl. 2001, 40:2004-2021.
    • (2001) Angew. Chem. Int. Ed. Engl. , vol.40 , pp. 2004-2021
    • Kolb, H.C.1
  • 31
    • 80053013322 scopus 로고    scopus 로고
    • Noncanonical amino acids in the interrogation of cellular protein synthesis
    • Ngo J.T., Tirrell D.A. Noncanonical amino acids in the interrogation of cellular protein synthesis. Acc. Chem. Res. 2011, 44:677-685.
    • (2011) Acc. Chem. Res. , vol.44 , pp. 677-685
    • Ngo, J.T.1    Tirrell, D.A.2
  • 32
    • 77955575354 scopus 로고    scopus 로고
    • Orthogonal alkynyl amino acid reporter for selective labeling of bacterial proteomes during infection
    • Grammel M., et al. Orthogonal alkynyl amino acid reporter for selective labeling of bacterial proteomes during infection. Angew. Chem. Int. Ed. Engl. 2010, 49:5970-5974.
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 5970-5974
    • Grammel, M.1
  • 33
    • 84855643309 scopus 로고    scopus 로고
    • Cell-selective labeling of bacterial proteomes with an orthogonal phenylalanine amino acid reporter
    • Grammel M., et al. Cell-selective labeling of bacterial proteomes with an orthogonal phenylalanine amino acid reporter. Chem. Commun. 2012, 48:1473-1474.
    • (2012) Chem. Commun. , vol.48 , pp. 1473-1474
    • Grammel, M.1
  • 34
    • 80052967509 scopus 로고    scopus 로고
    • A genetically incorporated crosslinker reveals chaperone cooperation in acid resistance
    • Zhang M., et al. A genetically incorporated crosslinker reveals chaperone cooperation in acid resistance. Nat. Chem. Biol. 2011, 7:671-677.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 671-677
    • Zhang, M.1
  • 35
    • 83755170862 scopus 로고    scopus 로고
    • Site-specific incorporation of photo-cross-linker and bioorthogonal amino acids into enteric bacterial pathogens
    • Lin S., et al. Site-specific incorporation of photo-cross-linker and bioorthogonal amino acids into enteric bacterial pathogens. J. Am. Chem. Soc. 2011, 133:20581-20587.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 20581-20587
    • Lin, S.1
  • 36
    • 84855880056 scopus 로고    scopus 로고
    • Multifunctional protein labeling via enzymatic N-terminal tagging and elaboration by click chemistry
    • Heal W.P., et al. Multifunctional protein labeling via enzymatic N-terminal tagging and elaboration by click chemistry. Nat. Protoc. 2012, 7:105-117.
    • (2012) Nat. Protoc. , vol.7 , pp. 105-117
    • Heal, W.P.1
  • 37
    • 77953643054 scopus 로고    scopus 로고
    • Adding new chemistries to the genetic code
    • Liu C.C., Schultz P.G. Adding new chemistries to the genetic code. Annu. Rev. Biochem. 2010, 79:413-444.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 413-444
    • Liu, C.C.1    Schultz, P.G.2
  • 38
    • 0030929377 scopus 로고    scopus 로고
    • Engineering chemical reactivity on cell surfaces through oligosaccharide biosynthesis
    • Mahal L.K., et al. Engineering chemical reactivity on cell surfaces through oligosaccharide biosynthesis. Science 1997, 276:1125-1128.
    • (1997) Science , vol.276 , pp. 1125-1128
    • Mahal, L.K.1
  • 39
    • 76549128410 scopus 로고    scopus 로고
    • Lipopolysaccharide: biosynthetic pathway and structure modification
    • Wang X., Quinn P.J. Lipopolysaccharide: biosynthetic pathway and structure modification. Prog. Lipid Res. 2010, 49:97-107.
    • (2010) Prog. Lipid Res. , vol.49 , pp. 97-107
    • Wang, X.1    Quinn, P.J.2
  • 40
    • 63149099211 scopus 로고    scopus 로고
    • Remodeling bacterial polysaccharides by metabolic pathway engineering
    • Yi W., et al. Remodeling bacterial polysaccharides by metabolic pathway engineering. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:4207-4212.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 4207-4212
    • Yi, W.1
  • 41
    • 0037453019 scopus 로고    scopus 로고
    • Metabolic incorporation of unnatural sialic acids into Haemophilus ducreyi lipooligosaccharides
    • Goon S., et al. Metabolic incorporation of unnatural sialic acids into Haemophilus ducreyi lipooligosaccharides. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:3089-3094.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3089-3094
    • Goon, S.1
  • 42
    • 80051789506 scopus 로고    scopus 로고
    • Metabolic labeling of fucosylated glycoproteins in Bacteroidales species
    • Besanceney-Webler C., et al. Metabolic labeling of fucosylated glycoproteins in Bacteroidales species. Bioorg. Med. Chem. Lett. 2011, 21:4989-4992.
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 4989-4992
    • Besanceney-Webler, C.1
  • 43
    • 68949136748 scopus 로고    scopus 로고
    • Metabolic profiling of Helicobacter pylori glycosylation
    • Koenigs M.B., et al. Metabolic profiling of Helicobacter pylori glycosylation. Mol. Biosyst. 2009, 5:909-912.
    • (2009) Mol. Biosyst. , vol.5 , pp. 909-912
    • Koenigs, M.B.1
  • 44
    • 67651173016 scopus 로고    scopus 로고
    • The engineering of bacteria bearing azido-pseudaminic acid-modified flagella
    • Liu F., et al. The engineering of bacteria bearing azido-pseudaminic acid-modified flagella. Chembiochem 2009, 10:1317-1320.
    • (2009) Chembiochem , vol.10 , pp. 1317-1320
    • Liu, F.1
  • 45
    • 0041692305 scopus 로고    scopus 로고
    • Cell surface labeling of Escherichia coli via copper(I)-catalyzed [3+2] cycloaddition
    • Link A.J., Tirrell D.A. Cell surface labeling of Escherichia coli via copper(I)-catalyzed [3+2] cycloaddition. J. Am. Chem. Soc. 2003, 125:11164-11165.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11164-11165
    • Link, A.J.1    Tirrell, D.A.2
  • 46
    • 4344561883 scopus 로고    scopus 로고
    • Presentation and detection of azide functionality in bacterial cell surface proteins
    • Link A.J., et al. Presentation and detection of azide functionality in bacterial cell surface proteins. J. Am. Chem. Soc. 2004, 126:10598-10602.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 10598-10602
    • Link, A.J.1
  • 47
    • 33745892390 scopus 로고    scopus 로고
    • Discovery of aminoacyl-tRNA synthetase activity through cell-surface display of noncanonical amino acids
    • Link A.J., et al. Discovery of aminoacyl-tRNA synthetase activity through cell-surface display of noncanonical amino acids. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:10180-10185.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 10180-10185
    • Link, A.J.1
  • 48
    • 0038661197 scopus 로고    scopus 로고
    • A new strategy for the site-specific modification of proteins in vivo
    • Zhang Z., et al. A new strategy for the site-specific modification of proteins in vivo. Biochemistry 2003, 42:6735-6746.
    • (2003) Biochemistry , vol.42 , pp. 6735-6746
    • Zhang, Z.1
  • 49
    • 40849118255 scopus 로고    scopus 로고
    • Bacterial growth and cell division: a mycobacterial perspective
    • Hett E.C., Rubin E.J. Bacterial growth and cell division: a mycobacterial perspective. Microbiol. Mol. Biol. Rev. 2008, 72:126-156.
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 126-156
    • Hett, E.C.1    Rubin, E.J.2
  • 50
    • 84867050665 scopus 로고    scopus 로고
    • Probing the mycobacterial trehalome with bioorthogonal chemistry
    • Swarts B.M., et al. Probing the mycobacterial trehalome with bioorthogonal chemistry. J. Am. Chem. Soc. 2012, 134:16123-16126.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 16123-16126
    • Swarts, B.M.1
  • 51
    • 0043029569 scopus 로고    scopus 로고
    • Cell wall engineering of living bacteria through biosynthesis
    • Sadamoto R., et al. Cell wall engineering of living bacteria through biosynthesis. Methods Enzymol. 2003, 362:273-286.
    • (2003) Methods Enzymol. , vol.362 , pp. 273-286
    • Sadamoto, R.1
  • 52
    • 0037036755 scopus 로고    scopus 로고
    • Cell-wall engineering of living bacteria
    • Sadamoto R., et al. Cell-wall engineering of living bacteria. J. Am. Chem. Soc. 2002, 124:9018-9019.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9018-9019
    • Sadamoto, R.1
  • 53
    • 1642322370 scopus 로고    scopus 로고
    • Control of bacteria adhesion by cell-wall engineering
    • Sadamoto R., et al. Control of bacteria adhesion by cell-wall engineering. J. Am. Chem. Soc. 2004, 126:3755-3761.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3755-3761
    • Sadamoto, R.1
  • 54
    • 56349126879 scopus 로고    scopus 로고
    • Bacterial surface engineering utilizing glucosamine phosphate derivatives as cell wall precursor surrogates
    • Sadamoto R., et al. Bacterial surface engineering utilizing glucosamine phosphate derivatives as cell wall precursor surrogates. Chemistry 2008, 14:10192-10195.
    • (2008) Chemistry , vol.14 , pp. 10192-10195
    • Sadamoto, R.1
  • 55
    • 79955031537 scopus 로고    scopus 로고
    • A novel in vivo cell-wall labeling approach sheds new light on peptidoglycan synthesis in Escherichia coli
    • Olrichs N.K., et al. A novel in vivo cell-wall labeling approach sheds new light on peptidoglycan synthesis in Escherichia coli. Chembiochem 2011, 12:1124-1133.
    • (2011) Chembiochem , vol.12 , pp. 1124-1133
    • Olrichs, N.K.1
  • 56
    • 79951581502 scopus 로고    scopus 로고
    • Emerging knowledge of regulatory roles of D-amino acids in bacteria
    • Cava F., et al. Emerging knowledge of regulatory roles of D-amino acids in bacteria. Cell. Mol. Life Sci. 2011, 68:817-831.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 817-831
    • Cava, F.1
  • 57
    • 84870593406 scopus 로고    scopus 로고
    • In situ probing of newly synthesized peptidoglycan in live bacteria with fluorescent D-amino acids
    • Kuru E., et al. In situ probing of newly synthesized peptidoglycan in live bacteria with fluorescent D-amino acids. Angew. Chem. Int. Ed. Engl. 2012, 51:12519-12523.
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 12519-12523
    • Kuru, E.1
  • 58
    • 33645137247 scopus 로고    scopus 로고
    • Sortases and the art of anchoring proteins to the envelopes of Gram-positive bacteria
    • Marraffini L.A., et al. Sortases and the art of anchoring proteins to the envelopes of Gram-positive bacteria. Microbiol. Mol. Biol. Rev. 2006, 70:192-221.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 192-221
    • Marraffini, L.A.1
  • 59
    • 78650551407 scopus 로고    scopus 로고
    • A biosynthetic strategy for re-engineering the Staphylococcus aureus cell wall with non-native small molecules
    • Nelson J.W., et al. A biosynthetic strategy for re-engineering the Staphylococcus aureus cell wall with non-native small molecules. ACS Chem. Biol. 2010, 5:1147-1155.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 1147-1155
    • Nelson, J.W.1
  • 60
    • 3042824772 scopus 로고    scopus 로고
    • Spontaneous integration of transmembrane peptides into a bacterial magnetic particle membrane and its application to display of useful proteins
    • Tanaka T., et al. Spontaneous integration of transmembrane peptides into a bacterial magnetic particle membrane and its application to display of useful proteins. Anal. Chem. 2004, 76:3764-3769.
    • (2004) Anal. Chem. , vol.76 , pp. 3764-3769
    • Tanaka, T.1
  • 61
    • 81855183349 scopus 로고    scopus 로고
    • Ubiquitous detection of Gram-positive bacteria with bioorthogonal magnetofluorescent nanoparticles
    • Chung H.J., et al. Ubiquitous detection of Gram-positive bacteria with bioorthogonal magnetofluorescent nanoparticles. ACS Nano 2011, 5:8834-8841.
    • (2011) ACS Nano , vol.5 , pp. 8834-8841
    • Chung, H.J.1
  • 62
    • 33746639594 scopus 로고    scopus 로고
    • Imaging peptidoglycan biosynthesis in Bacillus subtilis with fluorescent antibiotics
    • Tiyanont K., et al. Imaging peptidoglycan biosynthesis in Bacillus subtilis with fluorescent antibiotics. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:11033-11038.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 11033-11038
    • Tiyanont, K.1
  • 63
    • 0032908481 scopus 로고    scopus 로고
    • BOCILLIN FL, a sensitive and commercially available reagent for detection of penicillin-binding proteins
    • Zhao G., et al. BOCILLIN FL, a sensitive and commercially available reagent for detection of penicillin-binding proteins. Antimicrob. Agents Chemother. 1999, 43:1124-1128.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1124-1128
    • Zhao, G.1
  • 64
    • 34447102458 scopus 로고    scopus 로고
    • Biological safety concepts of genetically modified live bacterial vaccines
    • Frey J. Biological safety concepts of genetically modified live bacterial vaccines. Vaccine 2007, 25:5598-5605.
    • (2007) Vaccine , vol.25 , pp. 5598-5605
    • Frey, J.1
  • 65
    • 80053013758 scopus 로고    scopus 로고
    • Chemical tags for labeling proteins inside living cells
    • Jing C., Cornish V.W. Chemical tags for labeling proteins inside living cells. Acc. Chem. Res. 2011, 44:784-792.
    • (2011) Acc. Chem. Res. , vol.44 , pp. 784-792
    • Jing, C.1    Cornish, V.W.2
  • 66
    • 84865035333 scopus 로고    scopus 로고
    • Imaging beyond the proteome
    • Chang P.V., Bertozzi C.R. Imaging beyond the proteome. Chem. Commun. 2012, 48:8864-8879.
    • (2012) Chem. Commun. , vol.48 , pp. 8864-8879
    • Chang, P.V.1    Bertozzi, C.R.2
  • 67
    • 36749016781 scopus 로고    scopus 로고
    • Duplication and segregation of the actin (MreB) cytoskeleton during the prokaryotic cell cycle
    • Vats P., Rothfield L. Duplication and segregation of the actin (MreB) cytoskeleton during the prokaryotic cell cycle. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:17795-17800.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 17795-17800
    • Vats, P.1    Rothfield, L.2
  • 68
    • 84863229704 scopus 로고    scopus 로고
    • Helical insertion of peptidoglycan produces chiral ordering of the bacterial cell wall
    • Wang S., et al. Helical insertion of peptidoglycan produces chiral ordering of the bacterial cell wall. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:E595-E604.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109
    • Wang, S.1
  • 69
    • 84871055385 scopus 로고    scopus 로고
    • The helical MreB cytoskeleton in E. coli MC1000/pLE7 is an artifact of the N-terminal YFP tag
    • Swulius M.T., Jensen G.J. The helical MreB cytoskeleton in E. coli MC1000/pLE7 is an artifact of the N-terminal YFP tag. J. Bacteriol. 2012, 194:6382-6386.
    • (2012) J. Bacteriol. , vol.194 , pp. 6382-6386
    • Swulius, M.T.1    Jensen, G.J.2
  • 71
    • 84863574162 scopus 로고    scopus 로고
    • Small molecule perimeter defense in entomopathogenic bacteria
    • Crawford J.M., et al. Small molecule perimeter defense in entomopathogenic bacteria. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:10821-10826.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 10821-10826
    • Crawford, J.M.1
  • 72
    • 80053982187 scopus 로고    scopus 로고
    • Exploring isonitrile-based click chemistry for ligation with biomolecules
    • Stockmann H., et al. Exploring isonitrile-based click chemistry for ligation with biomolecules. Org. Biomol. Chem. 2011, 9:7303-7305.
    • (2011) Org. Biomol. Chem. , vol.9 , pp. 7303-7305
    • Stockmann, H.1
  • 73
    • 84856443106 scopus 로고    scopus 로고
    • Single cell Raman spectroscopy for cell sorting and imaging
    • Li M., et al. Single cell Raman spectroscopy for cell sorting and imaging. Curr. Opin. Biotechnol. 2012, 23:56-63.
    • (2012) Curr. Opin. Biotechnol. , vol.23 , pp. 56-63
    • Li, M.1
  • 74
    • 79955047997 scopus 로고    scopus 로고
    • Imaging of EdU, an alkyne-tagged cell proliferation probe, by Raman microscopy
    • Yamakoshi H., et al. Imaging of EdU, an alkyne-tagged cell proliferation probe, by Raman microscopy. J. Am. Chem. Soc. 2011, 133:6102-6105.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 6102-6105
    • Yamakoshi, H.1
  • 75
    • 34250815216 scopus 로고    scopus 로고
    • Tailored glycoproteomics and glycan site mapping using saccharide-selective bioorthogonal probes
    • Hanson S.R., et al. Tailored glycoproteomics and glycan site mapping using saccharide-selective bioorthogonal probes. J. Am. Chem. Soc. 2007, 129:7266-7267.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 7266-7267
    • Hanson, S.R.1
  • 76
    • 23344432754 scopus 로고    scopus 로고
    • Surfaceome of Leptospira spp
    • Cullen P.A., et al. Surfaceome of Leptospira spp. Infect. Immun. 2005, 73:4853-4863.
    • (2005) Infect. Immun. , vol.73 , pp. 4853-4863
    • Cullen, P.A.1
  • 77
    • 79960417505 scopus 로고    scopus 로고
    • Current methodologies for proteomics of bacterial surface-exposed and cell envelope proteins
    • Solis N., Cordwell S.J. Current methodologies for proteomics of bacterial surface-exposed and cell envelope proteins. Proteomics 2011, 11:3169-3189.
    • (2011) Proteomics , vol.11 , pp. 3169-3189
    • Solis, N.1    Cordwell, S.J.2
  • 78
    • 77958454595 scopus 로고    scopus 로고
    • Reverse vaccinology: developing vaccines in the era of genomics
    • Sette A., Rappuoli R. Reverse vaccinology: developing vaccines in the era of genomics. Immunity 2010, 33:530-541.
    • (2010) Immunity , vol.33 , pp. 530-541
    • Sette, A.1    Rappuoli, R.2
  • 79
    • 84861034877 scopus 로고    scopus 로고
    • Site-specific chemical protein conjugation using genetically encoded aldehyde tags
    • Rabuka D., et al. Site-specific chemical protein conjugation using genetically encoded aldehyde tags. Nat. Protoc. 2012, 7:1052-1067.
    • (2012) Nat. Protoc. , vol.7 , pp. 1052-1067
    • Rabuka, D.1
  • 80
    • 36849084059 scopus 로고    scopus 로고
    • Redirecting lipoic acid ligase for cell surface protein labeling with small-molecule probes
    • Fernandez-Suarez M., et al. Redirecting lipoic acid ligase for cell surface protein labeling with small-molecule probes. Nat. Biotechnol. 2007, 25:1483-1487.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 1483-1487
    • Fernandez-Suarez, M.1
  • 81
    • 18744401100 scopus 로고    scopus 로고
    • Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase
    • Chen I., et al. Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase. Nat. Methods 2005, 2:99-104.
    • (2005) Nat. Methods , vol.2 , pp. 99-104
    • Chen, I.1
  • 82
    • 0037225952 scopus 로고    scopus 로고
    • A general method for the covalent labeling of fusion proteins with small molecules in vivo
    • Keppler A., et al. A general method for the covalent labeling of fusion proteins with small molecules in vivo. Nat. Biotechnol. 2003, 21:86-89.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 86-89
    • Keppler, A.1
  • 83
    • 18744406025 scopus 로고    scopus 로고
    • In vivo protein labeling with trimethoprim conjugates: a flexible chemical tag
    • Miller L.W., et al. In vivo protein labeling with trimethoprim conjugates: a flexible chemical tag. Nat. Methods 2005, 2:255-257.
    • (2005) Nat. Methods , vol.2 , pp. 255-257
    • Miller, L.W.1
  • 84
    • 57449114045 scopus 로고    scopus 로고
    • Sortase A localizes to distinct foci on the Streptococcus pyogenes membrane
    • Raz A., Fischetti V.A. Sortase A localizes to distinct foci on the Streptococcus pyogenes membrane. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:18549-18554.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 18549-18554
    • Raz, A.1    Fischetti, V.A.2
  • 85
    • 84864397080 scopus 로고    scopus 로고
    • A magnetic Gram stain for bacterial detection
    • Budin G., et al. A magnetic Gram stain for bacterial detection. Angew. Chem. Int. Ed. Engl. 2012, 51:7752-7755.
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 7752-7755
    • Budin, G.1
  • 86
    • 79953785400 scopus 로고    scopus 로고
    • Multiplex PCR and emerging technologies for the detection of respiratory pathogens
    • Caliendo A.M. Multiplex PCR and emerging technologies for the detection of respiratory pathogens. Clin. Infect. Dis. 2011, 52(Suppl. 4):S326-S330.
    • (2011) Clin. Infect. Dis. , vol.52 , Issue.SUPPL. 4
    • Caliendo, A.M.1
  • 87
    • 84865331355 scopus 로고    scopus 로고
    • Cell-surface sensors: lighting the cellular environment
    • Ali M.M., et al. Cell-surface sensors: lighting the cellular environment. Wiley Interdiscip. Rev. Nanomed. Nanobiotechnol. 2012, 4:547-561.
    • (2012) Wiley Interdiscip. Rev. Nanomed. Nanobiotechnol. , vol.4 , pp. 547-561
    • Ali, M.M.1
  • 88
    • 63849275691 scopus 로고    scopus 로고
    • Programmed assembly of 3-dimensional microtissues with defined cellular connectivity
    • Gartner Z.J., Bertozzi C.R. Programmed assembly of 3-dimensional microtissues with defined cellular connectivity. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:4606-4610.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 4606-4610
    • Gartner, Z.J.1    Bertozzi, C.R.2
  • 89
    • 83655181083 scopus 로고    scopus 로고
    • Sociomicrobiology in engineered landscapes
    • Connell J.L., et al. Sociomicrobiology in engineered landscapes. Nat. Chem. Biol. 2012, 8:10-13.
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 10-13
    • Connell, J.L.1
  • 90
    • 66849142315 scopus 로고    scopus 로고
    • Evolving concepts in biofilm infections
    • Hall-Stoodley L., Stoodley P. Evolving concepts in biofilm infections. Cell. Microbiol. 2009, 11:1034-1043.
    • (2009) Cell. Microbiol. , vol.11 , pp. 1034-1043
    • Hall-Stoodley, L.1    Stoodley, P.2
  • 91
    • 77950438894 scopus 로고    scopus 로고
    • Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane
    • Chng S.S., et al. Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:5363-5368.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 5363-5368
    • Chng, S.S.1


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