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Volumn 61, Issue PART7, 2012, Pages 919-926

Recent developments in bacterial protein glycan coupling technology and glycoconjugate vaccine design

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; GLYCAN; GLYCOCONJUGATE; IMMUNOGLOBULIN M; VACCINE;

EID: 84862659885     PISSN: 00222615     EISSN: None     Source Type: Journal    
DOI: 10.1099/jmm.0.039438-0     Document Type: Review
Times cited : (67)

References (44)
  • 1
    • 0035670918 scopus 로고    scopus 로고
    • Antibody repertoires in infants and adults: Effects of T-independent and T-dependent immunizations
    • Adderson, E. E. (2001). Antibody repertoires in infants and adults: effects of T-independent and T-dependent immunizations. Springer Semin Immunopathol 23, 387-403.
    • (2001) Springer Semin Immunopathol , vol.23 , pp. 387-403
    • Adderson, E.E.1
  • 2
    • 0028988630 scopus 로고
    • pilO, a gene required for glycosylation of Pseudomonas aeruginosa 1244 pilin
    • Castric, P. (1995). pilO, a gene required for glycosylation of Pseudomonas aeruginosa 1244 pilin. Microbiology 141, 1247-1254.
    • (1995) Microbiology , vol.141 , pp. 1247-1254
    • Castric, P.1
  • 3
    • 78651248164 scopus 로고    scopus 로고
    • The Actinobacillus pleuropneumoniae HMW1C-like glycosyltransferase mediates N-linked glycosylation of the Haemophilus influenzae HMW1 adhesin
    • Choi, K. J., Grass, S., Paek, S., St Geme, J. W., III & Yeo, H. J. (2010). The Actinobacillus pleuropneumoniae HMW1C-like glycosyltransferase mediates N-linked glycosylation of the Haemophilus influenzae HMW1 adhesin. PLoS ONE 5, e15888.
    • (2010) PLoS ONE , vol.5
    • Choi, K.J.1    Grass, S.2    Paek, S.3    Geme III., J.W.S.4    Yeo, H.J.5
  • 4
    • 41949117894 scopus 로고    scopus 로고
    • Type IV pili: Paradoxes in form and function
    • Craig, L. & Li, J. (2008). Type IV pili: paradoxes in form and function. Curr Opin Struct Biol 18, 267-277.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 267-277
    • Craig, L.1    Li, J.2
  • 5
    • 77955053157 scopus 로고    scopus 로고
    • Glycoconjugate vaccines and immune interference: A review
    • Dagan, R., Poolman, J. & Siegrist, C. A. (2010). Glycoconjugate vaccines and immune interference: a review. Vaccine 28, 5513-5523.
    • (2010) Vaccine , vol.28 , pp. 5513-5523
    • Dagan, R.1    Poolman, J.2    Siegrist, C.A.3
  • 6
    • 80053602806 scopus 로고    scopus 로고
    • O-linked glycosylation of the PilA pilin protein of Francisella tularensis: Identification of the endogenous protein-targeting oligosaccharyltransferase and characterization of the native oligosaccharide
    • other authors
    • Egge-Jacobsen, W., Salomonsson, E. N., Aas, F. E., Forslund, A. L., Winther-Larsen, H. C., Maier, J., Macellaro, A., Kuoppa, K., Oyston, P. C. & other authors (2011). O-linked glycosylation of the PilA pilin protein of Francisella tularensis: identification of the endogenous protein-targeting oligosaccharyltransferase and characterization of the native oligosaccharide. J Bacteriol 193, 5487-5497.
    • (2011) J Bacteriol , vol.193 , pp. 5487-5497
    • Egge-Jacobsen, W.1    Salomonsson, E.N.2    Aas, F.E.3    Forslund, A.L.4    Winther-Larsen, H.C.5    Maier, J.6    Macellaro, A.7    Kuoppa, K.8    Oyston, P.C.9
  • 7
    • 70350445517 scopus 로고    scopus 로고
    • Functional characterization of flagellin glycosylation in Campylobacter jejuni 81-176
    • Ewing, C. P., Andreishcheva, E. & Guerry, P. (2009). Functional characterization of flagellin glycosylation in Campylobacter jejuni 81-176. J Bacteriol 191, 7086-7093.
    • (2009) J Bacteriol , vol.191 , pp. 7086-7093
    • Ewing, C.P.1    Andreishcheva, E.2    Guerry, P.3
  • 8
    • 36549029858 scopus 로고    scopus 로고
    • Functional characterization of bacterial oligosaccharyltransferases involved in O-linked protein glycosylation
    • Faridmoayer, A., Fentabil, M. A., Mills, D. C., Klassen, J. S. & Feldman, M. F. (2007). Functional characterization of bacterial oligosaccharyltransferases involved in O-linked protein glycosylation. J Bacteriol 189, 8088-8098.
    • (2007) J Bacteriol , vol.189 , pp. 8088-8098
    • Faridmoayer, A.1    Fentabil, M.A.2    Mills, D.C.3    Klassen, J.S.4    Feldman, M.F.5
  • 9
    • 58049214870 scopus 로고    scopus 로고
    • Extreme substrate promiscuity of the Neisseria oligosaccharyl transferase involved in protein Oglycosylation
    • Faridmoayer, A., Fentabil, M. A., Haurat, M. F., Yi, W., Woodward, R., Wang, P. G. & Feldman, M. F. (2008). Extreme substrate promiscuity of the Neisseria oligosaccharyl transferase involved in protein Oglycosylation. J Biol Chem 283, 34596-34604.
    • (2008) J Biol Chem , vol.283 , pp. 34596-34604
    • Faridmoayer, A.1    Fentabil, M.A.2    Haurat, M.F.3    Yi, W.4    Woodward, R.5    Wang, P.G.6    Feldman, M.F.7
  • 12
    • 70350070727 scopus 로고    scopus 로고
    • Preparation of bacterial polysaccharide-protein conjugates: Analytical and manufacturing challenges
    • Frasch, C. E. (2009). Preparation of bacterial polysaccharide-protein conjugates: analytical and manufacturing challenges. Vaccine 27, 6468-6470.
    • (2009) Vaccine , vol.27 , pp. 6468-6470
    • Frasch, C.E.1
  • 13
    • 0037673430 scopus 로고    scopus 로고
    • The Haemophilus influenzae HMW1 adhesin is glycosylated in a process that requires HMW1C and phosphoglucomutase, an enzyme involved in lipooligosaccharide biosynthesis
    • Grass, S., Buscher, A. Z., Swords, W. E., Apicella, M. A., Barenkamp, S. J., Ozchlewski, N. & St Geme, J. W., III (2003). The Haemophilus influenzae HMW1 adhesin is glycosylated in a process that requires HMW1C and phosphoglucomutase, an enzyme involved in lipooligosaccharide biosynthesis. Mol Microbiol 48, 737-751.
    • (2003) Mol Microbiol , vol.48 , pp. 737-751
    • Grass, S.1    Buscher, A.Z.2    Swords, W.E.3    Apicella, M.A.4    Barenkamp, S.J.5    Ozchlewski, N.6    Geme III., J.W.S.7
  • 14
    • 77954080496 scopus 로고    scopus 로고
    • The Haemophilus influenzae HMW1C protein is a glycosyltransferase that transfers hexose residues to asparagine sites in the HMW1 adhesin
    • Grass, S., Lichti, C. F., Townsend, R. R., Gross, J. & St Geme, J. W., III (2010). The Haemophilus influenzae HMW1C protein is a glycosyltransferase that transfers hexose residues to asparagine sites in the HMW1 adhesin. PLoS Pathog 6, e1000919.
    • (2010) PLoS Pathog , vol.6
    • Grass, S.1    Lichti, C.F.2    Townsend, R.R.3    Gross, J.4    Geme III., J.W.S.5
  • 15
    • 54449094921 scopus 로고    scopus 로고
    • The Haemophilus influenzae HMW1 adhesin is a glycoprotein with an unusual N-linked carbohydrate modification
    • Gross, J., Grass, S., Davis, A. E., Gilmore-Erdmann, P., Townsend, R. R. & St Geme, J. W., III (2008). The Haemophilus influenzae HMW1 adhesin is a glycoprotein with an unusual N-linked carbohydrate modification. J Biol Chem 283, 26010-26015.
    • (2008) J Biol Chem , vol.283 , pp. 26010-26015
    • Gross, J.1    Grass, S.2    Davis, A.E.3    Gilmore-Erdmann, P.4    Townsend, R.R.5    Geme III., J.W.S.6
  • 16
    • 79956083561 scopus 로고    scopus 로고
    • Desulfovibrio desulfuricans PglB homolog possesses oligosaccharyltransferase activity with relaxed glycan specificity and distinct protein acceptor sequence requirements
    • Ielmini, M. V. & Feldman, M. F. (2011). Desulfovibrio desulfuricans PglB homolog possesses oligosaccharyltransferase activity with relaxed glycan specificity and distinct protein acceptor sequence requirements. Glycobiology 21, 734-742.
    • (2011) Glycobiology , vol.21 , pp. 734-742
    • Ielmini, M.V.1    Feldman, M.F.2
  • 17
    • 38049051311 scopus 로고    scopus 로고
    • Structure-guided identification of a new catalytic motif of oligosaccharyltransferase
    • Igura, M., Maita, N., Kamishikiryo, J., Yamada, M., Obita, T., Maenaka, K. & Kohda, D. (2008). Structure-guided identification of a new catalytic motif of oligosaccharyltransferase. EMBO J 27, 234-243.
    • (2008) EMBO J , vol.27 , pp. 234-243
    • Igura, M.1    Maita, N.2    Kamishikiryo, J.3    Yamada, M.4    Obita, T.5    Maenaka, K.6    Kohda, D.7
  • 20
    • 80055095714 scopus 로고    scopus 로고
    • Structural insights into the glycosyltransferase activity of the Actinobacillus pleuropneumoniae HMW1C-like protein
    • Kawai, F., Grass, S., Kim, Y., Choi, K. J., St Geme, J. W., III & Yeo, H. J. (2011). Structural insights into the glycosyltransferase activity of the Actinobacillus pleuropneumoniae HMW1C-like protein. J Biol Chem 286, 38546-38557.
    • (2011) J Biol Chem , vol.286 , pp. 38546-38557
    • Kawai, F.1    Grass, S.2    Kim, Y.3    Choi, K.J.4    Geme III., J.W.S.5    Yeo, H.J.6
  • 24
    • 66949119639 scopus 로고    scopus 로고
    • N-linked glycosylation in bacteria: An unexpected application
    • Langdon, R. H., Cuccui, J. & Wren, B. W. (2009). N-linked glycosylation in bacteria: an unexpected application. Future Microbiol 4, 401-412.
    • (2009) Future Microbiol , vol.4 , pp. 401-412
    • Langdon, R.H.1    Cuccui, J.2    Wren, B.W.3
  • 26
    • 0038309565 scopus 로고    scopus 로고
    • Three monophyletic superfamilies account for the majority of the known glycosyltransferases
    • Liu, J. & Mushegian, A. (2003). Three monophyletic superfamilies account for the majority of the known glycosyltransferases. Protein Sci 12, 1418-1431.
    • (2003) Protein Sci , vol.12 , pp. 1418-1431
    • Liu, J.1    Mushegian, A.2
  • 27
    • 79959191882 scopus 로고    scopus 로고
    • X-ray structure of a bacterial oligosaccharyltransferase
    • Lizak, C., Gerber, S., Numao, S., Aebi, M. & Locher, K. P. (2011). X-ray structure of a bacterial oligosaccharyltransferase. Nature 474, 350-355.
    • (2011) Nature , vol.474 , pp. 350-355
    • Lizak, C.1    Gerber, S.2    Numao, S.3    Aebi, M.4    Locher, K.P.5
  • 28
    • 0035863209 scopus 로고    scopus 로고
    • PIG-M transfers the first mannose to glycosylphosphatidylinositol on the lumenal side of the ER
    • Maeda, Y., Watanabe, R., Harris, C. L., Hong, Y., Ohishi, K., Kinoshita, K. & Kinoshita, T. (2001). PIG-M transfers the first mannose to glycosylphosphatidylinositol on the lumenal side of the ER. EMBO J 20, 250-261.
    • (2001) EMBO J , vol.20 , pp. 250-261
    • Maeda, Y.1    Watanabe, R.2    Harris, C.L.3    Hong, Y.4    Ohishi, K.5    Kinoshita, K.6    Kinoshita, T.7
  • 29
    • 77950861521 scopus 로고    scopus 로고
    • Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases
    • Maita, N., Nyirenda, J., Igura, M., Kamishikiryo, J. & Kohda, D. (2010). Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases. J Biol Chem 285, 4941-4950.
    • (2010) J Biol Chem , vol.285 , pp. 4941-4950
    • Maita, N.1    Nyirenda, J.2    Igura, M.3    Kamishikiryo, J.4    Kohda, D.5
  • 31
    • 77958099601 scopus 로고    scopus 로고
    • Protein glycosylation in bacteria: Sweeter than ever
    • Nothaft, H. & Szymanski, C. M. (2010). Protein glycosylation in bacteria: sweeter than ever. Nat Rev Microbiol 8, 765-778.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 765-778
    • Nothaft, H.1    Szymanski, C.M.2
  • 33
    • 33746351043 scopus 로고    scopus 로고
    • Pilin glycosylation in Neisseria meningitidis occurs by a similar pathway to wzydependent O-antigen biosynthesis in Escherichia coli
    • Power, P. M., Seib, K. L. & Jennings, M. P. (2006). Pilin glycosylation in Neisseria meningitidis occurs by a similar pathway to wzydependent O-antigen biosynthesis in Escherichia coli. Biochem Biophys Res Commun 347, 904-908.
    • (2006) Biochem Biophys Res Commun , vol.347 , pp. 904-908
    • Power, P.M.1    Seib, K.L.2    Jennings, M.P.3
  • 34
    • 79952000705 scopus 로고    scopus 로고
    • Relaxed acceptor site specificity of bacterial oligosaccharyltransferase in vivo
    • Schwarz, F., Lizak, C., Fan, Y. Y., Fleurkens, S., Kowarik, M. & Aebi, M. (2011). Relaxed acceptor site specificity of bacterial oligosaccharyltransferase in vivo. Glycobiology 21, 45-54.
    • (2011) Glycobiology , vol.21 , pp. 45-54
    • Schwarz, F.1    Lizak, C.2    Fan, Y.Y.3    Fleurkens, S.4    Kowarik, M.5    Aebi, M.6
  • 35
    • 61749095310 scopus 로고    scopus 로고
    • NMR structure determination of a segmentally labeled glycoprotein using in vitro glycosylation
    • Slynko, V., Schubert, M., Numao, S., Kowarik, M., Aebi, M. & Allain, F. H. (2009). NMR structure determination of a segmentally labeled glycoprotein using in vitro glycosylation. J Am Chem Soc 131, 1274-1281.
    • (2009) J Am Chem Soc , vol.131 , pp. 1274-1281
    • Slynko, V.1    Schubert, M.2    Numao, S.3    Kowarik, M.4    Aebi, M.5    Allain, F.H.6
  • 36
    • 0027400465 scopus 로고
    • Highmolecular- weight proteins of nontypable Haemophilus influenzae mediate attachment to human epithelial cells
    • St Geme, J. W., III, Falkow, S. & Barenkamp, S. J. (1993). Highmolecular- weight proteins of nontypable Haemophilus influenzae mediate attachment to human epithelial cells. Proc Natl Acad Sci U S A 90, 2875-2879.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 2875-2879
    • Geme III., J.W.S.1    Falkow, S.2    Barenkamp, S.J.3
  • 37
    • 0031985210 scopus 로고    scopus 로고
    • Prevalence and distribution of the hmw and hia genes and the HMW and Hia adhesins among genetically diverse strains of nontypeable Haemophilus influenzae
    • St Geme, J. W., III, Kumar, V. V., Cutter, D. & Barenkamp, S. J. (1998). Prevalence and distribution of the hmw and hia genes and the HMW and Hia adhesins among genetically diverse strains of nontypeable Haemophilus influenzae. Infect Immun 66, 364-368.
    • (1998) Infect Immun , vol.66 , pp. 364-368
    • Geme III., J.W.S.1    Kumar, V.V.2    Cutter, D.3    Barenkamp, S.J.4
  • 38
  • 39
    • 0033024228 scopus 로고    scopus 로고
    • Evidence for a system of general protein glycosylation in Campylobacter jejuni
    • Szymanski, C. M., Yao, R., Ewing, C. P., Trust, T.J. & Guerry, P. (1999). Evidence for a system of general protein glycosylation in Campylobacter jejuni. Mol Microbiol 32, 1022-1030.
    • (1999) Mol Microbiol , vol.32 , pp. 1022-1030
    • Szymanski, C.M.1    Yao, R.2    Ewing, C.P.3    Trust, T.J.4    Guerry, P.5
  • 42
    • 33646482093 scopus 로고    scopus 로고
    • Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems
    • other authors
    • Wacker, M., Feldman, M. F., Callewaert, N., Kowarik, M., Clarke, B. R., Pohl, N. L., Hernandez, M., Vines, E. D., Valvano, M. A. & other authors (2006). Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems. Proc Natl Acad Sci U S A 103, 7088-7093.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7088-7093
    • Wacker, M.1    Feldman, M.F.2    Callewaert, N.3    Kowarik, M.4    Clarke, B.R.5    Pohl, N.L.6    Hernandez, M.7    Vines, E.D.8    Valvano, M.A.9
  • 43
    • 0037044765 scopus 로고    scopus 로고
    • Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni
    • other authors
    • Young, N. M., Brisson, J. R., Kelly, J., Watson, D. C., Tessier, L., Lanthier, P. H., Jarrell, H. C., Cadotte, N., St Michael, F. & other authors (2002). Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni. J Biol Chem 277, 42530-42539.
    • (2002) J Biol Chem , vol.277 , pp. 42530-42539
    • Young, N.M.1    Brisson, J.R.2    Kelly, J.3    Watson, D.C.4    Tessier, L.5    Lanthier, P.H.6    Jarrell, H.C.7    Cadotte, N.8    Michael St., F.9
  • 44
    • 0028834273 scopus 로고
    • STT3, a highly conserved protein required for yeast oligosaccharyl transferase activity in vivo
    • Zufferey, R., Knauer, R., Burda, P., Stagljar, I., te Heesen, S., Lehle, L. & Aebi, M. (1995). STT3, a highly conserved protein required for yeast oligosaccharyl transferase activity in vivo. EMBO J 14, 4949-4960.
    • (1995) EMBO J , vol.14 , pp. 4949-4960
    • Zufferey, R.1    Knauer, R.2    Burda, P.3    Stagljar, I.4    te Heesen, S.5    Lehle, L.6    Aebi, M.7


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