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Volumn 14, Issue 8, 2012, Pages 1174-1182

Host sialoglycans and bacterial sialidases: A mucosal perspective

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; IMMUNOGLOBULIN A; IMMUNOGLOBULIN G; LACTOFERRIN; LIGAND; MUCIN; PROTEIN SERINE THREONINE KINASE; SIALIC ACID; SIALIDASE; SIALOGLYCOPROTEIN; TOLL LIKE RECEPTOR 4;

EID: 84863999494     PISSN: 14625814     EISSN: 14625822     Source Type: Journal    
DOI: 10.1111/j.1462-5822.2012.01807.x     Document Type: Review
Times cited : (163)

References (54)
  • 1
    • 0035047041 scopus 로고    scopus 로고
    • Comparative enzymology, biochemistry and pathophysiology of human exo-alpha-sialidases (neuraminidases)
    • Achyuthan, K.E., and Achyuthan, A.M. (2001) Comparative enzymology, biochemistry and pathophysiology of human exo-alpha-sialidases (neuraminidases). Comp Biochem Physiol B Biochem Mol Biol 129: 29-64.
    • (2001) Comp Biochem Physiol B Biochem Mol Biol , vol.129 , pp. 29-64
    • Achyuthan, K.E.1    Achyuthan, A.M.2
  • 2
    • 69049084604 scopus 로고    scopus 로고
    • Sialic acid catabolism confers a competitive advantage to pathogenic vibrio cholerae in the mouse intestine
    • Almagro-Moreno, S., and Boyd, E.F. (2009) Sialic acid catabolism confers a competitive advantage to pathogenic vibrio cholerae in the mouse intestine. Infect Immun 77: 3807-3816.
    • (2009) Infect Immun , vol.77 , pp. 3807-3816
    • Almagro-Moreno, S.1    Boyd, E.F.2
  • 3
    • 70450223518 scopus 로고    scopus 로고
    • Neu1 desialylation of sialyl alpha-2,3-linked beta-galactosyl residues of TOLL-like receptor 4 is essential for receptor activation and cellular signaling
    • Amith, S.R., Jayanth, P., Franchuk, S., Finlay, T., Seyrantepe, V., Beyaert, R., etal. (2010) Neu1 desialylation of sialyl alpha-2, 3-linked beta-galactosyl residues of TOLL-like receptor 4 is essential for receptor activation and cellular signaling. Cell Signal 22: 314-324.
    • (2010) Cell Signal , vol.22 , pp. 314-324
    • Amith, S.R.1    Jayanth, P.2    Franchuk, S.3    Finlay, T.4    Seyrantepe, V.5    Beyaert, R.6
  • 4
    • 0036462606 scopus 로고    scopus 로고
    • Chemical diversity in the sialic acids and related alpha-keto acids: an evolutionary perspective
    • Angata, T., and Varki, A. (2002) Chemical diversity in the sialic acids and related alpha-keto acids: an evolutionary perspective. Chem Rev 102: 439-469.
    • (2002) Chem Rev , vol.102 , pp. 439-469
    • Angata, T.1    Varki, A.2
  • 5
    • 77956185954 scopus 로고    scopus 로고
    • A novel role for the IgG Fc glycan: the anti-inflammatory activity of sialylated IgG Fcs
    • Anthony, R.M., and Ravetch, J.V. (2010) A novel role for the IgG Fc glycan: the anti-inflammatory activity of sialylated IgG Fcs. J Clin Immunol 30 (Suppl. 1): S9-14.
    • (2010) J Clin Immunol , vol.30 , Issue.SUPPL. 1
    • Anthony, R.M.1    Ravetch, J.V.2
  • 6
    • 33750489397 scopus 로고    scopus 로고
    • SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans
    • Aspholm, M., Olfat, F.O., Norden, J., Sonden, B., Lundberg, C., Sjostrom, R., etal. (2006) SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans. PLoS Pathog 2: e110.
    • (2006) PLoS Pathog , vol.2
    • Aspholm, M.1    Olfat, F.O.2    Norden, J.3    Sonden, B.4    Lundberg, C.5    Sjostrom, R.6
  • 7
    • 84862141706 scopus 로고    scopus 로고
    • Glycosylation of human milk lactoferrin exhibits dynamic changes during early lactationenhancing its role in pathogenic bacteria-host interactions
    • Epub 19 January).
    • Barboza, M., Pinzon, J., Wickramasinghe, S., Froehlich, J.W., Moeller, I., Smilowitz, J.T., etal. (2012) Glycosylation of human milk lactoferrin exhibits dynamic changes during early lactationenhancing its role in pathogenic bacteria-host interactions. Mol Cell Proteomics (Epub 19 January).
    • (2012) Mol Cell Proteomics
    • Barboza, M.1    Pinzon, J.2    Wickramasinghe, S.3    Froehlich, J.W.4    Moeller, I.5    Smilowitz, J.T.6
  • 9
    • 0025327554 scopus 로고
    • Sialidase activity of the 'Streptococcus milleri group' and other viridans group streptococci
    • Beighton, D., and Whiley, R.A. (1990) Sialidase activity of the 'Streptococcus milleri group' and other viridans group streptococci. J Clin Microbiol 28: 1431-1433.
    • (1990) J Clin Microbiol , vol.28 , pp. 1431-1433
    • Beighton, D.1    Whiley, R.A.2
  • 10
    • 0042307333 scopus 로고    scopus 로고
    • Host-derived sialic acid is incorporated into Haemophilus influenzae lipopolysaccharide and is a major virulence factor in experimental otitis media
    • Bouchet, V., Hood, D.W., Li, J., Brisson, J.R., Randle, G.A., Martin, A., etal. (2003) Host-derived sialic acid is incorporated into Haemophilus influenzae lipopolysaccharide and is a major virulence factor in experimental otitis media. Proc Natl Acad Sci USA 100: 8898-8903.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 8898-8903
    • Bouchet, V.1    Hood, D.W.2    Li, J.3    Brisson, J.R.4    Randle, G.A.5    Martin, A.6
  • 11
    • 66149087332 scopus 로고    scopus 로고
    • Sialic acid (N-acetyl neuraminic acid) utilization by Bacteroides fragilis requires a novel N-acetyl mannosamine epimerase
    • Brigham, C., Caughlan, R., Gallegos, R., Dallas, M.B., Godoy, V.G., and Malamy, M.H. (2009) Sialic acid (N-acetyl neuraminic acid) utilization by Bacteroides fragilis requires a novel N-acetyl mannosamine epimerase. J Bacteriol 191: 3629-3638.
    • (2009) J Bacteriol , vol.191 , pp. 3629-3638
    • Brigham, C.1    Caughlan, R.2    Gallegos, R.3    Dallas, M.B.4    Godoy, V.G.5    Malamy, M.H.6
  • 12
    • 0026580427 scopus 로고
    • Sialidases (neuraminidases) in bacterial vaginosis and bacterial vaginosis-associated microflora
    • Briselden, A.M., Moncla, B.J., Stevens, C.E., and Hillier, S.L. (1992) Sialidases (neuraminidases) in bacterial vaginosis and bacterial vaginosis-associated microflora. J Clin Microbiol 30: 663-666.
    • (1992) J Clin Microbiol , vol.30 , pp. 663-666
    • Briselden, A.M.1    Moncla, B.J.2    Stevens, C.E.3    Hillier, S.L.4
  • 13
    • 0030307332 scopus 로고    scopus 로고
    • Utilization of sialic acid by viridans streptococci
    • Byers, H.L., Homer, K.A., and Beighton, D. (1996) Utilization of sialic acid by viridans streptococci. J Dent Res 75: 1564-1571.
    • (1996) J Dent Res , vol.75 , pp. 1564-1571
    • Byers, H.L.1    Homer, K.A.2    Beighton, D.3
  • 14
    • 57349192094 scopus 로고    scopus 로고
    • Incorporation of a non-human glycan mediates human susceptibility to a bacterial toxin
    • Byres, E., Paton, A.W., Paton, J.C., Lofling, J.C., Smith, D.F., Wilce, M.C., etal. (2008) Incorporation of a non-human glycan mediates human susceptibility to a bacterial toxin. Nature 456: 648-652.
    • (2008) Nature , vol.456 , pp. 648-652
    • Byres, E.1    Paton, A.W.2    Paton, J.C.3    Lofling, J.C.4    Smith, D.F.5    Wilce, M.C.6
  • 15
    • 84863289353 scopus 로고    scopus 로고
    • Leukocyte inflammatory responses provoked by pneumococcal sialidase
    • pii
    • Chang, Y.C., Uchiyama, S., Varki, A., and Nizet, V. (2012) Leukocyte inflammatory responses provoked by pneumococcal sialidase. MBio 3 (1): pii: e00220-11.
    • (2012) MBio , vol.3 , Issue.1
    • Chang, Y.C.1    Uchiyama, S.2    Varki, A.3    Nizet, V.4
  • 16
    • 33947602811 scopus 로고    scopus 로고
    • Siglecs and their roles in the immune system
    • Crocker, P.R., Paulson, J.C., and Varki, A. (2007) Siglecs and their roles in the immune system. Nat Rev Immunol 7: 255-266.
    • (2007) Nat Rev Immunol , vol.7 , pp. 255-266
    • Crocker, P.R.1    Paulson, J.C.2    Varki, A.3
  • 17
    • 0032904283 scopus 로고    scopus 로고
    • Reduction in the adherence of Pseudomonas aeruginosa to native cystic fibrosis epithelium with anti-asialoGM1 antibody and neuraminidase inhibition
    • Davies, J., Dewar, A., Bush, A., Pitt, T., Gruenert, D., Geddes, D.M., and Alton, E.W. (1999) Reduction in the adherence of Pseudomonas aeruginosa to native cystic fibrosis epithelium with anti-asialoGM1 antibody and neuraminidase inhibition. Eur Respir J 13: 565-570.
    • (1999) Eur Respir J , vol.13 , pp. 565-570
    • Davies, J.1    Dewar, A.2    Bush, A.3    Pitt, T.4    Gruenert, D.5    Geddes, D.M.6    Alton, E.W.7
  • 18
    • 22844442011 scopus 로고    scopus 로고
    • A cellular deficiency of gangliosides causes hypersensitivity to Clostridium perfringens phospholipase C
    • Flores-Diaz, M., Alape-Giron, A., Clark, G., Catimel, B., Hirabayashi, Y., Nice, E., etal. (2005) A cellular deficiency of gangliosides causes hypersensitivity to Clostridium perfringens phospholipase C. J Biol Chem 280: 26680-26689.
    • (2005) J Biol Chem , vol.280 , pp. 26680-26689
    • Flores-Diaz, M.1    Alape-Giron, A.2    Clark, G.3    Catimel, B.4    Hirabayashi, Y.5    Nice, E.6
  • 19
    • 0018079485 scopus 로고
    • Neuraminidase production by clostridia
    • Fraser, A.G. (1978) Neuraminidase production by clostridia. J Med Microbiol 11: 269-280.
    • (1978) J Med Microbiol , vol.11 , pp. 269-280
    • Fraser, A.G.1
  • 20
    • 0027526941 scopus 로고
    • A role for Bacteroides fragilis neuraminidase in bacterial growth in two model systems
    • Godoy, V.G., Dallas, M.M., Russo, T.A., and Malamy, M.H. (1993) A role for Bacteroides fragilis neuraminidase in bacterial growth in two model systems. Infect Immun 61: 4415-4426.
    • (1993) Infect Immun , vol.61 , pp. 4415-4426
    • Godoy, V.G.1    Dallas, M.M.2    Russo, T.A.3    Malamy, M.H.4
  • 21
    • 78650912796 scopus 로고    scopus 로고
    • Role of Tannerella forsythia NanH sialidase in epithelial cell attachment
    • Honma, K., Mishima, E., and Sharma, A. (2011) Role of Tannerella forsythia NanH sialidase in epithelial cell attachment. Infect Immun 79: 393-401.
    • (2011) Infect Immun , vol.79 , pp. 393-401
    • Honma, K.1    Mishima, E.2    Sharma, A.3
  • 23
    • 76149123543 scopus 로고    scopus 로고
    • Pneumococcal modification of host sugars: a major contributor to colonization of the human airway?
    • King, S.J. (2010) Pneumococcal modification of host sugars: a major contributor to colonization of the human airway? Mol Oral Microbiol 25: 15-24.
    • (2010) Mol Oral Microbiol , vol.25 , pp. 15-24
    • King, S.J.1
  • 24
    • 33645087140 scopus 로고    scopus 로고
    • Deglycosylation of human glycoconjugates by the sequential activities of exoglycosidases expressed by Streptococcus pneumoniae
    • King, S.J., Hippe, K.R., and Weiser, J.N. (2006) Deglycosylation of human glycoconjugates by the sequential activities of exoglycosidases expressed by Streptococcus pneumoniae. Mol Microbiol 59: 961-974.
    • (2006) Mol Microbiol , vol.59 , pp. 961-974
    • King, S.J.1    Hippe, K.R.2    Weiser, J.N.3
  • 25
    • 66249136714 scopus 로고    scopus 로고
    • A complex, but uniform O-glycosylation of the human MUC2 mucin from colonic biopsies analyzed by nanoLC/MSn
    • Larsson, J.M., Karlsson, H., Sjovall, H., and Hansson, G.C. (2009) A complex, but uniform O-glycosylation of the human MUC2 mucin from colonic biopsies analyzed by nanoLC/MSn. Glycobiology 19: 756-766.
    • (2009) Glycobiology , vol.19 , pp. 756-766
    • Larsson, J.M.1    Karlsson, H.2    Sjovall, H.3    Hansson, G.C.4
  • 26
    • 84855832123 scopus 로고    scopus 로고
    • Hydrolysis of secreted sialoglycoprotein immunoglobulin A (IgA) in ex vivo and biochemical models of bacterial vaginosis
    • Lewis, W.G., Robinson, L.S., Perry, J., Bick, J.L., Peipert, J.F., Allsworth, J.E., and Lewis, A.L. (2012) Hydrolysis of secreted sialoglycoprotein immunoglobulin A (IgA) in ex vivo and biochemical models of bacterial vaginosis. J Biol Chem 287: 2079-2089.
    • (2012) J Biol Chem , vol.287 , pp. 2079-2089
    • Lewis, W.G.1    Robinson, L.S.2    Perry, J.3    Bick, J.L.4    Peipert, J.F.5    Allsworth, J.E.6    Lewis, A.L.7
  • 27
    • 84863231535 scopus 로고    scopus 로고
    • Abrogation of neuraminidase reduces biofilm formation, capsule biosynthesis, and virulence of Porphyromonas gingivalis
    • Li, C., Kurniyati, K., Hu, B., Bian, J., Sun, J., Zhang, W., etal. (2012) Abrogation of neuraminidase reduces biofilm formation, capsule biosynthesis, and virulence of Porphyromonas gingivalis. Infect Immun 80: 3-13.
    • (2012) Infect Immun , vol.80 , pp. 3-13
    • Li, C.1    Kurniyati, K.2    Hu, B.3    Bian, J.4    Sun, J.5    Zhang, W.6
  • 28
    • 84855269934 scopus 로고    scopus 로고
    • Sialidases affect the host cell adherence and epsilon toxin-induced cytotoxicity of Clostridium perfringens type D strain CN3718
    • Li, J., Sayeed, S., Robertson, S., Chen, J., and McClane, B.A. (2011) Sialidases affect the host cell adherence and epsilon toxin-induced cytotoxicity of Clostridium perfringens type D strain CN3718. PLoS Pathog 7: e1002429.
    • (2011) PLoS Pathog , vol.7
    • Li, J.1    Sayeed, S.2    Robertson, S.3    Chen, J.4    McClane, B.A.5
  • 29
    • 0037414478 scopus 로고    scopus 로고
    • Purification and renaturation of membrane neuraminidase from Haemophilus parasuis
    • Lichtensteiger, C.A., and Vimr, E.R. (2003) Purification and renaturation of membrane neuraminidase from Haemophilus parasuis. Vet Microbiol 93: 79-87.
    • (2003) Vet Microbiol , vol.93 , pp. 79-87
    • Lichtensteiger, C.A.1    Vimr, E.R.2
  • 30
    • 79960978002 scopus 로고    scopus 로고
    • Sialylation and fucosylation of epidermal growth factor receptor suppress its dimerization and activation in lung cancer cells
    • Liu, Y.C., Yen, H.Y., Chen, C.Y., Chen, C.H., Cheng, P.F., Juan, Y.H., etal. (2011) Sialylation and fucosylation of epidermal growth factor receptor suppress its dimerization and activation in lung cancer cells. Proc Natl Acad Sci USA 108: 11332-11337.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 11332-11337
    • Liu, Y.C.1    Yen, H.Y.2    Chen, C.Y.3    Chen, C.H.4    Cheng, P.F.5    Juan, Y.H.6
  • 32
    • 53049089034 scopus 로고    scopus 로고
    • Capnocytophaga canimorsus: a human pathogen feeding at the surface of epithelial cells and phagocytes
    • Mally, M., Shin, H., Paroz, C., Landmann, R., and Cornelis, G.R. (2008) Capnocytophaga canimorsus: a human pathogen feeding at the surface of epithelial cells and phagocytes. PLoS Pathog 4: e1000164.
    • (2008) PLoS Pathog , vol.4
    • Mally, M.1    Shin, H.2    Paroz, C.3    Landmann, R.4    Cornelis, G.R.5
  • 33
    • 80054886353 scopus 로고    scopus 로고
    • Bacteroides in the infant gut consume milk oligosaccharides via mucus-utilization pathways
    • Marcobal, A., Barboza, M., Sonnenburg, E.D., Pudlo, N., Martens, E.C., Desai, P., etal. (2011) Bacteroides in the infant gut consume milk oligosaccharides via mucus-utilization pathways. Cell Host Microbe 10: 507-514.
    • (2011) Cell Host Microbe , vol.10 , pp. 507-514
    • Marcobal, A.1    Barboza, M.2    Sonnenburg, E.D.3    Pudlo, N.4    Martens, E.C.5    Desai, P.6
  • 34
    • 0025164808 scopus 로고
    • Sialidase (neuraminidase) activity among gram-negative anaerobic and capnophilic bacteria
    • Moncla, B.J., Braham, P., and Hillier, S.L. (1990) Sialidase (neuraminidase) activity among gram-negative anaerobic and capnophilic bacteria. J Clin Microbiol 28: 422-425.
    • (1990) J Clin Microbiol , vol.28 , pp. 422-425
    • Moncla, B.J.1    Braham, P.2    Hillier, S.L.3
  • 35
    • 80052587040 scopus 로고    scopus 로고
    • Sweet-talk: role of host glycosylation in bacterial pathogenesis of the gastrointestinal tract
    • Moran, A.P., Gupta, A., and Joshi, L. (2011) Sweet-talk: role of host glycosylation in bacterial pathogenesis of the gastrointestinal tract. Gut 60: 1412-1425.
    • (2011) Gut , vol.60 , pp. 1412-1425
    • Moran, A.P.1    Gupta, A.2    Joshi, L.3
  • 37
    • 60549098063 scopus 로고    scopus 로고
    • The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter
    • Mulligan, C., Geertsma, E.R., Severi, E., Kelly, D.J., Poolman, B., and Thomas, G.H. (2009) The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter. Proc Natl Acad Sci USA 106: 1778-1783.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1778-1783
    • Mulligan, C.1    Geertsma, E.R.2    Severi, E.3    Kelly, D.J.4    Poolman, B.5    Thomas, G.H.6
  • 38
    • 0016325394 scopus 로고
    • Induction of neuraminidase from Clostridium perfringens and the correlation of the enzyme with acetylneuraminate pyruvate-lyase
    • Nees, S., and Shauer, R. (1974) Induction of neuraminidase from Clostridium perfringens and the correlation of the enzyme with acetylneuraminate pyruvate-lyase. Behring Inst Mitt 55: 68-78.
    • (1974) Behring Inst Mitt , vol.55 , pp. 68-78
    • Nees, S.1    Shauer, R.2
  • 39
    • 69049109896 scopus 로고    scopus 로고
    • The NanA neuraminidase of Streptococcus pneumoniae is involved in biofilm formation
    • Parker, D., Soong, G., Planet, P., Brower, J., Ratner, A.J., and Prince, A. (2009) The NanA neuraminidase of Streptococcus pneumoniae is involved in biofilm formation. Infect Immun 77: 3722-3730.
    • (2009) Infect Immun , vol.77 , pp. 3722-3730
    • Parker, D.1    Soong, G.2    Planet, P.3    Brower, J.4    Ratner, A.J.5    Prince, A.6
  • 40
    • 84860241831 scopus 로고    scopus 로고
    • Siglecs as sensors of self in innate and adaptive immune responses
    • Paulson, J.C., Macauley, M.S., and Kawasaki, N. (2012) Siglecs as sensors of self in innate and adaptive immune responses. Ann N Y Acad Sci 1253: 37-48.
    • (2012) Ann N Y Acad Sci , vol.1253 , pp. 37-48
    • Paulson, J.C.1    Macauley, M.S.2    Kawasaki, N.3
  • 41
    • 0027185635 scopus 로고
    • The sialidase superfamily and its spread by horizontal gene transfer
    • Roggentin, P., Schauer, R., Hoyer, L.L., and Vimr, E.R. (1993) The sialidase superfamily and its spread by horizontal gene transfer. Mol Microbiol 9: 915-921.
    • (1993) Mol Microbiol , vol.9 , pp. 915-921
    • Roggentin, P.1    Schauer, R.2    Hoyer, L.L.3    Vimr, E.R.4
  • 42
    • 80155132436 scopus 로고    scopus 로고
    • Role of sialidase in glycoprotein utilization by Tannerella forsythia
    • Roy, S., Honma, K., Douglas, C.W., Sharma, A., and Stafford, G.P. (2011) Role of sialidase in glycoprotein utilization by Tannerella forsythia. Microbiology 157: 3195-3202.
    • (2011) Microbiology , vol.157 , pp. 3195-3202
    • Roy, S.1    Honma, K.2    Douglas, C.W.3    Sharma, A.4    Stafford, G.P.5
  • 43
    • 0038165519 scopus 로고    scopus 로고
    • Secretory IgA N- and O-glycans provide a link between the innate and adaptive immune systems
    • Royle, L., Roos, A., Harvey, D.J., Wormald, M.R., van Gijlswijk-Janssen, D., Redwan, R.M., etal. (2003) Secretory IgA N- and O-glycans provide a link between the innate and adaptive immune systems. J Biol Chem 278: 20140-20153.
    • (2003) J Biol Chem , vol.278 , pp. 20140-20153
    • Royle, L.1    Roos, A.2    Harvey, D.J.3    van Wormald, M.R.4    Gijlswijk-Janssen, D.5    Redwan, R.M.6
  • 45
    • 79953329975 scopus 로고    scopus 로고
    • An infant-associated bacterial commensal utilizes breast milk sialyloligosaccharides
    • Sela, D.A., Li, Y., Lerno, L., Wu, S., Marcobal, A.M., German, J.B., etal. (2011) An infant-associated bacterial commensal utilizes breast milk sialyloligosaccharides. J Biol Chem 286: 11909-11918.
    • (2011) J Biol Chem , vol.286 , pp. 11909-11918
    • Sela, D.A.1    Li, Y.2    Lerno, L.3    Wu, S.4    Marcobal, A.M.5    German, J.B.6
  • 46
    • 27944469933 scopus 로고    scopus 로고
    • Sialic acid transport in Haemophilus influenzae is essential for lipopolysaccharide sialylation and serum resistance and is dependent on a novel tripartite ATP-independent periplasmic transporter
    • Severi, E., Randle, G., Kivlin, P., Whitfield, K., Young, R., Moxon, R., etal. (2005) Sialic acid transport in Haemophilus influenzae is essential for lipopolysaccharide sialylation and serum resistance and is dependent on a novel tripartite ATP-independent periplasmic transporter. Mol Microbiol 58: 1173-1185.
    • (2005) Mol Microbiol , vol.58 , pp. 1173-1185
    • Severi, E.1    Randle, G.2    Kivlin, P.3    Whitfield, K.4    Young, R.5    Moxon, R.6
  • 48
    • 33746692516 scopus 로고    scopus 로고
    • Bacterial neuraminidase facilitates mucosal infection by participating in biofilm production
    • Soong, G., Muir, A., Gomez, M.I., Waks, J., Reddy, B., Planet, P., etal. (2006) Bacterial neuraminidase facilitates mucosal infection by participating in biofilm production. J Clin Invest 116: 2297-2305.
    • (2006) J Clin Invest , vol.116 , pp. 2297-2305
    • Soong, G.1    Muir, A.2    Gomez, M.I.3    Waks, J.4    Reddy, B.5    Planet, P.6
  • 49
    • 0030444832 scopus 로고    scopus 로고
    • Sialidases: structures, biological significance and therapeutic potential
    • Taylor, G. (1996) Sialidases: structures, biological significance and therapeutic potential. Curr Opin Struct Biol 6: 830-837.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 830-837
    • Taylor, G.1
  • 50
    • 34247565506 scopus 로고    scopus 로고
    • Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins
    • Varki, A. (2007) Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins. Nature 446: 1023-1029.
    • (2007) Nature , vol.446 , pp. 1023-1029
    • Varki, A.1
  • 52
    • 59649099923 scopus 로고    scopus 로고
    • Structural studies on the Pseudomonas aeruginosa sialidase-like enzyme PA2794 suggest substrate and mechanistic variations
    • Xu, G., Ryan, C., Kiefel, M.J., Wilson, J.C., and Taylor, G.L. (2009) Structural studies on the Pseudomonas aeruginosa sialidase-like enzyme PA2794 suggest substrate and mechanistic variations. J Mol Biol 386: 828-840.
    • (2009) J Mol Biol , vol.386 , pp. 828-840
    • Xu, G.1    Ryan, C.2    Kiefel, M.J.3    Wilson, J.C.4    Taylor, G.L.5
  • 53
    • 77956823164 scopus 로고    scopus 로고
    • Deglycosylation of FcalphaR at N58 increases its binding to IgA
    • Xue, J., Zhao, Q., Zhu, L., and Zhang, W. (2010) Deglycosylation of FcalphaR at N58 increases its binding to IgA. Glycobiology 20: 905-915.
    • (2010) Glycobiology , vol.20 , pp. 905-915
    • Xue, J.1    Zhao, Q.2    Zhu, L.3    Zhang, W.4
  • 54
    • 79951996840 scopus 로고    scopus 로고
    • Comprehensive characterization of the site-specific N-glycosylation of wild-type and recombinant human lactoferrin expressed in the milk of transgenic cloned cattle
    • Yu, T., Guo, C., Wang, J., Hao, P., Sui, S., Chen, X., etal. (2011) Comprehensive characterization of the site-specific N-glycosylation of wild-type and recombinant human lactoferrin expressed in the milk of transgenic cloned cattle. Glycobiology 21: 206-224.
    • (2011) Glycobiology , vol.21 , pp. 206-224
    • Yu, T.1    Guo, C.2    Wang, J.3    Hao, P.4    Sui, S.5    Chen, X.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.