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Volumn 290, Issue 52, 2015, Pages 30888-30900

A second β-hexosaminidase encoded in the streptococcus pneumoniae genome provides an expanded biochemical ability to degrade host glycans

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIODEGRADATION; ENZYMES; PLANTS (BOTANY); POLYSACCHARIDES; SUGARS;

EID: 84951768903     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.688630     Document Type: Article
Times cited : (19)

References (52)
  • 1
    • 81855185463 scopus 로고    scopus 로고
    • An endo-β-N-acetylglucosaminidase from Enterococcus faecalis V583 responsible for the hydrolysis of high-mannose and hybrid-type N-linked glycans
    • Bøhle, L. A., Mathiesen, G., Vaaje-Kolstad, G., and Eijsink, V. G. (2011) An endo-β-N-acetylglucosaminidase from Enterococcus faecalis V583 responsible for the hydrolysis of high-mannose and hybrid-type N-linked glycans. FEMS Microbiol. Lett. 325, 123-129
    • (2011) FEMS Microbiol. Lett. , vol.325 , pp. 123-129
    • Bøhle, L.A.1    Mathiesen, G.2    Vaaje-Kolstad, G.3    Eijsink, V.G.4
  • 2
    • 83355163344 scopus 로고    scopus 로고
    • Structural basis for the substrate specificity of a novel β-N-acetylhexosaminidase StrH protein from Streptococcus pneumoniae R6
    • Jiang, Y.-L., Yu, W.-L., Zhang, J.-W., Frolet, C., Di Guilmi, A.-M., Zhou, C.-Z., Vernet, T., and Chen, Y. (2011) Structural basis for the substrate specificity of a novel β-N-acetylhexosaminidase StrH protein from Streptococcus pneumoniae R6. J. Biol. Chem. 286, 43004-43012
    • (2011) J. Biol. Chem. , vol.286 , pp. 43004-43012
    • Jiang, Y.-L.1    Yu, W.-L.2    Zhang, J.-W.3    Frolet, C.4    Di Guilmi, A.-M.5    Zhou, C.-Z.6    Vernet, T.7    Chen, Y.8
  • 3
    • 0034647424 scopus 로고    scopus 로고
    • Structures of chitobiase mutants complexed with the substrate di-N-acetyl-D-glucosamine: The catalytic role of the conserved acidic pair, aspartate 539 and glutamate 540
    • Prag, G., Papanikolau, Y., Tavlas, G., Vorgias, C. E., Petratos, K., and Oppenheim, A. B. (2000) Structures of chitobiase mutants complexed with the substrate di-N-acetyl-D-glucosamine: The catalytic role of the conserved acidic pair, aspartate 539 and glutamate 540. J. Mol. Biol. 300, 611-617
    • (2000) J. Mol. Biol. , vol.300 , pp. 611-617
    • Prag, G.1    Papanikolau, Y.2    Tavlas, G.3    Vorgias, C.E.4    Petratos, K.5    Oppenheim, A.B.6
  • 4
    • 84858380596 scopus 로고    scopus 로고
    • Gaining insight into the inhibition of glycoside hydrolase family 20 exo-β-N-acetylhexosaminidases using a structural approach
    • Sumida, T., Stubbs, K. A., Ito, M., and Yokoyama, S. (2012) Gaining insight into the inhibition of glycoside hydrolase family 20 exo-β-N-acetylhexosaminidases using a structural approach. Org. Biomol. Chem. 10, 2607-2612
    • (2012) Org. Biomol. Chem. , vol.10 , pp. 2607-2612
    • Sumida, T.1    Stubbs, K.A.2    Ito, M.3    Yokoyama, S.4
  • 5
    • 0037131312 scopus 로고    scopus 로고
    • Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state
    • Williams, S. J., Mark, B. L., Vocadlo, D. J., James, M. N., and Withers, S. G. (2002) Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. J. Biol. Chem. 277, 40055-40065
    • (2002) J. Biol. Chem. , vol.277 , pp. 40055-40065
    • Williams, S.J.1    Mark, B.L.2    Vocadlo, D.J.3    James, M.N.4    Withers, S.G.5
  • 6
    • 0031466989 scopus 로고    scopus 로고
    • Serratia marcescens chitobiase is a retaining glycosidase utilizing substrate acetamido group participation
    • Drouillard, S., Armand, S., Davies, G. J., Vorgias, C. E., and Henrissat, B. (1997) Serratia marcescens chitobiase is a retaining glycosidase utilizing substrate acetamido group participation. Biochem. J. 328, 945-949
    • (1997) Biochem. J. , vol.328 , pp. 945-949
    • Drouillard, S.1    Armand, S.2    Davies, G.J.3    Vorgias, C.E.4    Henrissat, B.5
  • 8
    • 84883435173 scopus 로고    scopus 로고
    • Lacto-N-biosidase encoded by a novel gene of Bifidobacterium longum subspecies longum shows unique substrate specificity and requires a designated chaperone for its active expression
    • Sakurama, H., Kiyohara, M., Wada, J., Honda, Y., Yamaguchi, M., Fukiya, S., Yokota, A., Ashida, H., Kumagai, H., Kitaoka, M., Yamamoto, K., and Katayama, T. (2013) Lacto-N-biosidase encoded by a novel gene of Bifidobacterium longum subspecies longum shows unique substrate specificity and requires a designated chaperone for its active expression. J. Biol. Chem. 288, 25194-25206
    • (2013) J. Biol. Chem. , vol.288 , pp. 25194-25206
    • Sakurama, H.1    Kiyohara, M.2    Wada, J.3    Honda, Y.4    Yamaguchi, M.5    Fukiya, S.6    Yokota, A.7    Ashida, H.8    Kumagai, H.9    Kitaoka, M.10    Yamamoto, K.11    Katayama, T.12
  • 11
    • 0019772309 scopus 로고
    • Liberation of N-acetylglucosamine-6-sulfate by human β-N-acetylhexosaminidase A
    • Kresse, H., Fuchs, W., Glössl, J., Holtfrerich, D., and Gilberg, W. (1981) Liberation of N-acetylglucosamine-6-sulfate by human β-N-acetylhexosaminidase A. J. Biol. Chem. 256, 12926-12932
    • (1981) J. Biol. Chem. , vol.256 , pp. 12926-12932
    • Kresse, H.1    Fuchs, W.2    Glössl, J.3    Holtfrerich, D.4    Gilberg, W.5
  • 12
    • 0032850439 scopus 로고    scopus 로고
    • Biochemical consequences of mutations causing the GM2 gangliosidoses
    • Mahuran, D. J. (1999) Biochemical consequences of mutations causing the GM2 gangliosidoses. Biochim. Biophys. Acta 1455, 105-138
    • (1999) Biochim. Biophys. Acta , vol.1455 , pp. 105-138
    • Mahuran, D.J.1
  • 14
    • 0000497859 scopus 로고
    • The extracellular glycosidases of Diplococcus pneumonia. II. Purification and properties of a β-N-acetylglucosaminidase. Action on a derivative on the α-1-acid glycoprotein of human plasma
    • Hughes, R. C., and Jeanloz, R. W. (1964) The extracellular glycosidases of Diplococcus pneumoniae. II. Purification and properties of a β-N-acetylglucosaminidase. Action on a derivative on the α-1-acid glycoprotein of human plasma. Biochemistry 3, 1535-1543
    • (1964) Biochemistry , vol.3 , pp. 1535-1543
    • Hughes, R.C.1    Jeanloz, R.W.2
  • 15
    • 0019880919 scopus 로고
    • Substrate specificity of Diplococcal β-N-acetylhexosaminidase, a useful enzyme for the structural studies of complex type asparagine-linked sugar chains
    • Yamashita, K., Ohkura, T., Yoshima, H., and Kobata, A. (1981) Substrate specificity of Diplococcal β-N-acetylhexosaminidase, a useful enzyme for the structural studies of complex type asparagine-linked sugar chains. Biochem Biophys Res Commun. 100, 226-232
    • (1981) Biochem Biophys Res Commun. , vol.100 , pp. 226-232
    • Yamashita, K.1    Ohkura, T.2    Yoshima, H.3    Kobata, A.4
  • 16
    • 0028988019 scopus 로고
    • Cloning and expression of the β-N-acetylglucosaminidase gene from Streptococcus pneumonia. Generation of truncated enzymes with modified aglycon specificity
    • Clarke, V. A., Platt, N., and Butters, T. D. (1995) Cloning and expression of the β-N-acetylglucosaminidase gene from Streptococcus pneumoniae. Generation of truncated enzymes with modified aglycon specificity. J. Biol. Chem. 270, 8805-8814
    • (1995) J. Biol. Chem. , vol.270 , pp. 8805-8814
    • Clarke, V.A.1    Platt, N.2    Butters, T.D.3
  • 17
    • 77951210702 scopus 로고    scopus 로고
    • Three surface exoglycosidases from Streptococcus pneumoniae, NanA, BgaA, and StrH, promote resistance to opsonophagocytic killing by human neutrophils
    • Dalia, A. B., Standish, A. J., and Weiser, J. N. (2010) Three surface exoglycosidases from Streptococcus pneumoniae, NanA, BgaA, and StrH, promote resistance to opsonophagocytic killing by human neutrophils. Infect. Immun. 78, 2108-2116
    • (2010) Infect. Immun. , vol.78 , pp. 2108-2116
    • Dalia, A.B.1    Standish, A.J.2    Weiser, J.N.3
  • 18
    • 8144231515 scopus 로고    scopus 로고
    • Molecular pathogenesis of pneumococcal pneumonia
    • McCullers, J. A., and Tuomanen, E. I. (2001) Molecular pathogenesis of pneumococcal pneumonia. Front. Biosci. 6, 877-889
    • (2001) Front. Biosci. , vol.6 , pp. 877-889
    • McCullers, J.A.1    Tuomanen, E.I.2
  • 19
    • 1442299471 scopus 로고    scopus 로고
    • Streptococcus pneumoniae colonisation: The key to pneumococcal disease
    • Bogaert, D., De Groot, R., and Hermans, P. W. (2004) Streptococcus pneumoniae colonisation: The key to pneumococcal disease. Lancet Infect. Dis. 4, 144-154
    • (2004) Lancet Infect. Dis. , vol.4 , pp. 144-154
    • Bogaert, D.1    De Groot, R.2    Hermans, P.W.3
  • 20
    • 0036047758 scopus 로고    scopus 로고
    • Large-scale identification of serotype 4 Streptococcus pneumoniae virulence factors
    • Hava, D. L., and Camilli, A. (2002) Large-scale identification of serotype 4 Streptococcus pneumoniae virulence factors. Mol. Microbiol. 45, 1389-1406
    • (2002) Mol. Microbiol. , vol.45 , pp. 1389-1406
    • Hava, D.L.1    Camilli, A.2
  • 23
    • 37549072622 scopus 로고    scopus 로고
    • Growth of Streptococcus pneumoniae on human glycoconjugates is dependent upon the sequential activity of bacterial exoglycosidases
    • Burnaugh, A. M., Frantz, L. J., and King, S. J. (2008) Growth of Streptococcus pneumoniae on human glycoconjugates is dependent upon the sequential activity of bacterial exoglycosidases. J. Bacteriol. 190, 221-230
    • (2008) J. Bacteriol. , vol.190 , pp. 221-230
    • Burnaugh, A.M.1    Frantz, L.J.2    King, S.J.3
  • 24
    • 79961039084 scopus 로고    scopus 로고
    • BgaA acts as an adhesin to mediate attachment of some pneumococcal strains to human epithelial cells
    • Limoli, D. H., Sladek, J. A., Fuller, L. A., Singh, A. K., and King, S. J. (2011) BgaA acts as an adhesin to mediate attachment of some pneumococcal strains to human epithelial cells. Microbiology 157, 2369-2381
    • (2011) Microbiology , vol.157 , pp. 2369-2381
    • Limoli, D.H.1    Sladek, J.A.2    Fuller, L.A.3    Singh, A.K.4    King, S.J.5
  • 25
    • 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
  • 27
    • 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
  • 28
    • 33745585810 scopus 로고    scopus 로고
    • Pneumococcal neuraminidases A and B both have essential roles during infection of the respiratory tract and sepsis
    • Manco, S., Hernon, F., Yesilkaya, H., Paton, J. C., Andrew, P. W., and Kadioglu, A. (2006) Pneumococcal neuraminidases A and B both have essential roles during infection of the respiratory tract and sepsis. Infect. Immun. 74, 4014-4020
    • (2006) Infect. Immun. , vol.74 , pp. 4014-4020
    • Manco, S.1    Hernon, F.2    Yesilkaya, H.3    Paton, J.C.4    Andrew, P.W.5    Kadioglu, A.6
  • 30
    • 39649089147 scopus 로고    scopus 로고
    • Structure of N-acetyl-β-D-glucosaminidase (GcnA) from the endocarditis pathogen Streptococcus gordonii and its complex with the mechanism-based inhibitor NAG-thiazoline
    • Langley, D. B., Harty, D. W., Jacques, N. A., Hunter, N., Guss, J. M., and Collyer, C. A (2008) Structure of N-acetyl-β-D-glucosaminidase (GcnA) from the endocarditis pathogen Streptococcus gordonii and its complex with the mechanism-based inhibitor NAG-thiazoline. J. Mol. Biol. 377, 104-116
    • (2008) J. Mol. Biol. , vol.377 , pp. 104-116
    • Langley, D.B.1    Harty, D.W.2    Jacques, N.A.3    Hunter, N.4    Guss, J.M.5    Collyer, C.A.6
  • 32
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No. 4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 33
  • 35
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. (1992) Free R value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 38
    • 0033005813 scopus 로고    scopus 로고
    • Transformation of a type 4 encapsu-lated strain of Streptococcus pneumoniae
    • Bricker, A. L., and Camilli, A. (1999) Transformation of a type 4 encapsu-lated strain of Streptococcus pneumoniae. FEMS Microbiol. Lett. 172, 131-135
    • (1999) FEMS Microbiol. Lett. , vol.172 , pp. 131-135
    • Bricker, A.L.1    Camilli, A.2
  • 39
    • 0037336363 scopus 로고    scopus 로고
    • Characterization of a novel fucose-regulated promoter (PfcsK) suitable for gene essentiality and antibacterial mode-of-action studies in Streptococcus pneumoniae
    • Chan, P. F., O'Dwyer, K. M., Palmer, L. M., Ambrad, J. D., Ingraham, K. A., So, C., Lonetto, M. A., Biswas, S., Rosenberg, M., Holmes, D. J., and Zalacain, M. (2003) Characterization of a novel fucose-regulated promoter (PfcsK) suitable for gene essentiality and antibacterial mode-of-action studies in Streptococcus pneumoniae. J. Bacteriol. 185, 2051-2058
    • (2003) J. Bacteriol. , vol.185 , pp. 2051-2058
    • Chan, P.F.1    O'Dwyer, K.M.2    Palmer, L.M.3    Ambrad, J.D.4    Ingraham, K.A.5    So, C.6    Lonetto, M.A.7    Biswas, S.8    Rosenberg, M.9    Holmes, D.J.10    Zalacain, M.11
  • 40
    • 0013861147 scopus 로고
    • Integration efficiency and genetic recombination in pneumococcal transformation
    • Lacks, S. (1966) Integration efficiency and genetic recombination in pneumococcal transformation. Genetics 53, 207-235
    • (1966) Genetics , vol.53 , pp. 207-235
    • Lacks, S.1
  • 41
    • 84863561152 scopus 로고    scopus 로고
    • Pneumococcal surface proteins: When the whole is greater than the sum of its parts
    • Pérez-Dorado, I., Galan-Bartual, S., and Hermoso, J. A (2012) Pneumococcal surface proteins: When the whole is greater than the sum of its parts. Mol. Oral Microbiol. 27, 221-245
    • (2012) Mol. Oral Microbiol. , vol.27 , pp. 221-245
    • Pérez-Dorado, I.1    Galan-Bartual, S.2    Hermoso, J.A.3
  • 42
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • Henrissat, B., and Davies, G. (1997) Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol. 7, 637-644
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 43
    • 84932643053 scopus 로고    scopus 로고
    • Structural-functional analysis reveals a specific domain organization in family GH20 hexosaminidases
    • Val-Cid, C., Biarnés, X., Faijes, M., and Planas, A. (2015) Structural-functional analysis reveals a specific domain organization in family GH20 hexosaminidases. PLoS ONE 10, e0128075
    • (2015) PLoS ONE , vol.10 , pp. e0128075
    • Val-Cid, C.1    Biarnés, X.2    Faijes, M.3    Planas, A.4
  • 44
    • 19444383900 scopus 로고    scopus 로고
    • Structural analysis of dispersin B, a biofilm-releasing glycoside hydrolase from the periodontopathogen Actinobacillus actinomycetemcomitans
    • Ramasubbu, N., Thomas, L. M., Ragunath, C., and Kaplan, J. B. (2005) Structural analysis of dispersin B, a biofilm-releasing glycoside hydrolase from the periodontopathogen Actinobacillus actinomycetemcomitans. J. Mol. Biol. 349, 475-486
    • (2005) J. Mol. Biol. , vol.349 , pp. 475-486
    • Ramasubbu, N.1    Thomas, L.M.2    Ragunath, C.3    Kaplan, J.B.4
  • 45
    • 0029940470 scopus 로고    scopus 로고
    • Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease
    • Tews, I., Perrakis, A., Oppenheim, A., Dauter, Z., Wilson, K. S., and Vorgias, C. E. (1996) Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease. Nat. Struct. Biol. 3, 638-648
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 638-648
    • Tews, I.1    Perrakis, A.2    Oppenheim, A.3    Dauter, Z.4    Wilson, K.S.5    Vorgias, C.E.6
  • 46
    • 0025782244 scopus 로고
    • N-Acetylglucosaminono-1,5-lactone oxime and the corresponding (phenylcarbamoyl) oxime. Novel and potent inhibitors of β-N-acetylglucosaminidase
    • Horsch, M., Hoesch, L., Vasella, A., and Rast, D. M. (1991) N-Acetylglucosaminono-1,5-lactone oxime and the corresponding (phenylcarbamoyl) oxime. Novel and potent inhibitors of β-N-acetylglucosaminidase. Eur. J. Biochem. 197, 815-818
    • (1991) Eur. J. Biochem. , vol.197 , pp. 815-818
    • Horsch, M.1    Hoesch, L.2    Vasella, A.3    Rast, D.M.4
  • 47
    • 0035971079 scopus 로고    scopus 로고
    • Crystallographic evidence for substrate-assisted catalysis in a bacterial β-hexosaminidase
    • Mark, B. L., Vocadlo, D. J., Knapp, S., Triggs-Raine, B. L., Withers, S. G., and James, M. N. (2001) Crystallographic evidence for substrate-assisted catalysis in a bacterial β-hexosaminidase. J. Biol. Chem. 276, 10330-10337
    • (2001) J. Biol. Chem. , vol.276 , pp. 10330-10337
    • Mark, B.L.1    Vocadlo, D.J.2    Knapp, S.3    Triggs-Raine, B.L.4    Withers, S.G.5    James, M.N.6
  • 48
    • 79953006384 scopus 로고    scopus 로고
    • Structural determinants of an insect β-N-acetyl-D-hexosaminidase specialized as a chitinolytic enzyme
    • Liu, T., Zhang, H., Liu, F., Wu, Q., Shen, X., and Yang, Q. (2011) Structural determinants of an insect β-N-acetyl-D-hexosaminidase specialized as a chitinolytic enzyme. J. Biol. Chem. 286, 4049-4058
    • (2011) J. Biol. Chem. , vol.286 , pp. 4049-4058
    • Liu, T.1    Zhang, H.2    Liu, F.3    Wu, Q.4    Shen, X.5    Yang, Q.6
  • 49
    • 84858121089 scopus 로고    scopus 로고
    • A functional genomics approach to establish the complement of carbohydrate transporters in Streptococcus pneumoniae
    • Bidossi, A., Mulas, L., Decorosi, F., Colomba, L., Ricci, S., Pozzi, G., Deutscher, J., Viti, C., and Oggioni, M. R. (2012) A functional genomics approach to establish the complement of carbohydrate transporters in Streptococcus pneumoniae. PLoS ONE 7, e33320
    • (2012) PLoS ONE , vol.7 , pp. e33320
    • Bidossi, A.1    Mulas, L.2    Decorosi, F.3    Colomba, L.4    Ricci, S.5    Pozzi, G.6    Deutscher, J.7    Viti, C.8    Oggioni, M.R.9
  • 50
    • 65549094677 scopus 로고    scopus 로고
    • Characterization of the Streptococcus pneumoniae BgaC protein as a novel surface β-galactosidase with specific hydrolysis activity for the Galβ1-3GlcNAc moiety of oligosaccharides
    • Jeong, J. K., Kwon, O., Lee, Y. M., Oh, D.-B., Lee, J. M., Kim, S., Kim, E.-H., Le, T. N., Rhee, D.-K., and Kang, H. A. (2009) Characterization of the Streptococcus pneumoniae BgaC protein as a novel surface β-galactosidase with specific hydrolysis activity for the Galβ1-3GlcNAc moiety of oligosaccharides. J. Bacteriol. 191, 3011-3023
    • (2009) J. Bacteriol. , vol.191 , pp. 3011-3023
    • Jeong, J.K.1    Kwon, O.2    Lee, Y.M.3    Oh, D.-B.4    Lee, J.M.5    Kim, S.6    Kim, E.-H.7    Le, T.N.8    Rhee, D.-K.9    Kang, H.A.10
  • 52
    • 0029682322 scopus 로고    scopus 로고
    • Site-directed mutagenesis in vitro by megaprimer PCR
    • Barik, S. (1996) Site-directed mutagenesis in vitro by megaprimer PCR. Methods Mol. Biol. 57, 203-215 5
    • (1996) Methods Mol. Biol. , vol.57 , pp. 203-2155
    • Barik, S.1


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