메뉴 건너뛰기




Volumn 7, Issue 7, 2011, Pages

A structural model for binding of the serine-rich repeat adhesin gspb to host carbohydrate receptors

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; CARBOHYDRATE LIGAND; DISACCHARIDE; GSPB PROTEIN; IMMUNOGLOBULIN; LIGAND; PROTEIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; GLYCOCALICIN; LECTIN; MUCIN; SERINE; SIALIC ACID BINDING IG LIKE LECTIN; SIALIC ACID BINDING IG-LIKE LECTIN; SIALOSYL T ANTIGEN; SIALOSYL-T ANTIGEN; THROMBIN RECEPTOR;

EID: 79960931837     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002112     Document Type: Article
Times cited : (72)

References (75)
  • 1
    • 0036176120 scopus 로고    scopus 로고
    • Identification and characterization of hsa, the gene encoding the sialic acid-binding adhesin of Streptococcus gordonii DL1
    • Takahashi Y, Konishi K, Cisar JO, Yoshikawa M, (2002) Identification and characterization of hsa, the gene encoding the sialic acid-binding adhesin of Streptococcus gordonii DL1. Infect Immun 70: 1209-1218.
    • (2002) Infect Immun , vol.70 , pp. 1209-1218
    • Takahashi, Y.1    Konishi, K.2    Cisar, J.O.3    Yoshikawa, M.4
  • 2
    • 17644371383 scopus 로고    scopus 로고
    • Association of a novel high molecular weight, serine-rich protein (SrpA) with fibril-mediated adhesion of the oral biofilm bacterium Streptococcus cristatus
    • Handley PS, Correia FF, Russell K, Rosan B, DiRienzo JM, (2005) Association of a novel high molecular weight, serine-rich protein (SrpA) with fibril-mediated adhesion of the oral biofilm bacterium Streptococcus cristatus. Oral Microbiol Immunol 20: 131-140.
    • (2005) Oral Microbiol Immunol , vol.20 , pp. 131-140
    • Handley, P.S.1    Correia, F.F.2    Russell, K.3    Rosan, B.4    DiRienzo, J.M.5
  • 3
    • 0031959575 scopus 로고    scopus 로고
    • Isolation and characterization of Fap1, a fimbriae-associated adhesin of Streptococcus parasanguis FW213
    • Wu H, Mintz KP, Ladha M, Fives-Taylor PM, (1998) Isolation and characterization of Fap1, a fimbriae-associated adhesin of Streptococcus parasanguis FW213. Mol Microbiol 28: 487-500.
    • (1998) Mol Microbiol , vol.28 , pp. 487-500
    • Wu, H.1    Mintz, K.P.2    Ladha, M.3    Fives-Taylor, P.M.4
  • 4
    • 0036091006 scopus 로고    scopus 로고
    • An accessory sec locus of Streptococcus gordonii is required for export of the surface protein GspB and for normal levels of binding to human platelets
    • Bensing BA, Sullam PM, (2002) An accessory sec locus of Streptococcus gordonii is required for export of the surface protein GspB and for normal levels of binding to human platelets. Mol Microbiol 44: 1081-1094.
    • (2002) Mol Microbiol , vol.44 , pp. 1081-1094
    • Bensing, B.A.1    Sullam, P.M.2
  • 5
    • 77958137426 scopus 로고    scopus 로고
    • The pneumococcal serine-rich repeat protein is an intra-species bacterial adhesin that promotes bacterial aggregation in vivo and in biofilms
    • doi: 10.1371/journal.ppat.1001044
    • Sanchez CJ, Shivshankar P, Stol K, Trakhtenbroit S, Sullam PM, et al. (2010) The pneumococcal serine-rich repeat protein is an intra-species bacterial adhesin that promotes bacterial aggregation in vivo and in biofilms. PLoS Pathog 6 (8): e1001044 doi:10.1371/journal.ppat.1001044.
    • (2010) PLoS Pathog , vol.6 , Issue.8
    • Sanchez, C.J.1    Shivshankar, P.2    Stol, K.3    Trakhtenbroit, S.4    Sullam, P.M.5
  • 6
    • 16244372364 scopus 로고    scopus 로고
    • Role of SraP, a Serine-Rich Surface Protein of Staphylococcus aureus, in binding to human platelets
    • Siboo IR, Chambers HF, Sullam PM, (2005) Role of SraP, a Serine-Rich Surface Protein of Staphylococcus aureus, in binding to human platelets. Infect Immun 73: 2273-2280.
    • (2005) Infect Immun , vol.73 , pp. 2273-2280
    • Siboo, I.R.1    Chambers, H.F.2    Sullam, P.M.3
  • 7
    • 33645545315 scopus 로고    scopus 로고
    • A unique serine-rich repeat protein (Srr-2) and novel surface antigen (epsilon) associated with a virulent lineage of serotype III Streptococcus agalactiae
    • Seifert KN, Adderson EE, Whiting AA, Bohnsack JF, Crowley PJ, et al. (2006) A unique serine-rich repeat protein (Srr-2) and novel surface antigen (epsilon) associated with a virulent lineage of serotype III Streptococcus agalactiae. Microbiology 152: 1029-1040.
    • (2006) Microbiology , vol.152 , pp. 1029-1040
    • Seifert, K.N.1    Adderson, E.E.2    Whiting, A.A.3    Bohnsack, J.F.4    Crowley, P.J.5
  • 8
    • 0033431770 scopus 로고    scopus 로고
    • Identification of dipeptide repeats and a cell wall sorting signal in the fimbriae-associated adhesin, Fap1, of Streptococcus parasanguis
    • Wu H, Fives-Taylor PM, (1999) Identification of dipeptide repeats and a cell wall sorting signal in the fimbriae-associated adhesin, Fap1, of Streptococcus parasanguis. Mol Microbiol 34: 1070-1081.
    • (1999) Mol Microbiol , vol.34 , pp. 1070-1081
    • Wu, H.1    Fives-Taylor, P.M.2
  • 9
    • 17144431888 scopus 로고    scopus 로고
    • A serine-rich glycoprotein of Streptococcus sanguis mediates adhesion to platelets via GPIb
    • Plummer C, Wu H, Kerrigan SW, Meade G, Cox D, et al. (2005) A serine-rich glycoprotein of Streptococcus sanguis mediates adhesion to platelets via GPIb. Br J Haematol 129: 101-109.
    • (2005) Br J Haematol , vol.129 , pp. 101-109
    • Plummer, C.1    Wu, H.2    Kerrigan, S.W.3    Meade, G.4    Cox, D.5
  • 10
    • 33644781570 scopus 로고    scopus 로고
    • Binding of the streptococcal surface glycoproteins GspB and Hsa to human salivary proteins
    • Takamatsu D, Bensing BA, Prakobphol A, Fisher SJ, Sullam PM, (2006) Binding of the streptococcal surface glycoproteins GspB and Hsa to human salivary proteins. Infect Immun 74: 1933-1940.
    • (2006) Infect Immun , vol.74 , pp. 1933-1940
    • Takamatsu, D.1    Bensing, B.A.2    Prakobphol, A.3    Fisher, S.J.4    Sullam, P.M.5
  • 11
    • 26944480061 scopus 로고    scopus 로고
    • Binding of the Streptococcus gordonii surface glycoproteins GspB and Hsa to specific carbohydrate structures on platelet membrane glycoprotein Ib alpha
    • Takamatsu D, Bensing BA, Cheng H, Jarvis GA, Siboo IR, et al. (2005) Binding of the Streptococcus gordonii surface glycoproteins GspB and Hsa to specific carbohydrate structures on platelet membrane glycoprotein Ib alpha. Mol Microbiol 58: 380-392.
    • (2005) Mol Microbiol , vol.58 , pp. 380-392
    • Takamatsu, D.1    Bensing, B.A.2    Cheng, H.3    Jarvis, G.A.4    Siboo, I.R.5
  • 12
    • 65549095152 scopus 로고    scopus 로고
    • The group B streptococcal serine-rich repeat 1 glycoprotein mediates penetration of the blood-brain barrier
    • van Sorge NM, Quach D, Gurney MA, Sullam PM, Nizet V, et al. (2009) The group B streptococcal serine-rich repeat 1 glycoprotein mediates penetration of the blood-brain barrier. J Infect Dis 199: 1479-1487.
    • (2009) J Infect Dis , vol.199 , pp. 1479-1487
    • van Sorge, N.M.1    Quach, D.2    Gurney, M.A.3    Sullam, P.M.4    Nizet, V.5
  • 13
    • 67649404854 scopus 로고    scopus 로고
    • Molecular dissection of the secA2 locus of group B Streptococcus reveals that glycosylation of the Srr1 LPXTG protein is required for full virulence
    • Mistou MY, Dramsi S, Brega S, Poyart C, Trieu-Cuot P, (2009) Molecular dissection of the secA2 locus of group B Streptococcus reveals that glycosylation of the Srr1 LPXTG protein is required for full virulence. J Bacteriol 191: 4195-4206.
    • (2009) J Bacteriol , vol.191 , pp. 4195-4206
    • Mistou, M.Y.1    Dramsi, S.2    Brega, S.3    Poyart, C.4    Trieu-Cuot, P.5
  • 14
    • 51449098668 scopus 로고    scopus 로고
    • Hsa, an adhesin of Streptococcus gordonii DL1, binds to alpha2-3-linked sialic acid on glycophorin A of the erythrocyte membrane
    • Yajima A, Urano-Tashiro Y, Shimazu K, Takashima E, Takahashi Y, et al. (2008) Hsa, an adhesin of Streptococcus gordonii DL1, binds to alpha2-3-linked sialic acid on glycophorin A of the erythrocyte membrane. Microbiol Immunol 52: 69-77.
    • (2008) Microbiol Immunol , vol.52 , pp. 69-77
    • Yajima, A.1    Urano-Tashiro, Y.2    Shimazu, K.3    Takashima, E.4    Takahashi, Y.5
  • 15
    • 0030732136 scopus 로고    scopus 로고
    • A specific cell surface antigen of Streptococcus gordonii is associated with bacterial hemagglutination and adhesion to alpha2-3-linked sialic acid-containing receptors
    • Takahashi Y, Sandberg AL, Ruhl S, Muller J, Cisar JO, (1997) A specific cell surface antigen of Streptococcus gordonii is associated with bacterial hemagglutination and adhesion to alpha2-3-linked sialic acid-containing receptors. Infect Immun 65: 5042-5051.
    • (1997) Infect Immun , vol.65 , pp. 5042-5051
    • Takahashi, Y.1    Sandberg, A.L.2    Ruhl, S.3    Muller, J.4    Cisar, J.O.5
  • 16
    • 35649005443 scopus 로고    scopus 로고
    • The surface protein Srr-1 of Streptococcus agalactiae binds human keratin 4 and promotes adherence to epithelial HEp-2 cells
    • Samen U, Eikmanns BJ, Reinscheid DJ, Borges F, (2007) The surface protein Srr-1 of Streptococcus agalactiae binds human keratin 4 and promotes adherence to epithelial HEp-2 cells. Infect Immun 75: 5405-5414.
    • (2007) Infect Immun , vol.75 , pp. 5405-5414
    • Samen, U.1    Eikmanns, B.J.2    Reinscheid, D.J.3    Borges, F.4
  • 17
    • 70350168050 scopus 로고    scopus 로고
    • The Streptococcus pneumoniae adhesin PsrP binds to Keratin 10 on lung cells
    • Shivshankar P, Sanchez C, Rose LF, Orihuela CJ, (2009) The Streptococcus pneumoniae adhesin PsrP binds to Keratin 10 on lung cells. Mol Microbiol 73: 663-679.
    • (2009) Mol Microbiol , vol.73 , pp. 663-679
    • Shivshankar, P.1    Sanchez, C.2    Rose, L.F.3    Orihuela, C.J.4
  • 18
    • 50949085085 scopus 로고    scopus 로고
    • Role of the serine-rich surface glycoprotein GspB of Streptococcus gordonii in the pathogenesis of infective endocarditis
    • Xiong YQ, Bensing BA, Bayer AS, Chambers HF, Sullam PM, (2008) Role of the serine-rich surface glycoprotein GspB of Streptococcus gordonii in the pathogenesis of infective endocarditis. Microb Pathog 45: 297-301.
    • (2008) Microb Pathog , vol.45 , pp. 297-301
    • Xiong, Y.Q.1    Bensing, B.A.2    Bayer, A.S.3    Chambers, H.F.4    Sullam, P.M.5
  • 19
    • 33746637557 scopus 로고    scopus 로고
    • Identification of a Candidate Streptococcus pneumoniae core genome and regions of diversity correlated with invasive pneumococcal disease
    • Obert C, Sublett J, Kaushal D, Hinojosa E, Barton T, et al. (2006) Identification of a Candidate Streptococcus pneumoniae core genome and regions of diversity correlated with invasive pneumococcal disease. Infect Immun 74: 4766-4777.
    • (2006) Infect Immun , vol.74 , pp. 4766-4777
    • Obert, C.1    Sublett, J.2    Kaushal, D.3    Hinojosa, E.4    Barton, T.5
  • 20
    • 73449137237 scopus 로고    scopus 로고
    • Human platelets recognize a novel surface protein, PadA, on Streptococcus gordonii through a unique interaction involving fibrinogen receptor GPIIbIIIa
    • Petersen HJ, Keane C, Jenkinson HF, Vickerman MM, Jesionowski A, et al. (2010) Human platelets recognize a novel surface protein, PadA, on Streptococcus gordonii through a unique interaction involving fibrinogen receptor GPIIbIIIa. Infect Immun 78: 413-422.
    • (2010) Infect Immun , vol.78 , pp. 413-422
    • Petersen, H.J.1    Keane, C.2    Jenkinson, H.F.3    Vickerman, M.M.4    Jesionowski, A.5
  • 21
    • 36749086963 scopus 로고    scopus 로고
    • Role of Streptococcus gordonii surface proteins SspA/SspB and Hsa in platelet function
    • Kerrigan SW, Jakubovics NS, Keane C, Maguire P, Wynne K, et al. (2007) Role of Streptococcus gordonii surface proteins SspA/SspB and Hsa in platelet function. Infect Immun 75: 5740-5747.
    • (2007) Infect Immun , vol.75 , pp. 5740-5747
    • Kerrigan, S.W.1    Jakubovics, N.S.2    Keane, C.3    Maguire, P.4    Wynne, K.5
  • 22
    • 25444481307 scopus 로고    scopus 로고
    • Functions of cell surface-anchored antigen I/II family and Hsa polypeptides in interactions of Streptococcus gordonii with host receptors
    • Jakubovics NS, Kerrigan SW, Nobbs AH, Stromberg N, van Dolleweerd CJ, et al. (2005) Functions of cell surface-anchored antigen I/II family and Hsa polypeptides in interactions of Streptococcus gordonii with host receptors. Infect Immun 73: 6629-6638.
    • (2005) Infect Immun , vol.73 , pp. 6629-6638
    • Jakubovics, N.S.1    Kerrigan, S.W.2    Nobbs, A.H.3    Stromberg, N.4    van Dolleweerd, C.J.5
  • 23
    • 57149093798 scopus 로고    scopus 로고
    • A structural model of the Staphylococcus aureus ClfA-fibrinogen interaction opens new avenues for the design of anti-staphylococcal therapeutics
    • Ganesh VK, Rivera JJ, Smeds E, Ko YP, Bowden MG, et al. (2008) A structural model of the Staphylococcus aureus ClfA-fibrinogen interaction opens new avenues for the design of anti-staphylococcal therapeutics. PLoS Pathog 4: e1000226.
    • (2008) PLoS Pathog , vol.4
    • Ganesh, V.K.1    Rivera, J.J.2    Smeds, E.3    Ko, Y.P.4    Bowden, M.G.5
  • 24
    • 0030758696 scopus 로고    scopus 로고
    • Characterization of the interaction between the Staphylococcus aureus clumping factor (ClfA) and fibrinogen
    • McDevitt D, Nanavaty T, House-Pompeo K, Bell E, Turner N, et al. (1997) Characterization of the interaction between the Staphylococcus aureus clumping factor (ClfA) and fibrinogen. Eur J Biochem 247: 416-424.
    • (1997) Eur J Biochem , vol.247 , pp. 416-424
    • McDevitt, D.1    Nanavaty, T.2    House-Pompeo, K.3    Bell, E.4    Turner, N.5
  • 25
    • 34447265067 scopus 로고    scopus 로고
    • Both complement- and fibrinogen-dependent mechanisms contribute to platelet aggregation mediated by Staphylococcus aureus clumping factor B
    • Miajlovic H, Loughman A, Brennan M, Cox D, Foster TJ, (2007) Both complement- and fibrinogen-dependent mechanisms contribute to platelet aggregation mediated by Staphylococcus aureus clumping factor B. Infect Immun 75: 3335-3343.
    • (2007) Infect Immun , vol.75 , pp. 3335-3343
    • Miajlovic, H.1    Loughman, A.2    Brennan, M.3    Cox, D.4    Foster, T.J.5
  • 26
    • 22644446001 scopus 로고    scopus 로고
    • Roles for fibrinogen, immunoglobulin and complement in platelet activation promoted by Staphylococcus aureus clumping factor A
    • Loughman A, Fitzgerald JR, Brennan MP, Higgins J, Downer R, et al. (2005) Roles for fibrinogen, immunoglobulin and complement in platelet activation promoted by Staphylococcus aureus clumping factor A. Mol Microbiol 57: 804-818.
    • (2005) Mol Microbiol , vol.57 , pp. 804-818
    • Loughman, A.1    Fitzgerald, J.R.2    Brennan, M.P.3    Higgins, J.4    Downer, R.5
  • 27
    • 0036093924 scopus 로고    scopus 로고
    • Multiple mechanisms for the activation of human platelet aggregation by Staphylococcus aureus: roles for the clumping factors ClfA and ClfB, the serine-aspartate repeat protein SdrE and protein A
    • O'Brien L, Kerrigan SW, Kaw G, Hogan M, Penades J, et al. (2002) Multiple mechanisms for the activation of human platelet aggregation by Staphylococcus aureus: roles for the clumping factors ClfA and ClfB, the serine-aspartate repeat protein SdrE and protein A. Mol Microbiol 44: 1033-1044.
    • (2002) Mol Microbiol , vol.44 , pp. 1033-1044
    • O'Brien, L.1    Kerrigan, S.W.2    Kaw, G.3    Hogan, M.4    Penades, J.5
  • 28
    • 33646854563 scopus 로고    scopus 로고
    • The interaction of bacterial pathogens with platelets
    • Fitzgerald JR, Foster TJ, Cox D, (2006) The interaction of bacterial pathogens with platelets. Nat Rev Microbiol 4: 445-457.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 445-457
    • Fitzgerald, J.R.1    Foster, T.J.2    Cox, D.3
  • 29
    • 77958118272 scopus 로고    scopus 로고
    • Bacteriophage lysin mediates the binding of streptococcus mitis to human platelets through interaction with fibrinogen
    • doi: 1001010.1001371/journal.ppat.1001047
    • Seo HS, Xiong YQ, Mitchell J, Seepersaud R, Bayer AS, et al. (2010) Bacteriophage lysin mediates the binding of streptococcus mitis to human platelets through interaction with fibrinogen. PLoS Pathog 6 (8): e1001047 doi:1001010.1001371/journal.ppat.1001047.
    • (2010) PLoS Pathog , vol.6 , Issue.8
    • Seo, H.S.1    Xiong, Y.Q.2    Mitchell, J.3    Seepersaud, R.4    Bayer, A.S.5
  • 30
    • 0016706381 scopus 로고
    • Experimental bacterial endocarditis. IV. Structure and evolution of very early lesions
    • Durack DT, (1975) Experimental bacterial endocarditis. IV. Structure and evolution of very early lesions. J Pathol 115: 81-89.
    • (1975) J Pathol , vol.115 , pp. 81-89
    • Durack, D.T.1
  • 31
    • 24744467151 scopus 로고    scopus 로고
    • Identification of platelet receptors for the Streptococcus gordonii DL1 sialic acid-binding adhesin
    • Yajima A, Takahashi Y, Konishi K, (2005) Identification of platelet receptors for the Streptococcus gordonii DL1 sialic acid-binding adhesin. Microboil Immunol 49: 795-800.
    • (2005) Microboil Immunol , vol.49 , pp. 795-800
    • Yajima, A.1    Takahashi, Y.2    Konishi, K.3
  • 32
    • 7044249443 scopus 로고    scopus 로고
    • The Streptococcus gordonii surface proteins GspB and Hsa mediate binding to sialylated carbohydrate epitopes on the platelet membrane glycoprotein Ib alpha
    • Bensing BA, Lopez JA, Sullam PA, (2004) The Streptococcus gordonii surface proteins GspB and Hsa mediate binding to sialylated carbohydrate epitopes on the platelet membrane glycoprotein Ib alpha. Infect Immun 72: 6528-6537.
    • (2004) Infect Immun , vol.72 , pp. 6528-6537
    • Bensing, B.A.1    Lopez, J.A.2    Sullam, P.A.3
  • 33
    • 29644438453 scopus 로고    scopus 로고
    • Contribution of sialic acid-binding adhesin to pathogenesis of experimental endocarditis caused by Streptococcus gordonii DL1
    • Takahashi Y, Takashima E, Shimazu K, Yagishita H, Aoba T, et al. (2006) Contribution of sialic acid-binding adhesin to pathogenesis of experimental endocarditis caused by Streptococcus gordonii DL1. Infect Immun 74: 740-743.
    • (2006) Infect Immun , vol.74 , pp. 740-743
    • Takahashi, Y.1    Takashima, E.2    Shimazu, K.3    Yagishita, H.4    Aoba, T.5
  • 34
    • 0142227210 scopus 로고    scopus 로고
    • A "dock, lock, and latch" structural model for a staphylococcal adhesin binding to fibrinogen
    • Ponnuraj K, Bowden MG, Davis S, Gurusiddappa S, Moore D, et al. (2003) A "dock, lock, and latch" structural model for a staphylococcal adhesin binding to fibrinogen. Cell 115: 217-228.
    • (2003) Cell , vol.115 , pp. 217-228
    • Ponnuraj, K.1    Bowden, M.G.2    Davis, S.3    Gurusiddappa, S.4    Moore, D.5
  • 35
    • 0030852467 scopus 로고    scopus 로고
    • Structure of the collagen-binding domain from a Staphylococcus aureus adhesin
    • Symersky J, Patti JM, Carson M, House-Pompeo K, Teale M, et al. (1997) Structure of the collagen-binding domain from a Staphylococcus aureus adhesin. Nat Struct Biol 4: 833-838.
    • (1997) Nat Struct Biol , vol.4 , pp. 833-838
    • Symersky, J.1    Patti, J.M.2    Carson, M.3    House-Pompeo, K.4    Teale, M.5
  • 36
    • 12244313428 scopus 로고    scopus 로고
    • A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A
    • Deivanayagam CC, Wann ER, Chen W, Carson M, Rajashankar KR, et al. (2002) A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A. EMBO J 21: 6660-6672.
    • (2002) EMBO J , vol.21 , pp. 6660-6672
    • Deivanayagam, C.C.1    Wann, E.R.2    Chen, W.3    Carson, M.4    Rajashankar, K.R.5
  • 37
    • 0024468229 scopus 로고
    • Crystal structure of chaperone protein PapD reveals an immunoglobulin fold
    • Holmgren A, Branden CI, (1989) Crystal structure of chaperone protein PapD reveals an immunoglobulin fold. Nature 342: 248-251.
    • (1989) Nature , vol.342 , pp. 248-251
    • Holmgren, A.1    Branden, C.I.2
  • 38
    • 33749169530 scopus 로고    scopus 로고
    • The solution structure of the invasive tip complex from Afa/Dr fibrils
    • Cota E, Jones C, Simpson P, Altroff H, Anderson KL, et al. (2006) The solution structure of the invasive tip complex from Afa/Dr fibrils. Mol Microbiol 62: 356-366.
    • (2006) Mol Microbiol , vol.62 , pp. 356-366
    • Cota, E.1    Jones, C.2    Simpson, P.3    Altroff, H.4    Anderson, K.L.5
  • 39
    • 0033536633 scopus 로고    scopus 로고
    • Crystal structure of invasin: a bacterial integrin-binding protein
    • Hamburger ZA, Brown MS, Isberg RR, Bjorkman PJ, (1999) Crystal structure of invasin: a bacterial integrin-binding protein. Science 286: 291-295.
    • (1999) Science , vol.286 , pp. 291-295
    • Hamburger, Z.A.1    Brown, M.S.2    Isberg, R.R.3    Bjorkman, P.J.4
  • 41
    • 79952736436 scopus 로고    scopus 로고
    • A Model for Group B Streptococcus Pilus Type 1: The Structure of a 35-kDa C-Terminal Fragment of the Major Pilin GBS80
    • Vengadesan K, Ma X, Dwivedi P, Ton-That H, Narayana SV, (2011) A Model for Group B Streptococcus Pilus Type 1: The Structure of a 35-kDa C-Terminal Fragment of the Major Pilin GBS80. J Mol Biol 407: 731-743.
    • (2011) J Mol Biol , vol.407 , pp. 731-743
    • Vengadesan, K.1    Ma, X.2    Dwivedi, P.3    Ton-That, H.4    Narayana, S.V.5
  • 42
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • Holm L, Rosenstrom P, (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res 38: W545-549.
    • (2010) Nucleic Acids Res , vol.38 , pp. 545-549
    • Holm, L.1    Rosenstrom, P.2
  • 43
    • 77957772755 scopus 로고    scopus 로고
    • Structural insights into serine-rich fimbriae from gram-positive bacteria
    • Ramboarina S, Garnett JA, Zhou M, Li Y, Peng Z, et al. (2010) Structural insights into serine-rich fimbriae from gram-positive bacteria. J Biol Chem 285: 32446-32457.
    • (2010) J Biol Chem , vol.285 , pp. 32446-32457
    • Ramboarina, S.1    Garnett, J.A.2    Zhou, M.3    Li, Y.4    Peng, Z.5
  • 44
    • 0032037915 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of sialoadhesin in complex with 3′ sialyllactose at 1.85 A resolution
    • May AP, Robinson RC, Vinson M, Crocker PR, Jones EY, (1998) Crystal structure of the N-terminal domain of sialoadhesin in complex with 3′ sialyllactose at 1.85 A resolution. Mol Cell 1: 719-728.
    • (1998) Mol Cell , vol.1 , pp. 719-728
    • May, A.P.1    Robinson, R.C.2    Vinson, M.3    Crocker, P.R.4    Jones, E.Y.5
  • 45
    • 36549003234 scopus 로고    scopus 로고
    • Structural implications of Siglec-5-mediated sialoglycan recognition
    • Zhuravleva MA, Trandem K, Sun PD, (2008) Structural implications of Siglec-5-mediated sialoglycan recognition. J Mol Biol 375: 437-447.
    • (2008) J Mol Biol , vol.375 , pp. 437-447
    • Zhuravleva, M.A.1    Trandem, K.2    Sun, P.D.3
  • 46
    • 33845948942 scopus 로고    scopus 로고
    • Siglec-7 undergoes a major conformational change when complexed with the alpha(2,8)-disialylganglioside GT1b
    • Attrill H, Imamura A, Sharma RS, Kiso M, Crocker PR, et al. (2006) Siglec-7 undergoes a major conformational change when complexed with the alpha(2,8)-disialylganglioside GT1b. J Biol Chem 281: 32774-32783.
    • (2006) J Biol Chem , vol.281 , pp. 32774-32783
    • Attrill, H.1    Imamura, A.2    Sharma, R.S.3    Kiso, M.4    Crocker, P.R.5
  • 47
    • 36248995861 scopus 로고    scopus 로고
    • The crystal structure of staphylococcal superantigen-like protein 11 in complex with sialyl Lewis X reveals the mechanism for cell binding and immune inhibition
    • Chung MC, Wines BD, Baker H, Langley RJ, Baker EN, et al. (2007) The crystal structure of staphylococcal superantigen-like protein 11 in complex with sialyl Lewis X reveals the mechanism for cell binding and immune inhibition. Mol Microbiol 66: 1342-1355.
    • (2007) Mol Microbiol , vol.66 , pp. 1342-1355
    • Chung, M.C.1    Wines, B.D.2    Baker, H.3    Langley, R.J.4    Baker, E.N.5
  • 48
    • 36249026299 scopus 로고    scopus 로고
    • Crystal structures of the staphylococcal toxin SSL5 in complex with sialyl Lewis X reveal a conserved binding site that shares common features with viral and bacterial sialic acid binding proteins
    • Baker HM, Basu I, Chung MC, Caradoc-Davies T, Fraser JD, et al. (2007) Crystal structures of the staphylococcal toxin SSL5 in complex with sialyl Lewis X reveal a conserved binding site that shares common features with viral and bacterial sialic acid binding proteins. J Mol Biol 374: 1298-1308.
    • (2007) J Mol Biol , vol.374 , pp. 1298-1308
    • Baker, H.M.1    Basu, I.2    Chung, M.C.3    Caradoc-Davies, T.4    Fraser, J.D.5
  • 49
    • 53249151506 scopus 로고    scopus 로고
    • Microbial recognition of human cell surface glycoconjugates
    • Imberty A, Varrot A, (2008) Microbial recognition of human cell surface glycoconjugates. Curr Opin Struct Biol 18: 567-576.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 567-576
    • Imberty, A.1    Varrot, A.2
  • 51
  • 53
    • 45849137475 scopus 로고    scopus 로고
    • The allosteric role of the Ca2+ switch in adhesion and elasticity of C-cadherin
    • Sotomayor M, Schulten K, (2008) The allosteric role of the Ca2+ switch in adhesion and elasticity of C-cadherin. Biophys J 94: 4621-4633.
    • (2008) Biophys J , vol.94 , pp. 4621-4633
    • Sotomayor, M.1    Schulten, K.2
  • 54
    • 53349117639 scopus 로고    scopus 로고
    • Catch-bond mechanism of force-enhanced adhesion: counterintuitive, elusive, but. widespread?
    • Sokurenko EV, Vogel V, Thomas WE, (2008) Catch-bond mechanism of force-enhanced adhesion: counterintuitive, elusive, but.widespread? Cell Host Microbe 4: 314-323.
    • (2008) Cell Host Microbe , vol.4 , pp. 314-323
    • Sokurenko, E.V.1    Vogel, V.2    Thomas, W.E.3
  • 55
    • 78149323419 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray diffraction analysis of the carbohydrate-binding region of the Streptococcus gordonii adhesin GspB
    • Pyburn TM, Yankovskaya V, Bensing BA, Cecchini G, Sullam PM, et al. (2010) Purification, crystallization and preliminary X-ray diffraction analysis of the carbohydrate-binding region of the Streptococcus gordonii adhesin GspB. Acta Crystallogr F Struct Biol Cryst Commun 66: 1503-1507.
    • (2010) Acta Crystallogr F Struct Biol Cryst Commun , vol.66 , pp. 1503-1507
    • Pyburn, T.M.1    Yankovskaya, V.2    Bensing, B.A.3    Cecchini, G.4    Sullam, P.M.5
  • 56
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Macromolecular Crystallography, Pt A 276: 307-326.
    • (1997) Macromolecular Crystallography, Pt A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 57
    • 0028103275 scopus 로고
    • The Ccp4 Suite - Programs for Protein Crystallography
    • Bailey S, (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
    • Bailey, S.1
  • 58
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick GM, (2008) A short history of SHELX. Acta Crystallogr A 64: 112-122.
    • (2008) Acta Crystallogr A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 59
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de La Fortelle E, Bricogne G, (1997) Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Macromolecular Crystallography, Pt A 276: 472-494.
    • (1997) Macromolecular Crystallography, Pt A , vol.276 , pp. 472-494
    • de la Fortelle, E.1    Bricogne, G.2
  • 60
    • 0028103275 scopus 로고
    • The Ccp4 Suite - Programs for Protein Crystallography
    • Bailey S, (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
    • Bailey, S.1
  • 63
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR system
    • Brunger AT, (2007) Version 1.2 of the Crystallography and NMR system. Nat Protoc 2: 2728-2733.
    • (2007) Nat Protoc , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 64
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 67
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: a tool for high-throughput crystallography of protein-ligand complexes
    • Schuttelkopf AW, van Aalten DM, (2004) PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr D Biol Crystallogr 60: 1355-1363.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    van Aalten, D.M.2
  • 68
    • 79960956408 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System
    • DeLano WL, (2002) The PyMOL Molecular Graphics System.
    • (2002)
    • DeLano, W.L.1
  • 69
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme
    • Hayward S, Berendsen HJ, (1998) Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme. Proteins 30: 144-154.
    • (1998) Proteins , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.2
  • 70
    • 0033620366 scopus 로고    scopus 로고
    • A broadly applicable method for the efficient synthesis of alpha-O-linked glycopeptides and clustered sialic acid residues
    • Schwarz JB, Kuduk SD, Chen XT, Sames D, Glunz PW, et al. (1999) A broadly applicable method for the efficient synthesis of alpha-O-linked glycopeptides and clustered sialic acid residues. J Am Chem Soc 121: 2662-2673.
    • (1999) J Am Chem Soc , vol.121 , pp. 2662-2673
    • Schwarz, J.B.1    Kuduk, S.D.2    Chen, X.T.3    Sames, D.4    Glunz, P.W.5
  • 71
    • 34247472609 scopus 로고    scopus 로고
    • Mechanism of cell surface expression of the Streptococcus mitis platelet binding proteins PblA and PblB
    • Mitchell J, Siboo IR, Takamatsu D, Chambers HF, Sullam PM, (2007) Mechanism of cell surface expression of the Streptococcus mitis platelet binding proteins PblA and PblB. Mol Microbiol 64: 844-857.
    • (2007) Mol Microbiol , vol.64 , pp. 844-857
    • Mitchell, J.1    Siboo, I.R.2    Takamatsu, D.3    Chambers, H.F.4    Sullam, P.M.5
  • 72
    • 1942423779 scopus 로고    scopus 로고
    • Genes in the accessory sec locus of Streptococcus gordonii have three functionally distinct effects on the expression of the platelet-binding protein GspB
    • Takamatsu D, Bensing BA, Sullam PM, (2004) Genes in the accessory sec locus of Streptococcus gordonii have three functionally distinct effects on the expression of the platelet-binding protein GspB. Mol Microbiol 52: 189-203.
    • (2004) Mol Microbiol , vol.52 , pp. 189-203
    • Takamatsu, D.1    Bensing, B.A.2    Sullam, P.M.3
  • 73
    • 28244483290 scopus 로고    scopus 로고
    • Determinants of the streptococcal surface glycoprotein GspB that facilitate export by the accessory Sec system
    • Bensing BA, Takamatsu D, Sullam PM, (2005) Determinants of the streptococcal surface glycoprotein GspB that facilitate export by the accessory Sec system. Mol Microbiol 58: 1468-1481.
    • (2005) Mol Microbiol , vol.58 , pp. 1468-1481
    • Bensing, B.A.1    Takamatsu, D.2    Sullam, P.M.3
  • 74
    • 0037474197 scopus 로고    scopus 로고
    • High resolution crystal structures of Siglec-7. Insights into ligand specificity in the Siglec family
    • Alphey MS, Attrill H, Crocker PR, van Aalten DM, (2003) High resolution crystal structures of Siglec-7. Insights into ligand specificity in the Siglec family. J Biol Chem 278: 3372-3377.
    • (2003) J Biol Chem , vol.278 , pp. 3372-3377
    • Alphey, M.S.1    Attrill, H.2    Crocker, P.R.3    van Aalten, D.M.4
  • 75
    • 0030501419 scopus 로고    scopus 로고
    • Use of non-crystallographic symmetry in protein structure refinement
    • Kleywegt GJ, (1996) Use of non-crystallographic symmetry in protein structure refinement. Acta Crystallogr D Biol Crystallogr 52: 842-857.
    • (1996) Acta Crystallogr D Biol Crystallogr , vol.52 , pp. 842-857
    • Kleywegt, G.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.