메뉴 건너뛰기




Volumn 289, Issue 32, 2014, Pages 21877-21887

The calcium-induced conformation and glycosylation of scavenger-rich cysteine repeat (SRCR) domains of glycoprotein 340 influence the high affinity interaction with antigen I/II homologs

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; CARBOHYDRATES;

EID: 84905844120     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.565507     Document Type: Article
Times cited : (28)

References (52)
  • 1
    • 0018862241 scopus 로고
    • Immunization with a purified protein from Streptococcus mutans against dental caries in rhesus monkeys
    • Lehner, T., Russell, M. W., and Caldwell, J. (1980) Immunization with a purified protein from Streptococcus mutans against dental caries in rhesus monkeys. Lancet 1, 995-996
    • (1980) Lancet , vol.1 , pp. 995-996
    • Lehner, T.1    Russell, M.W.2    Caldwell, J.3
  • 2
    • 2642548781 scopus 로고    scopus 로고
    • A Caries vaccine? the state of the science of immunization against dental caries
    • Russell, M. W., Childers, N. K., Michalik, S. M., Smith, D. J., and Taanman, M. A. (2004) A Caries vaccine? The state of the science of immunization against dental caries. Caries Res. 38, 230-235
    • (2004) Caries Res. , vol.38 , pp. 230-235
    • Russell, M.W.1    Childers, N.K.2    Michalik, S.M.3    Smith, D.J.4    Taanman, M.A.5
  • 3
    • 80051563535 scopus 로고    scopus 로고
    • A therapeutic anti-Streptococcus mutans monoclonal antibody used in human passive protection trials influences the adaptive immune response
    • Robinette, R. A., Olli, M. W., McArthur, W. P., and Brady, L. J. (2011) A therapeutic anti-Streptococcus mutans monoclonal antibody used in human passive protection trials influences the adaptive immune response. Vaccine 29, 6292-6300
    • (2011) Vaccine , vol.29 , pp. 6292-6300
    • Robinette, R.A.1    Olli, M.W.2    McArthur, W.P.3    Brady, L.J.4
  • 4
    • 0034834201 scopus 로고    scopus 로고
    • Regulation of Streptococcus gordonii SspB by the SspA gene product
    • El-Sabens, A., Demuth, D. R., and Lamont, R. J. (2001) Regulation of Streptococcus gordonii SspB by the SspA gene product. Infect. Immun. 69, 6520-6522
    • (2001) Infect. Immun. , vol.69 , pp. 6520-6522
    • El-Sabens, A.1    Demuth, D.R.2    Lamont, R.J.3
  • 5
    • 0035987235 scopus 로고    scopus 로고
    • Role of the Streptococcus gordonii SspB protein in the development of Porphyromonas gingivalis biofilms on streptococcal substrates
    • Lamont, R. J., El-Sabens, A., Park, Y., Cook, G. S., Costantin, J. W., and Demuth, D. R. (2002) Role of the Streptococcus gordonii SspB protein in the development of Porphyromonas gingivalis biofilms on streptococcal substrates. Microbiology 148, 1627-1636
    • (2002) Microbiology , vol.148 , pp. 1627-1636
    • Lamont, R.J.1    El-Sabens, A.2    Park, Y.3    Cook, G.S.4    Costantin, J.W.5    Demuth, D.R.6
  • 6
    • 0029880150 scopus 로고    scopus 로고
    • Tandem genes encode cell-surface polypeptides SspA and SspB which mediate adhesion of the oral bacterium Streptococcus gordonii to human and bacterial receptors
    • Demuth, D. R., Duan, Y., Brooks, W., Holmes, A. R., McNab, R., and Jenkinson, H. F. (1996) Tandem genes encode cell-surface polypeptides SspA and SspB which mediate adhesion of the oral bacterium Streptococcus gordonii to human and bacterial receptors. Mol. Microbiol. 20, 403-413
    • (1996) Mol. Microbiol. , vol.20 , pp. 403-413
    • Demuth, D.R.1    Duan, Y.2    Brooks, W.3    Holmes, A.R.4    McNab, R.5    Jenkinson, H.F.6
  • 7
    • 0343396431 scopus 로고    scopus 로고
    • Identification of a Porphyromonas gingivalis receptor for the Streptococcus gordonii SspB protein
    • Chung, W. O., Demuth, D. R., and Lamont, R. J. (2000) Identification of a Porphyromonas gingivalis receptor for the Streptococcus gordonii SspB protein. Infect. Immun. 68, 6758-6762
    • (2000) Infect. Immun. , vol.68 , pp. 6758-6762
    • Chung, W.O.1    Demuth, D.R.2    Lamont, R.J.3
  • 10
    • 0021104220 scopus 로고
    • Characterization of a salivary agglutinin reacting with a serotype c strain of Streptococcus mutans
    • Ericson, T., and Rundegren, J. (1983) Characterization of a salivary agglutinin reacting with a serotype c strain of Streptococcus mutans. Eur. J. Biochem. 133, 255-261
    • (1983) Eur. J. Biochem. , vol.133 , pp. 255-261
    • Ericson, T.1    Rundegren, J.2
  • 13
    • 79958742851 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal region of Streptococcus mutans antigen I/II and characterization of salivary agglutinin adherence domains
    • Larson, M. R., Rajashankar, K. R., Crowley, P. J., Kelly, C., Mitchell, T. J., Brady, L. J., and Deivanayagam, C. (2011) Crystal structure of the C-terminal region of Streptococcus mutans antigen I/II and characterization of salivary agglutinin adherence domains. J. Biol. Chem. 286, 21657-21666
    • (2011) J. Biol. Chem. , vol.286 , pp. 21657-21666
    • Larson, M.R.1    Rajashankar, K.R.2    Crowley, P.J.3    Kelly, C.4    Mitchell, T.J.5    Brady, L.J.6    Deivanayagam, C.7
  • 14
    • 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, C. C., Wann, E. R., Chen, W., Carson, M., Rajashankar, K. R., Höök, M., and Narayana, S. V. (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    Höök, M.6    Narayana, S.V.7
  • 15
    • 82455212276 scopus 로고    scopus 로고
    • The bacteria binding glycoprotein salivary agglutinin (SAG/gp340) activates complement via the lectin pathway
    • Leito, J. T., Ligtenberg, A. J., van Houdt, M., van den Berg, T. K., and Wouters, D. (2011) The bacteria binding glycoprotein salivary agglutinin (SAG/gp340) activates complement via the lectin pathway. Mol. Immunol. 49, 185-190
    • (2011) Mol. Immunol. , vol.49 , pp. 185-190
    • Leito, J.T.1    Ligtenberg, A.J.2    Van Houdt, M.3    Van Den Berg, T.K.4    Wouters, D.5
  • 16
    • 3042645084 scopus 로고    scopus 로고
    • Gp340 (SAG) binds to the V3 sequence of gp120 important for chemokine receptor interaction
    • Wu, Z., Golub, E., Abrams, W. R., and Malamud, D. (2004) gp340 (SAG) binds to the V3 sequence of gp120 important for chemokine receptor interaction. AIDS Res. Hum. Retroviruses 20, 600-607
    • (2004) AIDS Res. Hum. Retroviruses , vol.20 , pp. 600-607
    • Wu, Z.1    Golub, E.2    Abrams, W.R.3    Malamud, D.4
  • 17
    • 0037200055 scopus 로고    scopus 로고
    • Identification of the bacteria-binding peptide domain on salivary agglutinin (gp-340/DMBT1), a member of the scavenger receptor cysteine-rich superfamily
    • Bikker, F. J., Ligtenberg, A. J., Nazmi, K., Veerman, E. C., van't Hof, W., Bolscher, J. G., Poustka, A., Nieuw Amerongen, A. V., and Mollenhauer, J. (2002) Identification of the bacteria-binding peptide domain on salivary agglutinin (gp-340/DMBT1), a member of the scavenger receptor cysteine-rich superfamily. J. Biol. Chem. 277, 32109-32115
    • (2002) J. Biol. Chem. , vol.277 , pp. 32109-32115
    • Bikker, F.J.1    Ligtenberg, A.J.2    Nazmi, K.3    Veerman, E.C.4    Van'T Hof, W.5    Bolscher, J.G.6    Poustka, A.7    Nieuw Amerongen, A.V.8    Mollenhauer, J.9
  • 19
    • 0031984905 scopus 로고    scopus 로고
    • Binding of salivary glycoprotein-secretory immunoglobulin A complex to the surface protein antigen of Streptococcus mutans
    • Oho, T., Yu, H., Yamashita, Y., and Koga, T. (1998) Binding of salivary glycoprotein-secretory immunoglobulin A complex to the surface protein antigen of Streptococcus mutans. Infect. Immun. 66, 115-121
    • (1998) Infect. Immun. , vol.66 , pp. 115-121
    • Oho, T.1    Yu, H.2    Yamashita, Y.3    Koga, T.4
  • 20
    • 0025672608 scopus 로고
    • Comparison of Streptococcus mutans and Streptococcus sanguis receptors for human salivary agglutinin
    • Demuth, D. R., Lammey, M. S., Huck, M., Lally, E. T., and Malamud, D. (1990) Comparison of Streptococcus mutans and Streptococcus sanguis receptors for human salivary agglutinin. Microb. Pathog. 9, 199-211
    • (1990) Microb. Pathog. , vol.9 , pp. 199-211
    • Demuth, D.R.1    Lammey, M.S.2    Huck, M.3    Lally, E.T.4    Malamud, D.5
  • 23
    • 0033006297 scopus 로고    scopus 로고
    • Crystal structure of a scavenger receptor cysteine-rich domain sheds light on an ancient superfamily
    • Hohenester, E., Sasaki, T., and Timpl, R. (1999) Crystal structure of a scavenger receptor cysteine-rich domain sheds light on an ancient superfamily. Nat. Struct. Biol. 6, 228-232
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 228-232
    • Hohenester, E.1    Sasaki, T.2    Timpl, R.3
  • 24
    • 38449113053 scopus 로고    scopus 로고
    • Gp340 expressed on human genital epithelia binds HIV-1 envelope protein and facilitates viral transmission
    • Stoddard, E., Cannon, G., Ni, H., Karikó, K., Capodici, J., Malamud, D., and Weissman, D. (2007) gp340 expressed on human genital epithelia binds HIV-1 envelope protein and facilitates viral transmission. J. Immunol. 179, 3126-3132
    • (2007) J. Immunol. , vol.179 , pp. 3126-3132
    • Stoddard, E.1    Cannon, G.2    Ni, H.3    Karikó, K.4    Capodici, J.5    Malamud, D.6    Weissman, D.7
  • 26
    • 36248948670 scopus 로고    scopus 로고
    • Salivary agglutinin/glycoprotein-340/DMBT1: A single molecule with variable composition and with different functions in infection, inflammation and cancer
    • Ligtenberg, A. J., Veerman, E. C., Nieuw Amerongen, A. V., and Mollenhauer, J. (2007) Salivary agglutinin/glycoprotein-340/DMBT1: a single molecule with variable composition and with different functions in infection, inflammation and cancer. Biol. Chem. 388, 1275-1289
    • (2007) Biol. Chem. , vol.388 , pp. 1275-1289
    • Ligtenberg, A.J.1    Veerman, E.C.2    Nieuw Amerongen, A.V.3    Mollenhauer, J.4
  • 27
    • 78650997074 scopus 로고    scopus 로고
    • Deleted in malignant brain tumors-1 protein (DMBT1): A pattern recognition receptor with multiple binding sites
    • Ligtenberg, A. J., Karlsson, N. G., and Veerman, E. C. (2010) Deleted in malignant brain tumors-1 protein (DMBT1): a pattern recognition receptor with multiple binding sites. Int. J. Mol. Sci. 11, 5212-5233
    • (2010) Int. J. Mol. Sci. , vol.11 , pp. 5212-5233
    • Ligtenberg, A.J.1    Karlsson, N.G.2    Veerman, E.C.3
  • 28
    • 77953295344 scopus 로고    scopus 로고
    • Review: Gp-340/ DMBT1 in mucosal innate immunity
    • Madsen, J., Mollenhauer, J., and Holmskov, U. (2010) Review: Gp-340/ DMBT1 in mucosal innate immunity. Innate Immun. 16, 160-167
    • (2010) Innate Immun. , vol.16 , pp. 160-167
    • Madsen, J.1    Mollenhauer, J.2    Holmskov, U.3
  • 30
    • 16244391422 scopus 로고    scopus 로고
    • Fluid-or surface-phase human salivary scavenger protein gp340 exposes different bacterial recognition properties
    • Loimaranta, V., Jakubovics, N. S., Hytönen, J., Finne, J., Jenkinson, H. F., and Strömberg, N. (2005) Fluid-or surface-phase human salivary scavenger protein gp340 exposes different bacterial recognition properties. Infect. Immun. 73, 2245-2252
    • (2005) Infect. Immun. , vol.73 , pp. 2245-2252
    • Loimaranta, V.1    Jakubovics, N.S.2    Hytönen, J.3    Finne, J.4    Jenkinson, H.F.5    Strömberg, N.6
  • 32
    • 14844307064 scopus 로고    scopus 로고
    • Differential binding specificities of oral streptococcal antigen I/II family adhesins for human or bacterial ligands
    • Jakubovics, N. S., Strömberg, N., van Dolleweerd, C. J., Kelly, C. G., and Jenkinson, H. F. (2005) Differential binding specificities of oral streptococcal antigen I/II family adhesins for human or bacterial ligands. Mol. Microbiol. 55, 1591-1605
    • (2005) Mol. Microbiol. , vol.55 , pp. 1591-1605
    • Jakubovics, N.S.1    Strömberg, N.2    Van Dolleweerd, C.J.3    Kelly, C.G.4    Jenkinson, H.F.5
  • 33
    • 84878780196 scopus 로고    scopus 로고
    • Cloning, expression and purification of the SRCR domains of glycoprotein 340
    • Purushotham, S., and Deivanayagam, C. (2013) Cloning, expression and purification of the SRCR domains of glycoprotein 340. Protein Expr. Purif. 90, 67-73
    • (2013) Protein Expr. Purif. , vol.90 , pp. 67-73
    • Purushotham, S.1    Deivanayagam, C.2
  • 34
    • 0026579308 scopus 로고
    • Differentiation of salivary agglutinin-mediated adherence and aggregation of mutans streptococci by use of monoclonal antibodies against the major surface adhesin P1
    • Brady, L. J., Piacentini, D. A., Crowley, P. J., Oyston, P. C., and Bleiweis, A. S. (1992) Differentiation of salivary agglutinin-mediated adherence and aggregation of mutans streptococci by use of monoclonal antibodies against the major surface adhesin P1. Infect. Immun. 60, 1008-1017
    • (1992) Infect. Immun. , vol.60 , pp. 1008-1017
    • Brady, L.J.1    Piacentini, D.A.2    Crowley, P.J.3    Oyston, P.C.4    Bleiweis, A.S.5
  • 35
    • 33646354178 scopus 로고    scopus 로고
    • A whole cell BIAcore assay to evaluate P1-mediated adherence of Streptococcus mutans to human salivary agglutinin and inhibition by specific antibodies
    • Oli, M. W., McArthur, W. P., and Brady, L. J. (2006) A whole cell BIAcore assay to evaluate P1-mediated adherence of Streptococcus mutans to human salivary agglutinin and inhibition by specific antibodies. J. Microbiol. Methods 65, 503-511
    • (2006) J. Microbiol. Methods , vol.65 , pp. 503-511
    • Oli, M.W.1    McArthur, W.P.2    Brady, L.J.3
  • 36
    • 0030913948 scopus 로고    scopus 로고
    • Use of surface plasmon resonance to probe the equilibrium and dynamic aspects of interactions between biological macromolecules
    • Schuck, P. (1997) Use of surface plasmon resonance to probe the equilibrium and dynamic aspects of interactions between biological macromolecules. Annu. Rev. Biophys. Biomol. Struct. 26, 541-566
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 541-566
    • Schuck, P.1
  • 37
    • 77952580740 scopus 로고    scopus 로고
    • Requirement of NMB0065 for connecting assembly and export of sialic acid capsular polysaccharides in Neisseria meningitidis
    • Hobb, R. I., Tzeng, Y. L., Choudhury, B. P., Carlson, R. W., and Stephens, D. S. (2010) Requirement of NMB0065 for connecting assembly and export of sialic acid capsular polysaccharides in Neisseria meningitidis. Microbes Infect. 12, 476-487
    • (2010) Microbes Infect. , vol.12 , pp. 476-487
    • Hobb, R.I.1    Tzeng, Y.L.2    Choudhury, B.P.3    Carlson, R.W.4    Stephens, D.S.5
  • 38
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N., and Woody, R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287, 252-260
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 39
    • 1342310505 scopus 로고    scopus 로고
    • Dimethyl sulfoxide at 2.5% (v/v) alters the structural cooperativity and unfolding mechanism of dimeric bacterial NAD synthetase
    • Yang, Z. R., Tendian, S. W., Carson, W. M., Brouillette, W. J., Delucas, L. J., and Brouillette, C. G. (2004) Dimethyl sulfoxide at 2.5% (v/v) alters the structural cooperativity and unfolding mechanism of dimeric bacterial NAD synthetase. Protein Sci. 13, 830-841
    • (2004) Protein Sci. , vol.13 , pp. 830-841
    • Yang, Z.R.1    Tendian, S.W.2    Carson, W.M.3    Brouillette, W.J.4    Delucas, L.J.5    Brouillette, C.G.6
  • 40
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: A tutorial review
    • Lebowitz, J., Lewis, M. S., and Schuck, P. (2002) Modern analytical ultracentrifugation in protein science: a tutorial review. Protein Sci. 11, 2067-2079
    • (2002) Protein Sci. , vol.11 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 41
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys. J. 78, 1606-1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 42
    • 34250378347 scopus 로고    scopus 로고
    • Crystal structure of the third extracellular domain of CD5 reveals the fold of a group B scavenger cysteine-rich receptor domain
    • Rodamilans, B., Munõz, I. G., Bragado-Nilsson, E., Sarrias, M. R., Padilla, O., Blanco, F. J., Lozano, F., and Montoya, G. (2007) Crystal structure of the third extracellular domain of CD5 reveals the fold of a group B scavenger cysteine-rich receptor domain. J. Biol. Chem. 282, 12669-12677
    • (2007) J. Biol. Chem. , vol.282 , pp. 12669-12677
    • Rodamilans, B.1    Munõz, I.G.2    Bragado-Nilsson, E.3    Sarrias, M.R.4    Padilla, O.5    Blanco, F.J.6    Lozano, F.7    Montoya, G.8
  • 43
    • 34447503407 scopus 로고    scopus 로고
    • Crystal structure of the cysteine-rich domain of scavenger receptor MARCO reveals the presence of a basic and an acidic cluster that both contribute to ligand recognition
    • Ojala, J. R., Pikkarainen, T., Tuuttila, A., Sandalova, T., and Tryggvason, K. (2007) Crystal structure of the cysteine-rich domain of scavenger receptor MARCO reveals the presence of a basic and an acidic cluster that both contribute to ligand recognition. J. Biol. Chem. 282, 16654-16666
    • (2007) J. Biol. Chem. , vol.282 , pp. 16654-16666
    • Ojala, J.R.1    Pikkarainen, T.2    Tuuttila, A.3    Sandalova, T.4    Tryggvason, K.5
  • 44
    • 12444316010 scopus 로고    scopus 로고
    • The structure of the extracellular region of human hepsin reveals a serine protease domain and a novel scavenger receptor cysteinerich (SRCR) domain
    • Somoza, J. R., Ho, J. D., Luong, C., Ghate, M., Sprengeler, P. A., Mortara, K., Shrader, W. D., Sperandio, D., Chan, H., McGrath, M. E., and Katz, B. A. (2003) The structure of the extracellular region of human hepsin reveals a serine protease domain and a novel scavenger receptor cysteinerich (SRCR) domain. Structure 11, 1123-1131
    • (2003) Structure , vol.11 , pp. 1123-1131
    • Somoza, J.R.1    Ho, J.D.2    Luong, C.3    Ghate, M.4    Sprengeler, P.A.5    Mortara, K.6    Shrader, W.D.7    Sperandio, D.8    Chan, H.9    McGrath, M.E.10    Katz, B.A.11
  • 45
    • 0025951587 scopus 로고
    • Salivary-agglutinin-mediated adherence of Streptococcus mutans to early plaque bacteria
    • Lamont, R. J., Demuth, D. R., Davis, C. A., Malamud, D., and Rosan, B. (1991) Salivary-agglutinin-mediated adherence of Streptococcus mutans to early plaque bacteria. Infect. Immun. 59, 3446-3450
    • (1991) Infect. Immun. , vol.59 , pp. 3446-3450
    • Lamont, R.J.1    Demuth, D.R.2    Davis, C.A.3    Malamud, D.4    Rosan, B.5
  • 46
    • 84867588241 scopus 로고    scopus 로고
    • Host and bacterial phenotype variation in adhesion of Streptococcus mutans to matched human hosts
    • Esberg, A., Löfgren-Burström, A., Ohman, U., and Strömberg, N. (2012) Host and bacterial phenotype variation in adhesion of Streptococcus mutans to matched human hosts. Infect. Immun. 80, 3869-3879
    • (2012) Infect. Immun. , vol.80 , pp. 3869-3879
    • Esberg, A.1    Löfgren-Burström, A.2    Ohman, U.3    Strömberg, N.4
  • 48
    • 67349231433 scopus 로고    scopus 로고
    • Characterization of Ca2 and phosphocholine interactions with C-reactive protein using a surface plasmon resonance biosensor
    • Christopeit, T., Gossas, T., and Danielson, U. H. (2009) Characterization of Ca2 and phosphocholine interactions with C-reactive protein using a surface plasmon resonance biosensor. Anal. Biochem. 391, 39-44
    • (2009) Anal. Biochem. , vol.391 , pp. 39-44
    • Christopeit, T.1    Gossas, T.2    Danielson, U.H.3
  • 49
    • 0031242908 scopus 로고    scopus 로고
    • On the role of human salivary micelle-like globules in bacterial agglutination
    • Young, A., Rykke, M., Smistad, G., and Rølla, G. (1997) On the role of human salivary micelle-like globules in bacterial agglutination. Eur. J. Oral Sci. 105, 485-494
    • (1997) Eur. J. Oral Sci. , vol.105 , pp. 485-494
    • Young, A.1    Rykke, M.2    Smistad, G.3    Rølla, G.4
  • 51
    • 33745698597 scopus 로고    scopus 로고
    • The N-terminal SRCR-SID domain of gp-340 interacts with HIV type 1 gp120 sequences and inhibits viral infection
    • Wu, Z., Lee, S., Abrams, W., Weissman, D., and Malamud, D. (2006) The N-terminal SRCR-SID domain of gp-340 interacts with HIV type 1 gp120 sequences and inhibits viral infection. AIDS Res. Hum. Retroviruses 22, 508-515
    • (2006) AIDS Res. Hum. Retroviruses , vol.22 , pp. 508-515
    • Wu, Z.1    Lee, S.2    Abrams, W.3    Weissman, D.4    Malamud, D.5
  • 52
    • 69249217928 scopus 로고    scopus 로고
    • Gp340 promotes transcytosis of human immunodeficiency virus type 1 in genital tract-derived cell lines and primary endocervical tissue
    • Stoddard, E., Ni, H., Cannon, G., Zhou, C., Kallenbach, N., Malamud, D., and Weissman, D. (2009) gp340 promotes transcytosis of human immunodeficiency virus type 1 in genital tract-derived cell lines and primary endocervical tissue. J. Virol. 83, 8596-8603
    • (2009) J. Virol. , vol.83 , pp. 8596-8603
    • Stoddard, E.1    Ni, H.2    Cannon, G.3    Zhou, C.4    Kallenbach, N.5    Malamud, D.6    Weissman, D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.