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Volumn 181, Issue 3, 2008, Pages 1988-2000

Identification of residues in the Cμ4 domain of polymeric IgM essential for interaction with plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BINDING PROTEIN; ERYTHROCYTE MEMBRANE PROTEIN 1; IMMUNOGLOBULIN A; IMMUNOGLOBULIN G; IMMUNOGLOBULIN M; IMMUNOGLOBULIN M ANTIBODY; VIRULENCE FACTOR; ERYTHROCYTE MEMBRANE PROTEIN 1, PLASMODIUM FALCIPARUM; IMMUNOGLOBULIN FC FRAGMENT; LIGAND; POLYMERIC IGM; PROTOZOAL PROTEIN;

EID: 49649106080     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.181.3.1988     Document Type: Article
Times cited : (56)

References (62)
  • 1
    • 0009671779 scopus 로고
    • Structure and function of antibodies
    • F. Calabi and M. S. Neuberger, eds. Elsevier Science Biomedical Division, Amsterdam, pp
    • Burton, D. R. 1987. Structure and function of antibodies. In Molecular Genetics of Immunoglobulin. F. Calabi and M. S. Neuberger, eds. Elsevier Science (Biomedical Division), Amsterdam, pp. 1-49.
    • (1987) Molecular Genetics of Immunoglobulin , pp. 1-49
    • Burton, D.R.1
  • 2
    • 0026009904 scopus 로고
    • Solution structure of human and mouse immunoglobulin M by synchrotron X-ray scattering and molecular graphics modelling: A possible mechanism for complement activation
    • Perkins, S. J., A. S. Nealis, B. J. Sutton, and A. Feinstein. 1991. Solution structure of human and mouse immunoglobulin M by synchrotron X-ray scattering and molecular graphics modelling: a possible mechanism for complement activation. J. Mol. Biol. 221: 1345-1366.
    • (1991) J. Mol. Biol , vol.221 , pp. 1345-1366
    • Perkins, S.J.1    Nealis, A.S.2    Sutton, B.J.3    Feinstein, A.4
  • 6
    • 0020631316 scopus 로고
    • Specific monoclonal IgM is a potent adjuvant in murine malaria vaccination
    • Harte, P. G., A. Cooke, and J. H. Playfair. 1983. Specific monoclonal IgM is a potent adjuvant in murine malaria vaccination. Nature 302: 256-258.
    • (1983) Nature , vol.302 , pp. 256-258
    • Harte, P.G.1    Cooke, A.2    Playfair, J.H.3
  • 7
    • 22044440283 scopus 로고    scopus 로고
    • Parasite-specific IgM plays a significant role in the protective immune response to asexual erythrocytic stage Plasmodium chabaudi AS infection
    • Couper, K. N., R. S. Phillips, F. Brombacher, and J. Alexander. 2005. Parasite-specific IgM plays a significant role in the protective immune response to asexual erythrocytic stage Plasmodium chabaudi AS infection. Parasite Immunol. 27: 171-180.
    • (2005) Parasite Immunol , vol.27 , pp. 171-180
    • Couper, K.N.1    Phillips, R.S.2    Brombacher, F.3    Alexander, J.4
  • 9
    • 0032445137 scopus 로고    scopus 로고
    • A critical role of natural immunoglobulin M in immediate defense against systemic bacterial infection
    • Boes, M., A. P. Prodeus, T. Schmidt, M. C. Carroll, and J. Chen. 1998. A critical role of natural immunoglobulin M in immediate defense against systemic bacterial infection. J. Exp. Med. 188: 2381-2386.
    • (1998) J. Exp. Med , vol.188 , pp. 2381-2386
    • Boes, M.1    Prodeus, A.P.2    Schmidt, T.3    Carroll, M.C.4    Chen, J.5
  • 10
    • 0036591316 scopus 로고    scopus 로고
    • Non-immune IgM, but not IgG binds to the surface of Plasmodium falciparum-infected erythrocytes and correlates with rosetting and severe malaria
    • Rowe, J. A., J. Shafi, O. K. Kai, K. Marsh, and A. Raza. 2002. Non-immune IgM, but not IgG binds to the surface of Plasmodium falciparum-infected erythrocytes and correlates with rosetting and severe malaria. Am. J. Trop. Med. Hyg. 66: 692-699.
    • (2002) Am. J. Trop. Med. Hyg , vol.66 , pp. 692-699
    • Rowe, J.A.1    Shafi, J.2    Kai, O.K.3    Marsh, K.4    Raza, A.5
  • 11
    • 0025612532 scopus 로고
    • Human cerebral malaria: Association with erythrocyte rosetting and lack of anti-rosetting antibodies
    • Carlson, J., H. Helmby, A. V. Hill, D. Brewster, B. M. Greenwood, and M. Wahlgren. 1990. Human cerebral malaria: association with erythrocyte rosetting and lack of anti-rosetting antibodies. Lancet 336: 1457-1460.
    • (1990) Lancet , vol.336 , pp. 1457-1460
    • Carlson, J.1    Helmby, H.2    Hill, A.V.3    Brewster, D.4    Greenwood, B.M.5    Wahlgren, M.6
  • 12
    • 0029007199 scopus 로고
    • Plasmodium falciparum rosetting is associated with malaria severity in Kenya
    • Rowe, J. A., J. Obeiro, C. I. Newbold, and K. Marsh. 1995. Plasmodium falciparum rosetting is associated with malaria severity in Kenya. Infect. Immun. 63: 2323-2326.
    • (1995) Infect. Immun , vol.63 , pp. 2323-2326
    • Rowe, J.A.1    Obeiro, J.2    Newbold, C.I.3    Marsh, K.4
  • 13
    • 0032077688 scopus 로고    scopus 로고
    • Plasmodium falciparum: The importance of IgM in the rosetting of parasite-infected erythrocytes
    • Clough, B., F. A. Atilola, J. Black, and G. Pasvol. 1998. Plasmodium falciparum: the importance of IgM in the rosetting of parasite-infected erythrocytes. Exp. Parasitol. 89: 129-132.
    • (1998) Exp. Parasitol , vol.89 , pp. 129-132
    • Clough, B.1    Atilola, F.A.2    Black, J.3    Pasvol, G.4
  • 14
    • 0030020836 scopus 로고    scopus 로고
    • Novel fibrillar structure confers adhesive property to malaria-infected erythrocytes
    • Scholander, C., C. J. Treutiger, K. Hultenby, and M. Wahlgren. 1996. Novel fibrillar structure confers adhesive property to malaria-infected erythrocytes. Nat. Med. 2: 204-208.
    • (1996) Nat. Med , vol.2 , pp. 204-208
    • Scholander, C.1    Treutiger, C.J.2    Hultenby, K.3    Wahlgren, M.4
  • 15
    • 0034650977 scopus 로고    scopus 로고
    • Multiple human serum components act as bridging molecules in rosette formation by Plasmodium falciparum-infected erythrocytes
    • Somner, E. A., J. Black, and G. Pasvol. 2000. Multiple human serum components act as bridging molecules in rosette formation by Plasmodium falciparum-infected erythrocytes. Blood 95: 674-682.
    • (2000) Blood , vol.95 , pp. 674-682
    • Somner, E.A.1    Black, J.2    Pasvol, G.3
  • 17
    • 0041743960 scopus 로고    scopus 로고
    • Nonspecific immunoglobulin M binding and chondroitin sulfate A binding are linked phenotypes of Plasmodium falciparum isolates implicated in malaria during pregnancy
    • Creasey, A. M., T. Staalsoe, A. Raza, D. E. Arnot, and J. A. Rowe. 2003. Nonspecific immunoglobulin M binding and chondroitin sulfate A binding are linked phenotypes of Plasmodium falciparum isolates implicated in malaria during pregnancy. Infect. Immun. 71: 4767-4771.
    • (2003) Infect. Immun , vol.71 , pp. 4767-4771
    • Creasey, A.M.1    Staalsoe, T.2    Raza, A.3    Arnot, D.E.4    Rowe, J.A.5
  • 19
    • 1142286441 scopus 로고    scopus 로고
    • Interactions of immunoglobulins outside the antigen-combining site
    • Nezlin, R., and V. Ghetie. 2004. Interactions of immunoglobulins outside the antigen-combining site. Adv. Immunol. 82: 155-215.
    • (2004) Adv. Immunol , vol.82 , pp. 155-215
    • Nezlin, R.1    Ghetie, V.2
  • 20
    • 0029052741 scopus 로고
    • Cloning the P. falciparum gene encoding PfEMP1, a malarial variant antigen and adherence receptor on the surface of parasitized human erythrocytes
    • Baruch, D. I., B. L. Pasloske, H. B. Singh, X. Bi, X. C. Ma, M. Feldman, T. F. Taraschi, and R. J. Howard. 1995. Cloning the P. falciparum gene encoding PfEMP1, a malarial variant antigen and adherence receptor on the surface of parasitized human erythrocytes. Cell 82: 77-87.
    • (1995) Cell , vol.82 , pp. 77-87
    • Baruch, D.I.1    Pasloske, B.L.2    Singh, H.B.3    Bi, X.4    Ma, X.C.5    Feldman, M.6    Taraschi, T.F.7    Howard, R.J.8
  • 21
    • 0028982168 scopus 로고
    • Switches in expression of Plasmodium falciparum var genes correlate with changes in antigenic and cytoadherent phenotypes of infected erythrocytes
    • Smith, J. D., C. E. Chitnis, A. G. Craig, D. J. Roberts, D. E. Hudson-Taylor, D. S. Peterson, R. Pinches, C. I. Newbold, and L. H. Miller. 1995. Switches in expression of Plasmodium falciparum var genes correlate with changes in antigenic and cytoadherent phenotypes of infected erythrocytes. Cell 82: 101-110.
    • (1995) Cell , vol.82 , pp. 101-110
    • Smith, J.D.1    Chitnis, C.E.2    Craig, A.G.3    Roberts, D.J.4    Hudson-Taylor, D.E.5    Peterson, D.S.6    Pinches, R.7    Newbold, C.I.8    Miller, L.H.9
  • 22
    • 34748900529 scopus 로고    scopus 로고
    • Antigenic variation in Plasmodium falciparum: Gene organization and regulation of the var multigene family
    • Kyes, S. A., S. M. Kraemer, and J. D. Smith. 2007. Antigenic variation in Plasmodium falciparum: gene organization and regulation of the var multigene family. Eukaryot. Cell 6: 1511-1520.
    • (2007) Eukaryot. Cell , vol.6 , pp. 1511-1520
    • Kyes, S.A.1    Kraemer, S.M.2    Smith, J.D.3
  • 24
    • 0033727467 scopus 로고    scopus 로고
    • Classification of adhesive domains in the Plasmodium falciparum erythrocyte membrane protein 1 family
    • Smith, J. D., G. Subramanian, B. Gamain, D. I. Baruch, and L. H. Miller. 2000. Classification of adhesive domains in the Plasmodium falciparum erythrocyte membrane protein 1 family. Mol. Biochem. Parasitol. 110: 293-310.
    • (2000) Mol. Biochem. Parasitol , vol.110 , pp. 293-310
    • Smith, J.D.1    Subramanian, G.2    Gamain, B.3    Baruch, D.I.4    Miller, L.H.5
  • 25
    • 0034600909 scopus 로고    scopus 로고
    • The semi-conserved head structure of Plasmodium falciparum erythrocyte membrane protein 1 mediates binding to multiple independent host receptors
    • Chen, Q., A. Heddini, A. Barragan, V. Fernandez, S. F. Pearce, and M. Wahlgren. 2000. The semi-conserved head structure of Plasmodium falciparum erythrocyte membrane protein 1 mediates binding to multiple independent host receptors. J. Exp. Med. 192: 1-10.
    • (2000) J. Exp. Med , vol.192 , pp. 1-10
    • Chen, Q.1    Heddini, A.2    Barragan, A.3    Fernandez, V.4    Pearce, S.F.5    Wahlgren, M.6
  • 27
    • 33644830874 scopus 로고    scopus 로고
    • Identification of Plasmodium falciparum var1CSA and var2CSA domains that bind IgM natural antibodies
    • Semblat, J. P., A. Raza, S. A. Kyes, and J. A. Rowe. 2006. Identification of Plasmodium falciparum var1CSA and var2CSA domains that bind IgM natural antibodies. Mol. Biochem. Parasitol. 146: 192-197.
    • (2006) Mol. Biochem. Parasitol , vol.146 , pp. 192-197
    • Semblat, J.P.1    Raza, A.2    Kyes, S.A.3    Rowe, J.A.4
  • 28
    • 0028566589 scopus 로고
    • Plasmodium falciparum: A family of sulphated glycoconjugates disrupts erythrocyte rosettes
    • Rowe, J. A., A. R. Berendt, K. Marsh, and C. I. Newbold. 1994. Plasmodium falciparum: a family of sulphated glycoconjugates disrupts erythrocyte rosettes. Exp. Parasitol. 79: 506-516.
    • (1994) Exp. Parasitol , vol.79 , pp. 506-516
    • Rowe, J.A.1    Berendt, A.R.2    Marsh, K.3    Newbold, C.I.4
  • 29
    • 0026756157 scopus 로고
    • Plasmodium falciparum erythrocyte rosetting is mediated by promiscuous lectin-like interactions
    • Carlson, J., and M. Wahlgren. 1992. Plasmodium falciparum erythrocyte rosetting is mediated by promiscuous lectin-like interactions. J. Exp. Med. 176: 1311-1317.
    • (1992) J. Exp. Med , vol.176 , pp. 1311-1317
    • Carlson, J.1    Wahlgren, M.2
  • 30
    • 1842403514 scopus 로고    scopus 로고
    • Rowe, J. A., J. M. Moulds, C. I. Newbold, and L. H. Miller. 1997. P. falciparum rosetting mediated by a parasite-variant erythrocyte membrane protein and complement-receptor 1. Nature 388: 292-295.
    • Rowe, J. A., J. M. Moulds, C. I. Newbold, and L. H. Miller. 1997. P. falciparum rosetting mediated by a parasite-variant erythrocyte membrane protein and complement-receptor 1. Nature 388: 292-295.
  • 31
    • 0033971074 scopus 로고    scopus 로고
    • A simple RNA analysis method shows var and rif multigene family expression patterns in Plasmodium falciparum
    • Kyes, S. A., R. Pinches, and C. I. Newbold. 2000. A simple RNA analysis method shows var and rif multigene family expression patterns in Plasmodium falciparum. Mol. Biochem. Parasitol. 105: 311-315.
    • (2000) Mol. Biochem. Parasitol , vol.105 , pp. 311-315
    • Kyes, S.A.1    Pinches, R.2    Newbold, C.I.3
  • 32
  • 34
    • 0023918294 scopus 로고
    • Expression of herpes simplex virus type 1 glycoprotein D deletion mutants in mammalian cells
    • Cohen, G. H., W. C. Wilcox, D. L. Sodora, D. Long, J. Z. Levin, and R. J. Eisenberg. 1988. Expression of herpes simplex virus type 1 glycoprotein D deletion mutants in mammalian cells. J. Virol. 62: 1932-1940.
    • (1988) J. Virol , vol.62 , pp. 1932-1940
    • Cohen, G.H.1    Wilcox, W.C.2    Sodora, D.L.3    Long, D.4    Levin, J.Z.5    Eisenberg, R.J.6
  • 35
    • 0028275906 scopus 로고
    • Identification of the erythrocyte binding domains of Plasmodium vivax and Plasmodium knowlesi proteins involved in erythrocyte invasion
    • Chitnis, C. E., and L. H. Miller. 1994. Identification of the erythrocyte binding domains of Plasmodium vivax and Plasmodium knowlesi proteins involved in erythrocyte invasion. J. Exp. Med. 180: 497-506.
    • (1994) J. Exp. Med , vol.180 , pp. 497-506
    • Chitnis, C.E.1    Miller, L.H.2
  • 36
    • 0042326726 scopus 로고    scopus 로고
    • Definition of structural elements in Plasmodium vivax and P. knowlesi Duffy-binding domains necessary for erythrocyte invasion
    • Singh, S. K., A. P. Singh, S. Pandey, S. S. Yazdani, C. E. Chitnis, and A. Sharma. 2003. Definition of structural elements in Plasmodium vivax and P. knowlesi Duffy-binding domains necessary for erythrocyte invasion. Biochem. J. 374: 193-198.
    • (2003) Biochem. J , vol.374 , pp. 193-198
    • Singh, S.K.1    Singh, A.P.2    Pandey, S.3    Yazdani, S.S.4    Chitnis, C.E.5    Sharma, A.6
  • 37
    • 2042454191 scopus 로고    scopus 로고
    • Effect of the IgM and IgA secretory tailpieces on polymerization and secretion of IgM and IgG
    • Sørensen, V., I. B. Rasmussen, L. Norderhaug, I. Natvig, T. E. Michaelsen, and I. Sandlie. 1996. Effect of the IgM and IgA secretory tailpieces on polymerization and secretion of IgM and IgG. J. Immunol. 156: 2858-2865.
    • (1996) J. Immunol , vol.156 , pp. 2858-2865
    • Sørensen, V.1    Rasmussen, I.B.2    Norderhaug, L.3    Natvig, I.4    Michaelsen, T.E.5    Sandlie, I.6
  • 38
    • 0033559864 scopus 로고    scopus 로고
    • Polymerization of IgA and IgM: Roles of Cys309/Cys414 and the secretory tailpiece
    • Sørensen, V., V. Sundvold, T. E. Michaelsen, and I. Sandlie. 1999. Polymerization of IgA and IgM: roles of Cys309/Cys414 and the secretory tailpiece. J. Immunol. 162: 3448-3455.
    • (1999) J. Immunol , vol.162 , pp. 3448-3455
    • Sørensen, V.1    Sundvold, V.2    Michaelsen, T.E.3    Sandlie, I.4
  • 39
    • 0033957809 scopus 로고    scopus 로고
    • Sørensen, V., I. B. Rasmussen, V. Sundvold, T. E. Michaelsen, and I. Sandlie. 2000. Structural requirements for incorporation of J chain into human IgM and IgA. Int. Immunol. 12: 19-27.
    • Sørensen, V., I. B. Rasmussen, V. Sundvold, T. E. Michaelsen, and I. Sandlie. 2000. Structural requirements for incorporation of J chain into human IgM and IgA. Int. Immunol. 12: 19-27.
  • 40
    • 0037044766 scopus 로고    scopus 로고
    • The carboxyl-terminal domains of IgA and IgM direct isotype-specific polymerization and interaction with the polymeric immunoglobulin receptor
    • Braathen, R., V. Sorensen, P. Brandtzaeg, I. Sandlie, and F. E. Johansen. 2002. The carboxyl-terminal domains of IgA and IgM direct isotype-specific polymerization and interaction with the polymeric immunoglobulin receptor. J. Biol. Chem. 277: 42755-42762.
    • (2002) J. Biol. Chem , vol.277 , pp. 42755-42762
    • Braathen, R.1    Sorensen, V.2    Brandtzaeg, P.3    Sandlie, I.4    Johansen, F.E.5
  • 41
    • 0033551694 scopus 로고    scopus 로고
    • Identification of residues in the CH2/CH3 domain interface of IgA essential for interaction with the human Fcα receptor (FcαR) CD89
    • Pleass, R. J., J. I. Dunlop, C. M. Anderson, and J. M. Woof. 1999. Identification of residues in the CH2/CH3 domain interface of IgA essential for interaction with the human Fcα receptor (FcαR) CD89. J. Biol. Chem. 274: 23508-23514.
    • (1999) J. Biol. Chem , vol.274 , pp. 23508-23514
    • Pleass, R.J.1    Dunlop, J.I.2    Anderson, C.M.3    Woof, J.M.4
  • 42
    • 0022352682 scopus 로고
    • Human B-cell activation: Evidence for diverse signals provided by various monoclonal anti-IgM antibodies
    • Rudich, S. M., R. Winchester, and P. K. Mongini. 1985. Human B-cell activation: evidence for diverse signals provided by various monoclonal anti-IgM antibodies. J. Exp. Med. 162: 1236-1255.
    • (1985) J. Exp. Med , vol.162 , pp. 1236-1255
    • Rudich, S.M.1    Winchester, R.2    Mongini, P.K.3
  • 43
    • 0023220280 scopus 로고
    • Analysis of the domain specificity of various murine anti-human IgM monoclonal antibodies differing in human B-lymphocyte signaling activity
    • Rudich, S. M., E. Mihaesco, R. Winchester, and P. K. Mongini. 1987. Analysis of the domain specificity of various murine anti-human IgM monoclonal antibodies differing in human B-lymphocyte signaling activity. Mol. Immunol. 24: 809-820.
    • (1987) Mol. Immunol , vol.24 , pp. 809-820
    • Rudich, S.M.1    Mihaesco, E.2    Winchester, R.3    Mongini, P.K.4
  • 44
    • 0036227659 scopus 로고    scopus 로고
    • Transcription of multiple var genes by individual, trophozoite-stage Plasmodium falciparum cells expressing a chondroitin-sulphate A binding phenotype
    • Duffy, M. F., G. V. Brown, W. Basuki, E. O. Krejany, R. Noviyanti, A. F. Cowman, and J. C. Reeder. 2002. Transcription of multiple var genes by individual, trophozoite-stage Plasmodium falciparum cells expressing a chondroitin-sulphate A binding phenotype. Mol. Microbiol. 43: 1285-1293.
    • (2002) Mol. Microbiol , vol.43 , pp. 1285-1293
    • Duffy, M.F.1    Brown, G.V.2    Basuki, W.3    Krejany, E.O.4    Noviyanti, R.5    Cowman, A.F.6    Reeder, J.C.7
  • 45
    • 33646931473 scopus 로고    scopus 로고
    • Virulence of malaria is associated with differential expression of Plasmodium falciparum var gene subgroups in a case-control study
    • Kaestli, M., I. A. Cockburn, A. Cortés, K. Baea, J. A. Rowe, and H. P. Beck. 2006. Virulence of malaria is associated with differential expression of Plasmodium falciparum var gene subgroups in a case-control study. J. Infect. Dis. 193: 1567-1574.
    • (2006) J. Infect. Dis , vol.193 , pp. 1567-1574
    • Kaestli, M.1    Cockburn, I.A.2    Cortés, A.3    Baea, K.4    Rowe, J.A.5    Beck, H.P.6
  • 49
    • 0035896552 scopus 로고    scopus 로고
    • Streptococcal IgA-binding proteins bind in the Cα2-Cα3 interdomain region and inhibit binding of IgA to human CD89
    • Pleass, R. J., T. Areschoug, G. Lindahl, and J. M. Woof. 2001. Streptococcal IgA-binding proteins bind in the Cα2-Cα3 interdomain region and inhibit binding of IgA to human CD89. J. Biol. Chem. 276: 8197-8204.
    • (2001) J. Biol. Chem , vol.276 , pp. 8197-8204
    • Pleass, R.J.1    Areschoug, T.2    Lindahl, G.3    Woof, J.M.4
  • 50
    • 4344590884 scopus 로고    scopus 로고
    • The role of Plasmodium falciparum var genes in malaria in pregnancy
    • Rowe, J. A., and S. A. Kyes. 2004. The role of Plasmodium falciparum var genes in malaria in pregnancy. Mol. Microbiol. 53: 1011-1019.
    • (2004) Mol. Microbiol , vol.53 , pp. 1011-1019
    • Rowe, J.A.1    Kyes, S.A.2
  • 51
    • 33646900512 scopus 로고    scopus 로고
    • Disguising itself: Insights into Plasmodium falciparum binding and immune evasion from the DBL crystal structure
    • Howell, D. P., R. Samudrala, and J. D. Smith. 2006. Disguising itself: insights into Plasmodium falciparum binding and immune evasion from the DBL crystal structure. Mol. Biochem. Parasitol. 148: 1-9.
    • (2006) Mol. Biochem. Parasitol , vol.148 , pp. 1-9
    • Howell, D.P.1    Samudrala, R.2    Smith, J.D.3
  • 52
    • 36849045753 scopus 로고    scopus 로고
    • Mapping a common interaction site used by Plasmodium falciparum Duffy binding-like domains to bind diverse host receptors
    • Howell, D. P., E. A. Levin, A. L. Springer, S. M. Kraemer, D. J. Phippard, W. R. Schief, and J. D. Smith. 2007. Mapping a common interaction site used by Plasmodium falciparum Duffy binding-like domains to bind diverse host receptors. Mol. Microbiol. 67: 78-87.
    • (2007) Mol. Microbiol , vol.67 , pp. 78-87
    • Howell, D.P.1    Levin, E.A.2    Springer, A.L.3    Kraemer, S.M.4    Phippard, D.J.5    Schief, W.R.6    Smith, J.D.7
  • 53
    • 34250173750 scopus 로고    scopus 로고
    • Episodes of natural selection shaped the interactions of IgA-Fc with FcαRI and bacterial decoy proteins
    • Abi-Rached, L., K. Dorighi, P. J. Norman, M. Yawata, and P. Parham. 2007. Episodes of natural selection shaped the interactions of IgA-Fc with FcαRI and bacterial decoy proteins. J. Immunol. 178: 7943-7954.
    • (2007) J. Immunol , vol.178 , pp. 7943-7954
    • Abi-Rached, L.1    Dorighi, K.2    Norman, P.J.3    Yawata, M.4    Parham, P.5
  • 54
    • 35448981857 scopus 로고    scopus 로고
    • Structural basis for evasion of IgA immunity by Staphylococcus aureus revealed in the complex of SSL7 with Fc of human IgA1
    • Ramsland, P. A., N. Willoughby, H. M. Trist, W. Farrugia, P. M. Hogarth, J. D. Fraser, and B. D. Wines. 2007. Structural basis for evasion of IgA immunity by Staphylococcus aureus revealed in the complex of SSL7 with Fc of human IgA1. Proc. Natl. Acad. Sci. USA 104: 15051-15056.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 15051-15056
    • Ramsland, P.A.1    Willoughby, N.2    Trist, H.M.3    Farrugia, W.4    Hogarth, P.M.5    Fraser, J.D.6    Wines, B.D.7
  • 55
    • 0034548046 scopus 로고    scopus 로고
    • Mapping of the region of complement receptor (CR) 1 required for P. falciparum rosetting and demonstration of the importance of CR1 in resetting in field isolates
    • Rowe, A. J., S. J. Rogerson, A. Raza, J. M. Moulds, M. D. Kazatchkine, K. Marsh, C. I. Newbold, J. P. Atkinson, and L. H. Miller. 2000. Mapping of the region of complement receptor (CR) 1 required for P. falciparum rosetting and demonstration of the importance of CR1 in resetting in field isolates. J. Immunol. 165: 6341-6346.
    • (2000) J. Immunol , vol.165 , pp. 6341-6346
    • Rowe, A.J.1    Rogerson, S.J.2    Raza, A.3    Moulds, J.M.4    Kazatchkine, M.D.5    Marsh, K.6    Newbold, C.I.7    Atkinson, J.P.8    Miller, L.H.9
  • 56
    • 0032711446 scopus 로고    scopus 로고
    • C1q and C4b bind simultaneously to CR1 and additively support erythrocyte adhesion
    • Tas, S. W., L. B. Klickstein, S. F. Barbashov, and A. Nicholson-Weller. 1999. C1q and C4b bind simultaneously to CR1 and additively support erythrocyte adhesion. J. Immunol. 163: 5056-5063.
    • (1999) J. Immunol , vol.163 , pp. 5056-5063
    • Tas, S.W.1    Klickstein, L.B.2    Barbashov, S.F.3    Nicholson-Weller, A.4
  • 58
    • 4644295135 scopus 로고    scopus 로고
    • The fine specificity, but not the invasion inhibitory activity, of 19-kilodalton merozoite surface protein 1-specific antibodies is associated with resistance to malarial parasitemia in a cross-sectional survey in The Gambia
    • Corran, P. H., R. A. O'Donnell, J. Todd, C. Uthaipibull, A. A. Holder, B. S. Crabb, and E. M. Riley. 2004. The fine specificity, but not the invasion inhibitory activity, of 19-kilodalton merozoite surface protein 1-specific antibodies is associated with resistance to malarial parasitemia in a cross-sectional survey in The Gambia. Infect. Immun. 72: 6185-6189.
    • (2004) Infect. Immun , vol.72 , pp. 6185-6189
    • Corran, P.H.1    O'Donnell, R.A.2    Todd, J.3    Uthaipibull, C.4    Holder, A.A.5    Crabb, B.S.6    Riley, E.M.7
  • 59
    • 0018775747 scopus 로고
    • Primary structure of a human IgA1 immunoglobulin: IV. Streptococcal IgA1 protease, digestion, Fab and Fc fragments, and the complete amino acid sequence of the alpha 1 heavy chain
    • Putnam, F. W., Y. S. Liu, and T. L. Low. 1979. Primary structure of a human IgA1 immunoglobulin: IV. Streptococcal IgA1 protease, digestion, Fab and Fc fragments, and the complete amino acid sequence of the alpha 1 heavy chain. J. Biol. Chem. 254: 2865-2874.
    • (1979) J. Biol. Chem , vol.254 , pp. 2865-2874
    • Putnam, F.W.1    Liu, Y.S.2    Low, T.L.3
  • 60
    • 0029017509 scopus 로고
    • Assembly of IgM: The role of disulfide bonding and non-covalent interactions
    • Wiersma, E. J., and M. J. Shulman. 1995. Assembly of IgM: the role of disulfide bonding and non-covalent interactions. J. Immunol. 154: 5265-5272.
    • (1995) J. Immunol , vol.154 , pp. 5265-5272
    • Wiersma, E.J.1    Shulman, M.J.2
  • 61
    • 68549137519 scopus 로고    scopus 로고
    • Kabat, E. A., T. T. Wu, M. Reid-Miller, H. Perry, and K. S. Gottesman. 1987. Sequences of Proteins of Immunological Interest, 4th Ed. U.S. Department of Health and Human Services, National Institutes of Health, Washington D.C.
    • Kabat, E. A., T. T. Wu, M. Reid-Miller, H. Perry, and K. S. Gottesman. 1987. Sequences of Proteins of Immunological Interest, 4th Ed. U.S. Department of Health and Human Services, National Institutes of Health, Washington D.C.


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