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The 3D structure of C3dg reported here is of great interest for analysis of the role of this protein in the adaptive immune response. Since C3dg and EBV may bind to overlapping regions in CR2, this paper is also of interest with regard to interactions between EBV and CR2
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Manchester M., Valsamakis A., Kaufman R., Liszewski M.K., Alvarez J., Atkinson J.P., Lublin D.M., Oldstone M.B.A. Measles virus and C3 binding sites are distinct on membrane cofactor protein (CD46). Proc Natl Acad Sci USA. 92:1995;2303-2307.
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This paper, which describes a CD46 transgenic mouse line sensitive to measles virus, represents an important breakthrough in the study of both measles virus and CD46
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Oldstone M.B.A., Lewicki H., Thomas D., Tishon A., Dales S., Patterson J., Manchester M., Homann D., Naniche D., Holz A. Measles virus infection in a transgenic model: virus-induced immunosuppression and central nervous system disease. Cell. 98:1999;629-640. This paper, which describes a CD46 transgenic mouse line sensitive to measles virus, represents an important breakthrough in the study of both measles virus and CD46.
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Oldstone, M.B.A.1
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This paper describes studies of two picornaviruses that bind to different regions of CD55. Antibodies to one of these regions enhance binding of virus to the other region, providing an example of interactions between SCR domains
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Johnsson, E.1
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44
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Role of the hypervariable region in streptococcal M proteins: Binding of a human complement inhibitor
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This paper reports that two streptococcal M proteins have a binding site for FHL-1 in the hypervariable region. This result extends previous findings that other M proteins use the hypervariable region to bind C4BP and suggests that binding of an RCA protein may be a general property of this region
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Johnsson E., Berggård K., Kotarsky H., Hellwage J., Zipfel P.F., Sjöbring U., Lindahl G. Role of the hypervariable region in streptococcal M proteins: binding of a human complement inhibitor. J Immunol. 161:1998;4894-4901. This paper reports that two streptococcal M proteins have a binding site for FHL-1 in the hypervariable region. This result extends previous findings that other M proteins use the hypervariable region to bind C4BP and suggests that binding of an RCA protein may be a general property of this region.
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Johnsson, E.1
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45
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Regulation of complement-mediated swine endothelial cell lysis by a surface-bound form of human C4b binding protein
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Mikata S., Miyagawa S., Iwata K., Nagasawa S., Hatanaka M., Matsumoto M., Kamiike W., Matsuda H., Shirakura R., Seya T. Regulation of complement-mediated swine endothelial cell lysis by a surface-bound form of human C4b binding protein. Transplantation. 65:1998;363-368.
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Mikata, S.1
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46
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Bordetella pertussis binds the human complement regulator C4BP: Role of filamentous hemagglutinin
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Berggård K., Johnsson E., Mooi F.R., Lindahl G. Bordetella pertussis binds the human complement regulator C4BP: role of filamentous hemagglutinin. Infect Immun. 65:1997;3638-3643.
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47
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Interactions between Neisseria gonorrhoeae and C4b-binding protein: A molecular basis for gonococcal serum resistance
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Ram S., Gulati S., McQuillen D.P., Boden R., Elkins C., Pangburn M.K., Rice P.A. Interactions between Neisseria gonorrhoeae and C4b-binding protein: a molecular basis for gonococcal serum resistance. Mol Immunol Abstr. 36:1999;297.
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48
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Identification of human complement factor H as a ligand for L-selectin
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The ability of FH to bind L-selectin throws new light on the function of this plasma protein and is of interest also to the study of microbial pathogenesis, since it suggests that FH-binding pathogens may exploit FH not only to escape complement attack but also to adhere to L-selectin-expressing cells
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Malhotra R., Ward M., Sim R.B., Bird M.I. Identification of human complement factor H as a ligand for L-selectin. Biochem J. 341:1999;61-69. The ability of FH to bind L-selectin throws new light on the function of this plasma protein and is of interest also to the study of microbial pathogenesis, since it suggests that FH-binding pathogens may exploit FH not only to escape complement attack but also to adhere to L-selectin-expressing cells.
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49
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50
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Identification of a domain in human factor H and factor H-like protein-1 required for the interaction with streptococcal M proteins
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Kotarsky H., Hellwage J., Johnsson E., Skerka C., Svensson H.G., Lindahl G., Sjöbring U., Zipfel P.F. Identification of a domain in human factor H and factor H-like protein-1 required for the interaction with streptococcal M proteins. J Immunol. 160:1998;3349-3354.
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Kotarsky, H.1
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Svensson, H.G.5
Lindahl, G.6
Sjöbring, U.7
Zipfel, P.F.8
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52
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M protein of the group A Streptococcus binds to the seventh short consensus repeat of human complement factor H
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Blackmore T.K., Fischetti V.A., Sadlon T.A., Ward H.M., Gordon D.L. M protein of the group A Streptococcus binds to the seventh short consensus repeat of human complement factor H. Infect Immun. 66:1998;1427-1431.
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53
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The human complement regulatory factor H-like protein-1, which represents a truncated form of factor H, displays cell-attachment activity
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Hellwage J., Kühn S., Zipfel P.F. The human complement regulatory factor H-like protein-1, which represents a truncated form of factor H, displays cell-attachment activity. Biochem J. 326:1997;321-327.
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A novel sialic acid binding site on factor H mediates serum resistance of sialylated Neisseria gonorrhoeae
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This paper provides the first clear evidence that binding of a fluid-phase complement inhibitor to a human pathogen protects against complement attack. In the interaction described here, a novel sialic acid binding site in the carboxy-terminal region of FH binds to sialylated lipo-oligosaccharide on the surface of N. gonorrhoeae, causing serum resistance
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Ram S., Sharma A.K., Simpson S.D., Gulati S., McQuillen D.P., Pangburn M.K., Rice P.A. A novel sialic acid binding site on factor H mediates serum resistance of sialylated Neisseria gonorrhoeae. J Exp Med. 187:1998;743-752. This paper provides the first clear evidence that binding of a fluid-phase complement inhibitor to a human pathogen protects against complement attack. In the interaction described here, a novel sialic acid binding site in the carboxy-terminal region of FH binds to sialylated lipo-oligosaccharide on the surface of N. gonorrhoeae, causing serum resistance.
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J Exp Med
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Ram, S.1
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Pangburn, M.K.6
Rice, P.A.7
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55
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Binding of complement factor H to loop 5 of porin protein 1A: A molecular mechanism of serum resistance of nonsialylated Neisseria gonorrhoeae
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Previous evidence that FH can protect N. gonorrhoeae against complement attack by binding to sialylated lipo-oligosaccharide is extended to nonsialylated strains. Interestingly, these strains bind FH to another surface structure, a porin protein.
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Ram S., McQuillen D.P., Gulati S., Elkins C., Pangburn M.K., Rice P.A. Binding of complement factor H to loop 5 of porin protein 1A: a molecular mechanism of serum resistance of nonsialylated Neisseria gonorrhoeae. J Exp Med. 188:1998;671-680. Previous evidence that FH can protect N. gonorrhoeae against complement attack by binding to sialylated lipo-oligosaccharide is extended to nonsialylated strains. Interestingly, these strains bind FH to another surface structure, a porin protein.
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Ram, S.1
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Rice, P.A.6
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56
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0032797582
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Resistance to both complement activation and phagocytosis in type 3 pneumococci is mediated by the binding of complement regulatory protein factor H
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Neeleman C., Geelen S.P.M., Aerts P.C., Daha M.R., Mollnes T.E., Roord J.J., Posthuma G., van Dijk H., Fleer A. Resistance to both complement activation and phagocytosis in type 3 pneumococci is mediated by the binding of complement regulatory protein factor H. Infect Immun. 67:1999;4517-4524.
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Fleer, A.9
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57
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0029059046
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Human complement proteins C3b, C4b, factor H and properdin react with specific sites in gp120 and gp41, the envelope proteins of HIV-1
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