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Volumn 20, Issue 1, 1998, Pages 69-78

All individual domains of staphylococcal protein A show Fab binding

Author keywords

Fab fragment; Immunoglobulin; Interaction; Protein A; Surface plasmon resonance

Indexed keywords

IMMUNOGLOBULIN F(AB) FRAGMENT; STAPHYLOCOCCUS PROTEIN A;

EID: 0031884383     PISSN: 09288244     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0928-8244(97)00108-9     Document Type: Article
Times cited : (148)

References (43)
  • 1
    • 0020011459 scopus 로고
    • Protein A of Staphylococcus aureus and related immunoglobulin receptors produced by streptococci and pneumococci
    • Dixon, F.J. and Kuhnel, H.G., Eds. Academic Press, New York
    • Langone, J.J. (1982) Protein A of Staphylococcus aureus and related immunoglobulin receptors produced by streptococci and pneumococci. In: Advances in Immunology (Dixon, F.J. and Kuhnel, H.G., Eds.), Vol. 32, pp. 157-252. Academic Press, New York.
    • (1982) Advances in Immunology , vol.32 , pp. 157-252
    • Langone, J.J.1
  • 2
    • 0025362617 scopus 로고
    • Fusions to staphylococcal protein A
    • Nilsson, B. and Abrahmsén, L. (1990) Fusions to staphylococcal protein A. Methods Enzymol. 185, 144-161.
    • (1990) Methods Enzymol. , vol.185 , pp. 144-161
    • Nilsson, B.1    Abrahmsén, L.2
  • 4
    • 0031045390 scopus 로고    scopus 로고
    • The use of gene fusions to protein A and protein G in immunology and biotechnology
    • Ståhl, S. and Nygren, P.-Å. (1997) The use of gene fusions to protein A and protein G in immunology and biotechnology. Pathol. Biol. 45, 66-76.
    • (1997) Pathol. Biol. , vol.45 , pp. 66-76
    • Ståhl, S.1    Nygren, P.-Å.2
  • 7
    • 0019493843 scopus 로고
    • 2 epsilon protein A interactions
    • 2 epsilon protein A interactions. Scand. J. Immunol. 13, 343-352.
    • (1981) Scand. J. Immunol. , vol.13 , pp. 343-352
    • Inganäs, M.1
  • 8
    • 0027424299 scopus 로고
    • Immunoglobulin binding specificities of the homology regions (domains) of protein A
    • Ibrahim, S. (1993) Immunoglobulin binding specificities of the homology regions (domains) of protein A. Scand. J. Immunol. 38, 368-374.
    • (1993) Scand. J. Immunol. , vol.38 , pp. 368-374
    • Ibrahim, S.1
  • 9
    • 0028980073 scopus 로고
    • H3 family antibodies bind domain D of staphylococcal protein A
    • H3 family antibodies bind domain D of staphylococcal protein A. J. Immunol. 154, 6437-6445.
    • (1995) J. Immunol. , vol.154 , pp. 6437-6445
    • Roben, P.W.1    Salem, A.N.2    Silverman, G.J.3
  • 11
    • 0025876152 scopus 로고
    • Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system
    • Karlsson, R., Michaelsson, A. and Mattsson, L. (1991) Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system. J. Immunol. Methods 145, 229-240.
    • (1991) J. Immunol. Methods , vol.145 , pp. 229-240
    • Karlsson, R.1    Michaelsson, A.2    Mattsson, L.3
  • 13
    • 0022435191 scopus 로고
    • Analysis of the signals for secretion in the staphylococcal protein A gene
    • Abrahmsén, L., Moks, T., Nilsson, B., Hellman, U. and Uhlén, M. (1985) Analysis of the signals for secretion in the staphylococcal protein A gene. EMBO J. 4, 3901-3906.
    • (1985) EMBO J. , vol.4 , pp. 3901-3906
    • Abrahmsén, L.1    Moks, T.2    Nilsson, B.3    Hellman, U.4    Uhlén, M.5
  • 14
    • 0024835779 scopus 로고
    • Thiol-directed immobilization of recombinant IgG-binding receptors
    • Ljungquist, C., Jansson, B., Moks, T. and Uhlén, M. (1989) Thiol-directed immobilization of recombinant IgG-binding receptors. Eur. J. Biochem. 186, 557-561.
    • (1989) Eur. J. Biochem. , vol.186 , pp. 557-561
    • Ljungquist, C.1    Jansson, B.2    Moks, T.3    Uhlén, M.4
  • 15
    • 0025741617 scopus 로고
    • Structural and functional analysis of the human IgG-Fab receptor activity of streptococcal protein G
    • Eliasson, M., Andersson, R., Nygren, P.-Å. and Uhlén, M. (1990) Structural and functional analysis of the human IgG-Fab receptor activity of streptococcal protein G. Mol. Immunol. 28, 1055-1061.
    • (1990) Mol. Immunol. , vol.28 , pp. 1055-1061
    • Eliasson, M.1    Andersson, R.2    Nygren, P.-Å.3    Uhlén, M.4
  • 17
    • 0020480638 scopus 로고
    • pUR 250 allows rapid chemical sequencing of both DNA strands of inserts
    • Rüther, U. (1982) pUR 250 allows rapid chemical sequencing of both DNA strands of inserts. Nucleic Acids Res. 10, 5765-5772.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 5765-5772
    • Rüther, U.1
  • 18
    • 0026099079 scopus 로고
    • Bidirectional solid-phase sequencing of in vitro-amplified plasmid DNA
    • Hultman, T., Bergh, S., Moks, T. and Uhlén, M. (1991) Bidirectional solid-phase sequencing of in vitro-amplified plasmid DNA. Biotechniques 10, 84-93.
    • (1991) Biotechniques , vol.10 , pp. 84-93
    • Hultman, T.1    Bergh, S.2    Moks, T.3    Uhlén, M.4
  • 21
    • 0028006072 scopus 로고
    • Antibody fragments from a 'single pot' phage display library as immunochemical reagents
    • Nissim, A., Hoogenboom, H.R., Tomlinson, I.M., Flynn, G., Midgley, C., Lane, D. and Winter, G. (1994) Antibody fragments from a 'single pot' phage display library as immunochemical reagents. EMBO J. 13, 692-698.
    • (1994) EMBO J. , vol.13 , pp. 692-698
    • Nissim, A.1    Hoogenboom, H.R.2    Tomlinson, I.M.3    Flynn, G.4    Midgley, C.5    Lane, D.6    Winter, G.7
  • 22
    • 0025740577 scopus 로고
    • Multi-subunit proteins on the surface of filamentous phage: Methodologies for displaying antibody (Fab) heavy and light chains
    • Hoogenboom, H.R., Griffiths, A.D., Johnson, K.S., Chiswell, D.J., Hudson, P. and Winter, G. (1991) Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains. Nucleic Acids Res. 19, 4133-4137.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4133-4137
    • Hoogenboom, H.R.1    Griffiths, A.D.2    Johnson, K.S.3    Chiswell, D.J.4    Hudson, P.5    Winter, G.6
  • 24
    • 0023384982 scopus 로고
    • Engineering enzyme specificity by 'substrate-assisted catalysis'
    • Carter, P. and Wells, J.A. (1987) Engineering enzyme specificity by 'substrate-assisted catalysis'. Science 237, 394-399.
    • (1987) Science , vol.237 , pp. 394-399
    • Carter, P.1    Wells, J.A.2
  • 26
    • 0023974826 scopus 로고
    • An Escherichia coli mutation preventing degradation of abnormal proteins
    • Strauch, K.L. and Beckwith, J. (1988) An Escherichia coli mutation preventing degradation of abnormal proteins. Proc. Natl. Acad. Sci. USA 85, 1576-1580.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1576-1580
    • Strauch, K.L.1    Beckwith, J.2
  • 29
    • 0030043942 scopus 로고    scopus 로고
    • The mechanism of binding staphylococcal protein A to immunoglobulin G does not involve helix unwinding
    • Jendeberg, L., Tashiro, M., Tejero, R., Lyons, B.A., Uhlén, M., Montelione, G.T. and Nilsson, B. (1996) The mechanism of binding staphylococcal protein A to immunoglobulin G does not involve helix unwinding. Biochemistry 35, 22-31.
    • (1996) Biochemistry , vol.35 , pp. 22-31
    • Jendeberg, L.1    Tashiro, M.2    Tejero, R.3    Lyons, B.A.4    Uhlén, M.5    Montelione, G.T.6    Nilsson, B.7
  • 31
    • 0030042286 scopus 로고    scopus 로고
    • The serum-albumin binding domain of streptococcal protein G is a three-helical bundle: A heteronuclear NMR study
    • Kraulis, P.J., Jonasson, P., Nygren, P.-Å., Uhlén, M., Jendeberg, L., Nilsson, B. and Kördel, J. (1996) The serum-albumin binding domain of streptococcal protein G is a three-helical bundle: a heteronuclear NMR study. FEBS Lett. 378, 190-194.
    • (1996) FEBS Lett. , vol.378 , pp. 190-194
    • Kraulis, P.J.1    Jonasson, P.2    Nygren, P.-Å.3    Uhlén, M.4    Jendeberg, L.5    Nilsson, B.6    Kördel, J.7
  • 34
    • 0022413165 scopus 로고
    • H-associated reactivity of a monoclonal human IgM
    • H-associated reactivity of a monoclonal human IgM. J. Immunol. 135, 1232-1238.
    • (1985) J. Immunol. , vol.135 , pp. 1232-1238
    • Vidal, M.A.1    Conde, F.P.2
  • 35
    • 0029330511 scopus 로고
    • Kinetic analysis of the interaction between protein A domain variants and human Fc using plasmon resonance detection
    • Jendeberg, L., Persson, B. Andersson, R., Karlsson, R, Uhlén, M. and Nilsson, B. (1995) Kinetic analysis of the interaction between protein A domain variants and human Fc using plasmon resonance detection. J. Mol. Recogn. 8, 270-278.
    • (1995) J. Mol. Recogn. , vol.8 , pp. 270-278
    • Jendeberg, L.1    Persson, B.2    Andersson, R.3    Karlsson, R.4    Uhlén, M.5    Nilsson, B.6
  • 41
    • 0019969349 scopus 로고
    • Demonstration on protein A of two distinct immunoglobulin-binding sites and their role in the mitogenic activity of Staphylococcus aureus Cowan I on human B cells
    • Romagnani, S., Giudizi, M.G., del Prete, G., Maggi, E., Biagiotti, R., Almerigogna, F. and Ricci, M. (1982) Demonstration on protein A of two distinct immunoglobulin-binding sites and their role in the mitogenic activity of Staphylococcus aureus Cowan I on human B cells. J. Immunol 129, 596-602.
    • (1982) J. Immunol , vol.129 , pp. 596-602
    • Romagnani, S.1    Giudizi, M.G.2    Del Prete, G.3    Maggi, E.4    Biagiotti, R.5    Almerigogna, F.6    Ricci, M.7
  • 42
    • 0029131806 scopus 로고
    • Structures of bacterial immunoglobulin-binding domains and their complexes with immunoglobulins
    • Tashiro, M. and Montelione, G.T. (1995) Structures of bacterial immunoglobulin-binding domains and their complexes with immunoglobulins. Curr. Opin. Struct. Biol. 5, 471-481.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 471-481
    • Tashiro, M.1    Montelione, G.T.2
  • 43
    • 0025196843 scopus 로고
    • 1H NMR assignments and secondary structure of the B domain of staphylococcal protein A: Structural changes between the free B domain in solution and the Fc-bound B domain in crystal
    • 1H NMR assignments and secondary structure of the B domain of staphylococcal protein A: Structural changes between the free B domain in solution and the Fc-bound B domain in crystal. Biochemistry 29, 8787-8793.
    • (1990) Biochemistry , vol.29 , pp. 8787-8793
    • Torigoe, H.1    Shimada, I.2    Saito, A.3    Sato, M.4    Arata, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.