Three-dimensional structures of single-chain Fv-neuraminidase complexes

Journal of Molecular Biology

Volumn 279, Issue 4, 1998, Pages 901-910

  Malby, Robyn L ^a,b   McCoy, Airlie J ^a,c   Kortt, Alexander A ^a   Hudson, Peter J ^a   Colman, Peter M ^a  

^a CSIRO   (Australia)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c MEDICAL RESEARCH COUNCIL   (United Kingdom)

Author keywords

Antibody domain; Antigen antibody complex; Recombinant DNA; X ray crystallography

Indexed keywords

ANTIBODY; RECOMBINANT PROTEIN; SIALIDASE;

ANTIGEN ANTIBODY COMPLEX; ARTICLE; BINDING SITE; IMMUNOGLOBULIN VARIABLE REGION; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN DOMAIN; STOICHIOMETRY;

INFLUENZA VIRUS;

EID: 0032546756     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1794     Document Type: Article

References (44)

1. Air, G. M., Webster, R. G., Colman, P. M., & Laver, W. G. (1987). Distribution of sequence differences in influenza N9 neuraminidase of tern and whale viruses and crystallization of the whale neuraminidase complexed with antibodies. Virology, 160, 346-354.
2. Atwell, J. L., Pearce, L. A., Lah, M., Gruen, L. C., Kortt, A. A. & Hudson, P. J. (1996). Design and expression of a stable bispecific scFv dimer with affinity for both glycophorin and N9 neuraminidase. Mol. Immunol. 33, 1301-1312.
3. Bacon, D. & Anderson, W. F. (1989). A fast algorithm for rendering space filling molecule pictures. J. Mol. Graphics, 6, 219-220.
4. Brünger, A. T. (1992). X-PLOR Reference Manual Version 3.0, Molecular Simulations Inc., Waltham, MA.
5. Colman, P. M. (1988). Structure of antibody-antigen complexes: implications for immune recognition. Advan. Immunol. 43, 99-132.
6. Desplancq, D., King, D. J., Lawson, A. D. G. & Mountain, A. (1994). Multimerisation behaviour of single chain Fv variants for the tumour binding antibody B72.3. Protein Eng. 7, 1027-1033.
7. Freund, C., Ross, A., Pluckthun, A. & Holak, T. A. (1994). Structural and dynamic properties of the Fv fragment and the single-chain Fv fragment of an antibody in solution investigated by heteronuclear three-dimensional NMR spectroscopy. Biochemistry, 33, 3296-3303.
8. Griffiths, A. D., Malmquist, M., Marks, J. D., Bye, J. M., Embleton, M. J., McCafferty, J., Baier, M., Holliger, K. P., Gorik, B. D., Hughes-Jones, N. C., Hoogenboom, H. R. & Winter, G. (1993). Human anti-self antibodies with high specificity from phage display. EMBO J. 12, 725-734.
9. Higashi, T. (1989). The processing of diffraction data taken on a screenless Weissenberg camera for macromolecular crystallography. J. Appl. Crystallog. 22, 9-18.
10. Holliger, P., Prospero, T. & Winter, G. (1993). "Diabodies": small bivalent and bispecfic antibody fragments. Proc. Natl Acad. Sci. USA, 90, 6444-6448.
11. Holliger, P., Brissinck, J., Williams, R. L., Thielemans, K. & Winter, G. (1996). Specific killing of lymphoma cells by cytotoxic T-cells mediated by a bispecific diabody. Prot. Eng. 9, 299-305.
12. Hopp, T. P., Prickett, K. S., Price, V. L., Libby, R. T., March, C. J., Cerretti, D. P., Urdal, D. L. & Conlon, P. J. (1988). A short polypeptide marker sequence useful for recombinant protein identification and purification. Bio/Technology, 6, 1204-1210.
13. Hudson, P. (1995). Structure and application of single-chain Fvs as diagnostic and therapeutic agents. In Monoclonal Antibodies: The Second Generation. (Zola, H., ed.), pp. 183-202, BIOS Scientific Publications, Oxford, UK.
14. Huston, J. S., Mudgett-Hunter, M., Tai, M.-S., McCartney, J. E., Warren, F. D., Haber, E. & Oppermann, H. (1991). Protein engineering of single chain Fv analogs and fusion proteins. Methods Enzymol. 203, 46-88.
15. Jones, T. A., Zou, J-Y., Cowan, S. W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A, 47, 110-119.
16. Kishan, K. V. R., Zeelan, J. P., Noble, M. E. M., Borchert, T. V. & Wierenga, R. K. (1994). Comparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms. Protein Sci. 3, 779-787.
17. Kortt, A. A., Malby, R. L., Caldwell, J. B., Gruen, L. C., Ivancic, N., Lawrence, M. C., Howlett, G. J., Webster, R. G., Hudson, P. J. & Colman, P. M. (1994). Recombinant anti-sialidase single chain Fv antibody: characterization, formation of dimer and higher molecule mass multimers and the solution of the crystal structure of the scFv-sialidase complex. Eur. J. Biochem. 221, 151-157.
18. Kortt, A. A., Lah, M., Oddie, G. W., Gruen, L. C., Burns, J. E., Pearce, L. A., Atwell, J. L., McCoy, A. J., Howlett, G. J., Metzger, D. W., Webster, R. G. & Hudson, P. J. (1997). Single chain Fv fragments of anti-neuraminidase antibody NC10 containing five and ten residue linkers form dimers and with zero residue linker a trimer. Protein Eng. 10, 423-433.
19. Kraulis, P. J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
20. Laver, W. G., Webster, R. G. & Colman, P. M. (1986). Crystals of antibodies complexed with influenza virus neuraminidase show isosteric binding of antibody to wild-type and variant antigens. Virology, 156, 181-184.
21. Luzzati, V. (1952). Treatment of statistical errors in the determination of crystal structures. Acta Crystallog. 5, 802-810.
22. Malby, R. L., Caldwell, J. B., Gruen, L. C., Harley, V. R., Ivancic, N., Kortt, A. A., Lilley, g. G., Power, B. E., Webster, R. G., Colman, P. M. & Hudson, P. J. (1993). Recombinant antineuraminidase single chain antibody: expression, characterization, and crystallization in complex with antigen. Proteins: struct. Funct. Genet. 16, 57-63.
23. Malby, R. L., Tulip, W. R., Harley, V. R., McKimm-Breschin, J. L., Laver, W. G., Webster, R. G. & Colman, P. M. (1994). The structure of a complex between the NC10 antibody and the influenza virus neuraminidase and comparison with the overlapping binding site of the NC41 antibody. Structure, 2, 733-746.
24. Matthews, B. W. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
25. 2 made by protein folding and bonded through C-terminal cysteinyl peptides. Protein Eng. 8, 301-314.
26. McKimm-Breschkin, J. L., Caldwell, J. B., Guthrie, R. E. & Kortt, A. A. (1991). A new method for the purification of influenza A virus neuraminidase. J. Virol. Methods, 32, 121-124.
27. Merritt, E. A. & Murphy, M. E. P. (1994). RASTER3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallog. sect. D, 50, 869-873.
28. Neri, D., Momo, M., Prospero, T. & Winter, G. (1995). High-affinity antigen binding by chelating recombinant antibodies. J. Mol. Biol. 246, 367-373.
29. Pack, P., Muller, K., Zahn, P. & Plückthun, A. (1995). Tetravalent minibodies with high avidity assembling in E. coli J. Mol. Biol. 246, 28-34.
30. Perisic, O., Webb, P. A., Holliger, P., Winter, G. & Williams, R. L. (1994). Crystal structure of a diabody, a bivalent antibody fragment. Structure, 2, 1217-1226.
31. Ramachandran, G. N. & Sasisekharan, V. (1968). Conformation of polypeptides and proteins. Advan. Protein Chem. 23, 283-437.
32. Rossmann, M. G. (1972). The Molecular Replacement Method, Gordon & Breach, New York.
33. Sakabe, N. (1991). X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation. Nucl. Instr. Meth. Phys. Res. A, 303, 448-463.
34. Stanfield, R. L. & Wilson, I. A. (1994). Antigen-induced conformational changes in antibodies. Trends Biotechnol. 12, 275-279.
35. Steigemann, W. (1974). The development and use of computational methods and programs for structure analysis of proteins using as examples the trypsin-trypsin inhibitor complex, the free inhibitor and L-asparaginase. PhD thesis, Technical University, Munich, Germany.
36. Tulip, W. R., Varghese, J. N., Baker, A. T., van Donkelaar, A., Laver, W. G., Webster, R. G. & Colman, P. M. (1991). Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants. J. Mol. Biol. 221, 487-497.
37. Tulip, W. R., Varghese, J. N., Laver, W. G., Webster, R. G. & Colman, P. M. (1992). Refined crystal structure of the influenza virus N9 neuraminidse-NC41 Fab complex. J. Mol. Biol. 227, 122-148.
38. Varghese, J. N. & Colman, P. M. (1991). Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 Å resolution. J. Mol. Biol. 221, 473-486.
39. Varghese, J. N., Laver, W. G. & Colman, P. M. (1983). Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution. Nature, 303, 35-40.
40. Webster, R. G., Air, G. M., Metzger, D. W., Colman, P. M., Varghese, J. N., Baker, A. T. & Laver, W. G. (1987). Antigenic structure and variation in an influenza virus N9 neuraminidase. J. Virol. 61, 2910-2916.
41. Whitlow, M., Filpula, D., Rollence, M. L., Feng, S.-L. & Woods, J. F. (1994). Multivalent Fvs: characterisation of single-chain Fv oligomers and preparation of a bispecific Fv. Protein Eng. 7, 1017-1026.
42. Zdanov, A., Li, Y., Bundle, D. R., Deng, S-J., MacKenzie, C. R., Narang, S. A., Young, N. M. & Cygler, M. (1994). Structure of a single-chain antibody variable domain (Fv) fragment complexed with a carbohydrate antigen at 1.7 Å resolution. Proc. Natl Acad. Sci. USA, 91, 6423-6427.
43. Zhang, X-J., Wozniak, J. A. & Matthews, B. W. (1995). Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme. J. Mol. Biol. 250, 527-552.
44. Zhu, Z., Zapata, G., Shalaby, R., Snedecor, B., Chen, H. & Carter, P. (1996). High level secretion of a humanised bispecific diabody from E. coli. Biotechnology, 14, 192-196.