Substitution of surface-exposed framework residues alters secretion of recombinant fusion protein Fv/tumor necrosis factor in Escherichia coli

IUBMB Life

Volumn 48, Issue 3, 1999, Pages 327-332

  Yang, Junbao ^a   Jia, Zongchao ^b   Xiang, Jim ^a,c  

^a UNIVERSITY OF SASKATCHEWAN   (Canada)

^b QUEEN S UNIVERSITY   (Canada)

^c Saskatoon Cancer Center   (Canada)

Author keywords

Amino acid substitution; Escherichia coli; Framework region; Fusion protein; Secretion; Surface residue

Indexed keywords

ANTIBODY; HYBRID PROTEIN; TUMOR NECROSIS FACTOR;

AMINO ACID SUBSTITUTION; ANTIBODY PRODUCTION; ANTIBODY STRUCTURE; ARTICLE; CONTROLLED STUDY; ESCHERICHIA COLI; NONHUMAN; PROTEIN SECRETION;

ESCHERICHIA COLI; IMMUNOGLOBULIN FRAGMENTS; IMMUNOGLOBULIN VARIABLE REGION; MUTATION; RECOMBINANT FUSION PROTEINS; TUMOR NECROSIS FACTOR-ALPHA;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0032754293     PISSN: 15216543     EISSN: None     Source Type: Journal    
DOI: 10.1080/152165499307053     Document Type: Article

References (25)

1. Winter, G., and Milstein, C. (1991) Man-made antibodies. Nature 349, 293-299.
2. Huston, J., George, A., Tai, M., McCartney, J., Jin, D., Swgal, D., Keck, P., and Oppermann, H. (1995) In Antibody Engineering (Borrebaeck, C., ed.). pp. 158-228, IRL Press, Oxford.
3. Pluckthun, A., Krebber, A., Krebber, C., Horn, U., Knupfer, U., Wenderoth, R., Nieba, L., Proba, K., and Riesenberg, D. (1996) In Antibody Engineering. A Practical Approach (McCafferty, J., ed.). pp. 203-252, IRL Press, Oxford.
4. Knappik. A., and Pluckthun, A. (1995) Engineering turns of a recombinant antibody improve its in vivo folding. Protein Eng. 8, 81-89.
5. Ulrich, H., Patten, P., Yang, P., Romesberg, F., and Schultz, P. (1995) Expression studies of catalytic antibodies. Proc. Natl. Acad. Sci. U.S.A. 92, 11907-11911.
6. Deng, S., Mackenzie, C., Sadowska, J., Michniewicz, J., Young, M., Bundle, D., and Narang, S. (1994) Selection of antibody single-chain variable fragments with improved carbohydrate binding by phage display. J. Biol. Chem. 269, 9533-9538.
7. Nieba, L., Honegger, A., Krebber, C., and Pluckthun, A. (1997) Disrupting the hydrophobic patches at the antibody variable/constant domain interface: improved in vivo folding and physical characterization of an engineered scFv fragment. Protein Eng. 10, 435-444.
8. Forsberg, G., Forsgren, M., Jali, M., Norin, M., Sterky, C., Enhorning, A., Larsson, K., Ericsson, M., and Bjork, P. (1997) Identification of framework residues in a secreted recombinant antibody fragment that control production level and localization in Escherichia coli. J. Biol. Chem. 272, 12430-12436.
9. Sambrook, J., Fritsch, E., and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
10. Yang, J., Moyana, T., and Xiang, J. (1995) A genetically engineered single-chain FV/TNF molecule possesses the anti-tumor immunoreactivity of FV as well as the cytotoxic activity of tumor necrosis factor. Mol. Immunol. 32, 873-881.
11. Harlow, E., and Lane, D. (1988) Antibodies. A Laboratory Manual, 1st ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
12. Brady, R., Edwards, D., Hubbard, R., Jiang, J., Lange, G., Roberts, S., and Todd, R. (1992) Crystal structure of a chimeric Fab' fragment of an antibody binding tumor cells. J. Mol. Biol. 227, 253-264.
13. Kabat, E., Wu, T., Reid-Miller, M., Perry, H., and Gottesman, K. (1991) Sequences of Proteins of Immunological Interest, 5th ed. Department of Health and Human Services, Washington, DC.
14. Wishart, D., and Willard, L. (1994) Volume angles define area. In Protein Engineering Network of Centers of Excellence, University of Alberta, Edmonton, Alberta, Canada.
15. Xiang, J., Moyana, T., Kalra, J., Hamilton, T., and Qi, Y. (1992) Construction and characterization of a high-affinity chimeric anti-colorectal carcinoma antibody ccM4. Mol. Biother. 4, 174-181.
16. Sarkar, G., and Sommer, S. (1990) The "megaprimer" method of site-directed mutagenesis. Biotechnology 8, 404-407.
17. Yang, J., Moyana, T., Mackenzie, S., Xia, Q., and Xiang, J. (1998) One hundred seventy-fold increase in excretion of an FV fragment-tumor necrosis factor alpha fusion protein (sFV/TNF-alpha) from Escherichia coli caused by the synergistic effects of glycine and Triton X-100. Appl. Environ. Microbiol. 64, 2869-2874.
18. Pedersen, J., Henry, A., Searle, S., Guild, B., Roguska, M., and Rees, A. (1994) Comparison of surface accessible residues in human and murine immunoglobulin Fv domains. Implication for humanization of murine antibodies. J. Mol. Biol. 235, 959-973.
19. Sweet, R., and Eisenberg, D. (1983) Correlation of sequence hydrophobicities measures similarity in three dimensional protein structure. J. Mol. Biol. 171, 479-488.
20. Freund, C., Honegger, A., Hunziker, P., Holak, T., and Pluckthun, A. (1996) Folding nuclei of the scFv fragment of an antibody. Biochemistry 35, 8457-8464.
21. Sanger, F., Nicklen, S., and Coulson, A. (1977) DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. U.S.A. 74, 5463-5467.
22. Knappik, A., Krebber, C., and Pluckthun, A. (1993) The effect of folding catalysts on the in vivo folding process of different antibody fragments expressed in Escherichia coli. BioTechnology 11, 77-83.
23. Skerra, A., and Pluckthun, A. (1991) Secretion and in vivo folding of the Fab fragment of the antibody McPC603 in Escherichia coli: influence of disulphides and cis-prolines. Protein Eng. 4, 971-979.
24. Duenas, M., Ayala, M., Vazquez, J., Ohlin, M., Soderlind, E., Borrebaeck, C., and Gavilondo, J. (1995) A point mutation in a murine immunoglobulin V-region strongly influences the antibody yield in Escherichia coli. Gene 158, 61-66.
25. Leistler, B., and Perham, R. (1994) Solubilizing buried domains of proteins: a self-assembling interface domain from glutathione reductase. Biochemistry 33, 2773-2781.