Potent inhibition of huntingtin aggregation and cytotoxicity by a disulfide bond-free single-domain intracellular antibody

Proceedings of the National Academy of Sciences of the United States of America

Volumn 101, Issue 51, 2004, Pages 17616-17621

  Colby, David W ^a   Chu, YiJia ^b   Cassady, John P ^b   Duennwald, Martin ^c   Zazulak, Helen ^c   Webster, Jack M ^d   Messer, Anne ^d,e   Lindquist, Susan ^c   Ingram, Vernon Martin ^b   Wittrup, K Dane ^a,b  

^a Massachusetts Institute of Technology   (United States)

^b MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^c WHITEHEAD INSTITUTE FOR BIOMEDICAL RESEARCH   (United States)

^d WADSWORTH CENTER   (United States)

^e STATE UNIVERSITY OF NEW YORK   (United States)

Author keywords

Directed evolution; Huntington's disease; Neurodegeneration; Protein engineering; Yeast surface display

Indexed keywords

ANTIBODY; CELL PROTEIN; HUNTINGTIN; HUNTINGTIN ANTIBODY; UNCLASSIFIED DRUG;

ANIMAL CELL; ANTIBODY AFFINITY; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; CYTOTOXICITY; DISULFIDE BOND; DRUG CYTOTOXICITY; DRUG EFFECT; DRUG POTENCY; DRUG TARGETING; HUMAN; HUMAN CELL; HUNTINGTON CHOREA; NERVE CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DOMAIN; PROTEIN ENGINEERING; PROTEIN EXPRESSION; SACCHAROMYCES CEREVISIAE;

ANIMALS; ANTIBODIES; ANTIBODY AFFINITY; CELL LINE; DIRECTED MOLECULAR EVOLUTION; DISULFIDES; HUMANS; HUNTINGTON DISEASE; MODELS, MOLECULAR; MUTATION; NERVE TISSUE PROTEINS; NUCLEAR PROTEINS; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN STRUCTURE, QUATERNARY; SACCHAROMYCES CEREVISIAE;

ANIMALIA; SACCHAROMYCES CEREVISIAE;

EID: 19944395483     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0408134101     Document Type: Article

References (39)

1. Colby, D. W., Garg, P., Holden, T., Chao, G., Webster, J. M., Messer, A., Ingram, V. M. & Wittrup, K. D. (2004) J. Mol. Biol. 342, 901-912.
2. Khoshnan, A., Ko, J. & Patterson, P. H. (2002) Proc. Natl. Acad. Sci. USA 99, 1002-1007.
3. Lecerf, J. M., Shirley, T. L., Zhu, Q., Kazantsev, A., Amersdorfer, P., Housman, D. E., Messer, A. & Huston, J. S. (2001) Proc. Natl. Acad. Sci. USA 98, 4764-4769.
4. Murphy, R. C. & Messer, A. (2004) Brain Res. Mol. Brain Res. 121, 141-145.
5. Visintin, M., Tse, E., Axelson, H., Rabbitts, T. H. & Cattaneo, A. (1999) Proc. Natl. Acad. Sci. USA 96, 11723-11728.
6. Emadi, S., Liu, R., Yuan, B., Schulz, P., McAllister, C., Lyubchenko, Y., Messer, A. & Sierks, M. R. (2004) Biochemistry 43, 2871-2878.
7. Gennari, F., Mehta, S., Wang, Y., St. Clair Tallarico, A., Palu, G. & Marasco, W. A. (2004) J. Mol. Biol. 335, 193-207.
8. Proba, K., Worn, A., Honegger, A. & Pluckthun, A. (1998) J. Mol. Biol. 275, 245-253.
9. Rajpal, A. & Turi, T. G. (2001) J. Biol. Chem. 276, 33139-33146.
10. Arafat, W., Gomez-Navarro, J., Xiang, J., Siegal, G. P., Alvarez, R. D. & Curiel, D. T. (2000) Cancer Gene Ther. 7, 1250-1256.
11. Zhu, Q., Zeng, C., Huhalov, A., Yao, J., Turi, T. G., Danley, D., Hynes, T., Cong, Y., DiMattia, D., Kennedy, S., et al. (1999) J. Immunol. Methods 231, 207-222.
12. Boder, E. T. & Wittrup, K. D. (1997) Nat. Biotechnol. 15, 553-557.
13. Feldhaus, M. J., Siegel, R. W., Opresko, L. K., Coleman, J. R., Feldhaus, J. M., Yeung, Y. A., Cochran, J. R., Heinzelman, P., Colby, D., Swers, J., et al. (2003) Nat. Biotechnol. 21, 163-170.
14. Colby, D. W., Kellogg, B. A., Graff, C. P., Yeung, Y. A., Swers, J. S. & Wittrup, K. D. (2004) Methods Enzymol. 388, 348-358.
15. Graff, C. P., Chester, K., Begent, R. & Wittrup, K. D. (2004) Protein Eng. Des. Sel. 17, 293-304.
16. Rao, B. M., Girvin, A. T., Ciardelli, T., Lauffenburger, D. A. & Wittrup, K. D. (2003) Protein Eng. 16, 1081-1087.
17. Boder, E. T., Midelfort, K. S. & Wittrup, K. D. (2000) Proc. Natl. Acad. Sci. USA 97, 10701-10705.
18. Cochran, J. R., Kim, Y. S., Olsen, M. J., Bhandari, R. & Wittrup, K. D. (2004) J. Immunol. Methods 287, 147-158.
19. Orr, B. A., Carr, L. M., Wittrup, K. D., Roy, E. J. & Kranz, D. M. (2003) Biotechnol. Progr. 19, 631-638.
20. Shusta, E. V., Kieke, M. C., Parke, E., Kranz, D. M. & Wittrup, K. D. (1999) J. Mol. Biol. 292, 949-956.
21. Boder, E. T. & Wittrup, K. D. (2000) Methods Enzymol. 328, 430-444.
22. Raymond, C. K., Pownder, T. A. & Sexson, S. L. (1999) BioTechniques 26, 134-138, 140-141.
23. Cattaneo, E. & Conti, L. (1998) J. Neurosci. Res. 53, 223-234.
24. Webster, J. M., Tiwari, S., Weissman, A. M. & Wojcikiewicz, R. J. (2003) J. Biol. Chem. 278, 38238-38246.
25. Sherman, F. (1991) Methods Enzymol. 194, 3-21.
26. Ito, H., Fukuda, Y., Murata, K. & Kimura, A. (1983) J. Bacteriol. 153, 163-168.
27. Sikorski, R. S. & Hieter, P. (1989) Genetics 122, 19-27.
28. Muchowski, P. J., Schaffar, G., Sittler, A., Wanker, E. E., Hayer-Hartl, M. K. & Hartl, F. U. (2000) Proc. Natl. Acad. Sci. USA 97, 7841-7846.
29. Choo, Y. S., Johnson, G. V., MacDonald, M., Detloff, P. J. & Lesort, M. (2004) Hum. Mol. Genet. 13, 1407-1420.
30. Leenders, K. L., Frackowiak, R. S., Quinn, N. & Marsden, C. D. (1986) Movement Disorders 1, 69-77.
31. Mosmann, T. (1983) J. Immunol. Methods 65, 55-63.
32. Krobitsch, S. & Lindquist, S. (2000) Proc. Natl. Acad. Sci. USA 97, 1589-1594.
33. Meriin, A. B., Zhang, X., He, X., Newnam, G. P., Chernoff, Y. O. & Sherman, M. Y. (2002) J. Cell Biol. 157, 997-1004.
34. Schaffar, G., Breuer, P., Boteva, R., Behrends, C., Tzvetkov, N., Strippel, N., Sakahira, H., Siegers, K., Hayer-Hartl, M. & Hartl, F. U. (2004) Mol. Cell 15, 95-105.
35. Cumming, R. C., Andon, N. L., Haynes, P. A., Park, M., Fischer, W. H. & Schubert, D. (2004) J. Biol. Chem. 279, 21749-21758.
36. Ramm, K., Gehrig, P. & Pluckthun, A. (1999) J. Mol. Biol. 290, 535-546.
37. Holt, L. J., Herring, C., Jespers, L. S., Woolven, B. P. & Tomlinson, I. M. (2003) Trends Biotechnol. 21, 484-490.
38. Xu, L., Aha, P., Gu, K., Kuimelis, R. G., Kurz, M., Lam, T., Lim, A. C., Liu, H., Lohse, P. A., Sun, L., et al. (2002) Chem. Biol. 9, 933-942.
39. Zhou, C., Emadi, S., Sierks, M. R. & Messer, A. (2004) Mol. Ther. 10, 1023-1031.