Toward reducing immunogenicity of enzyme replacement therapy: Altering the specificity of human β-glucuronidase to compensate for α-iduronidase deficiency

Protein Engineering, Design and Selection

Volumn 28, Issue 11, 2015, Pages 519-529

  Chuang, Huai Yao ^a,b   Suen, Ching Shu ^b   Hwang, Ming Jing ^b   Roffler, Steve R ^a,b  

^a NATIONAL DEFENSE MEDICAL CENTER   (Taiwan)

^b INSTITUTE OF BIOMEDICAL SCIENCES   (Taiwan)

Author keywords

Enzyme replacement therapy; Mucopolysaccharidosis (MPS); Protein evolution; iduronidase; glucuronidase

Indexed keywords

METABOLISM; PATIENT TREATMENT;

BETA-GLUCURONIDASE; ENZYME REPLACEMENT THERAPY; GLUCURONIDASE; LYSOSOMAL STORAGE DISORDER; MUCOPOLYSACCHARIDOSIS (MPS); PROTEIN EVOLUTION; THERAPEUTIC BENEFITS; THERAPEUTIC EFFICACY;

ENZYMES;

BETA GLUCURONIDASE; LEVO IDURONIDASE;

ALPHA IDURONIDASE DEFICIENCY; AMINO ACID SEQUENCE; ANTIBODY RESPONSE; ARTICLE; DNA CONTAMINATION; EMBRYO; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME RELEASE; ENZYME REPLACEMENT; ENZYME SPECIFICITY; HEK293 CELL LINE; HUMAN; HUMAN CELL; IMMUNOGENICITY; IN VITRO STUDY; PHENOTYPE; PRIORITY JOURNAL; ADVERSE EFFECTS; CHEMICAL STRUCTURE; CHEMISTRY; DEFICIENCY; GENETICS; IMMUNOLOGY; METABOLISM; MUCOPOLYSACCHARIDOSIS; PROCEDURES; PROTEIN ENGINEERING;

AMINO ACID SEQUENCE; ENZYME REPLACEMENT THERAPY; GLUCURONIDASE; HEK293 CELLS; HUMANS; IDURONIDASE; MODELS, MOLECULAR; MUCOPOLYSACCHARIDOSES; PROTEIN ENGINEERING;

EID: 84948407175     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzv041     Document Type: Article

References (55)

1. Amalfitano, A., Bengur, A.R., Morse, R.P., et al. (2001) Genet. Med., 3, 132-138.
2. Banugaria, S.G., Patel, T.T., Mackey, J., Das, S., Amalfitano, A., Rosenberg, A.S., Charrow, J., Chen, Y.T. and Kishnani, P.S. (2012) Mol. Genet. Metab., 105, 677-680.
3. Banugaria, S.G., Prater, S.N., Patel, T.T., et al. (2013) PLoS ONE, 8, e67052.
4. Cantor, J.R., Yoo, T.H., Dixit, A., Iverson, B.L., Forsthuber, T.G. and Georgiou, G. (2011) Proc. Natl Acad. Sci. U.S.A., 108, 1272-1277.
5. Caras, I.W., Weddell, G.N., Davitz, M.A., Nussenzweig, V. and Martin, D.W., Jr. (1987) Science, 238, 1280-1283.
6. Carreno, B.M., Magrini, V., Becker-Hapak, M., et al. (2015) Science, 348, 803-808.
7. Chen, K.C., Cheng, T.L., Leu, Y.L., Prijovich, Z.M., Chuang, C.H., Chen, B.M. and Roffler, S.R. (2007) Cancer Gene Ther., 14, 187-200.
8. Chen, K.C., Wu, C.H., Chang, C.Y., et al. (2008) Chem. Biol., 15, 1277-1286.
9. Chen, C.P., Hsieh, Y.T., Prijovich, Z.M., et al. (2012) Protein Eng. Des. Sel., 25, 367-375.
10. Choi, Y., Griswold, K.E. and Bailey-Kellogg, C. (2013) J. Computat. Chem., 34, 879-891.
11. De Duve, C. and Wattiaux, R. (1966) Annu. Rev. Physiol., 28, 435-492.
12. Dickson, P., Peinovich, M., McEntee, M., et al. (2008) J. Clin. Invest., 118, 2868-2876.
13. Di Domenico, C., Villani, G.R., Di Napoli, D., Reyero, E.G., Lombardo, A., Naldini, L. and Di Natale, P. (2005) Hum. Gene Ther., 16, 81-90.
14. Di Domenico, C., Di Napoli, D., Gonzalez, Y.R.E., Lombardo, A., Naldini, L. and Di Natale, P. (2006) Hum. Gene Ther., 17, 1112-1121.
15. Durand, P., Fabrega, S., Henrissat, B., Mornon, J.P. and Lehn, P. (2000) Hum. Mol. Genet., 9, 967-977.
16. El-Amouri, S.S., Dai, M., Han, J.F., Brady, R.O. and Pan, D. (2014) Mol. Ther., 22, 2028-2037.
17. Ensina, L.F., Aranda, C.S., de Lacerda, A.E., Camelo-Nunes, I., Sole, D., Martins, A.M. and Castells, M. (2014) Pediatr. Allergy Immunol., 25, 498-499.
18. Fletcher, J.M. (2006) J. Inherit. Metab. Dis., 29, 405-408.
19. Freeman, C. and Hopwood, J.J. (1992) Biochem. J., 282(Pt 3), 899-908.
20. Geddie, M.L. and Matsumura, I. (2004) J. Biol. Chem., 279, 26462-26468.
21. Goding, J.W. (1976) J. Immunol. Methods, 13, 215-226.
22. Harmatz, P., Giugliani, R., Schwartz, I., et al. (2006) J. Pediatr., 148, 533-539.
23. Herati, R.S., Ma, X., Tittiger, M., Ohlemiller, K.K., Kovacs, A. and Ponder, K.P. (2008) J. Gene Med., 10, 972-982.
24. Islam, M.R., Tomatsu, S., Shah, G.N., Grubb, J.H., Jain, S. and Sly, W.S. (1999) J. Biol. Chem., 274, 23451-23455.
25. Jain, S., Drendel, W.B., Chen, Z.W., Mathews, F.S., Sly, W.S. and Grubb, J.H. (1996) Nat. Struct. Biol., 3, 375-381.
26. Kakkis, E.D., McEntee, M.F., Schmidtchen, A., et al. (1996) Biochem. Mol. Med., 58, 156-167.
27. Kishnani, P.S., Nicolino, M., Voit, T., et al. (2006) J. Pediatr., 149, 89-97.
28. Kishnani, P.S., Goldenberg, P.C., Dearmey, S.L., et al. (2009) Mol. Genet. Metab. doi: S1096-7192(09)00244-3.
29. Langereis, E.J., van Vlies, N., Church, H.J., et al. (2014) Mol. Genet. Metab. doi: 10.1016/j.ymgme.2014.10.012.
30. Lin, H.Y., Lin, S.P., Chuang, C.K., Chen, M.R., Chen, B.F. andWraith, J.E. (2005) J. Inherit. Metab. Dis., 28, 1146-1148.
31. Linthorst, G.E., Hollak, C.E., Donker-Koopman, W.E., Strijland, A. and Aerts, J. M. (2004) Kidney Int., 66, 1589-1595.
32. Maita, N., Tsukimura, T., Taniguchi, T., Saito, S., Ohno, K., Taniguchi, H. and Sakuraba, H. (2013) Proc. Natl Acad. Sci. U.S.A., 110, 14628-14633.
33. Matsumura, I. and Ellington, A.D. (2001) J. Mol. Biol., 305, 331-339.
34. Natowicz, M.R., Chi, M.M., Lowry, O.H. and Sly, W.S. (1979) Proc. Natl Acad. Sci. U.S.A., 76, 4322-4326.
35. Nieman, C.E., Wong, A.W., He, S., Clarke, L., Hopwood, J.J. and Withers, S.G. (2003) Biochemistry, 42, 8054-8065.
36. Ohashi, T., Iizuka, S., Ida, H. and Eto, Y. (2008) Mol. Genet. Metab., 94, 313-318.
37. Ohashi, T., Iizuka, S., Shimada, Y., Higuchi, T., Eto, Y., Ida, H. and Kobayashi, H. (2012) Mol. Ther., 20, 1924-1931.
38. Osipovitch, D.C., Parker, A.S., Makokha, C.D., Desrosiers, J., Kett, W.C., Moise, L., Bailey-Kellogg, C. and Griswold, K.E. (2012) Protein Eng. Des. Sel., 25, 613-623.
39. Parker, A.S., Zheng, W., Griswold, K.E. and Bailey-Kellogg, C. (2010) BMC Bioinform., 11, 180.
40. Pastores, G.M., Sibille, A.R. and Grabowski, G.A. (1993) Blood, 82, 408-416.
41. Patel, T.T., Banugaria, S.G., Case, L.E., Wenninger, S., Schoser, B. and Kishnani, P. S. (2012) Mol. Genet. Metab., 106, 301-309.
42. Peroni, D.G., Pescollderungg, L., Piacentini, G.L., Cassar, W. and Boner, A.L. (2009) J. Pediatr., 155, 940-941.
43. Rempel, B.P., Clarke, L.A. and Withers, S.G. (2005) Mol. Genet. Metab., 85, 28-37.
44. Salvat, R.S., Parker, A.S., Guilliams, A., Choi, Y., Bailey-Kellogg, C. and Griswold, K.E. (2014) Cell. Mol. Life Sci., 71, 4869-4880.
45. Schrodinger, LLC (2010) The PyMOL Molecular Graphics System, Version 1.7.4.
46. Staretz-Chacham, O., Lang, T.C., LaMarca, M.E., Krasnewich, D. and Sidransky, E. (2009) Pediatrics, 123, 1191-1207.
47. Sun, B., Bird, A., Young, S.P., Kishnani, P.S., Chen, Y.T. and Koeberl, D.D. (2007) Am. J. Hum. Genet., 81, 1042-1049.
48. Tsujihata, Y., So, T., Hashimoto, Y., Ueda, T. and Imoto, T. (2001) Mol. Immunol., 38, 375-381.
49. Tsukimura, T., Tajima, Y., Kawashima, I., et al. (2008) Biol. Pharm. Bull., 31, 1691-1695.
50. Unger, E.G., Durrant, J., Anson, D.S. and Hopwood, J.J. (1994) Biochem. J., 304 (Pt 1), 43-49.
51. Wang, J., Lozier, J., Johnson, G., Kirshner, S., Verthelyi, D., Pariser, A., Shores, E. and Rosenberg, A. (2008) Nat. Biotechnol., 26, 901-908.
52. Wang, D., El-Amouri, S.S., Dai, M., Kuan, C.Y., Hui, D.Y., Brady, R.O. and Pan, D. (2013) Proc. Natl Acad. Sci. U.S.A., 110, 2999-3004.
53. Wu, C.H., Balasubramanian, W.R., Ko, Y.P., Hsu, G., Chang, S.E., Prijovich, Z.M., Chen, K.C. and Roffler, S.R. (2004) Biotechnol. Appl. Biochem., 40, 167-172.
54. Xu, M., Liu, K., Swaroop, M., Sun, W., Dehdashti, S.J., McKew, J.C. and Zheng, W. (2014) J. Biomol. Screen., 19, 168-175.
55. Zarate, Y.A. and Hopkin, R.J. (2008) Lancet, 372, 1427-1435.