Protein Engineering of Single-Chain Fv Analogs and Fusion Proteins

Methods in Enzymology

Volumn 203, Issue C, 1991, Pages 46-52

  Huston, James S ^a   Mudgett Hunter, Meredith ^a   Tai, Mei Sheng ^a   McCartney, John ^a   Warren, Frederick ^a   Haber, Edgar ^a   Oppermann, Hermann ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; IMMUNOGLOBULIN A;

ARTICLE; BIOENGINEERING; IMMUNOGLOBULIN VARIABLE REGION; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANIMAL; ANTIBODY SPECIFICITY; BASE SEQUENCE; BINDING SITES, ANTIBODY; COMPUTER SIMULATION; GENES, IMMUNOGLOBULIN; HUMAN; IMMUNOGLOBULIN A; IMMUNOGLOBULIN G; IMMUNOGLOBULIN VARIABLE REGION; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PLASMACYTOMA; POLYMERASE CHAIN REACTION; PROTEIN CONFORMATION; PROTEIN ENGINEERING; RECOMBINANT FUSION PROTEINS; SUPPORT, U.S. GOV'T, P.H.S.;

EID: 0026334521     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/0076-6879(91)03005-2     Document Type: Article

References (125)

1. Inbar, D., Hochman, J., Givol, D., Proc. Natl. Acad. Sci. U.S.A., 69, 1972, 2659.
2. Hochman, J., Inbar, D., Givol, D., Biochemistry, 12, 1973, 1130.
3. Hochman, J., Gavish, M., Inbar, D., Givol, D., Biochemistry, 15, 1976, 2706.
4. Sharon, J., Givol, D., Biochemistry, 15, 1976, 1591.
5. Sen, J., Beychok, S., Proteins: Struct. Funct. Genet., 1, 1986, 256.
6. Kakimoto, K., Onoue, K., J. Immunol., 112, 1974, 1373.
7. Lin, L.-C., Putnam, F.W., Proc. Natl. Acad. Sci. U.S.A., 75, 1978, 2649.
8. Reth, M., Imanishi-Kari, T., Rajewsky, K., Eur. J. Immunol., 9, 1979, 1004.
9. Goni, F., Frangione, B., Proc. Natl. Acad. Sci. U.S.A., 80, 1983, 4837.
10. Reichmann, L., Foote, J., Winter, G., J. Mol. Biol., 203, 1988, 825.
11. Skerra, A., Plückthun, A., Science, 240, 1988, 1038.
12. Field, H., Yarranton, G.T., Rees, A.R., Ginsberg, H., Brown, F., Lerner, R.A., Channock, R.M., (eds.) Vaccines 88, 1988, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, 29.
13. A. Plückthun and A. Skerra, this series, Vol. 178, p. 497.
14. Field, H., Yarranton, G.T., Rees, A.R., Protein Eng., 3, 1990, 641.
15. Huston, J.S., Levinson, D., Mudgett-Hunter, M., Tai, M.-S., Novotny, J., Margolies, M.N., Ridge, R., Bruccoleri, R.E., Haber, E., Crea, R., Oppermann, H., Proc. Natl. Acad. Sci. U.S.A., 85, 1988, 5879.
16. Tai, M.-S., Mudgett-Hunter, M., Levinson, D., Wu, G.-M., Haber, E., Oppermann, H., Huston, J.S., Biochemistry, 29, 1990, 8024.
17. Shealy, D., Nedelman, M., Tai, M.-S., Huston, J.S., Berger, H., Lister-James, J., Dean, R.T., J. Nucl. Med., 31(5 Suppl), 1990, 776.
18. Bird, R.E., Hardman, K.D., Jacobson, J.W., Johnson, S., Kaufman, B.M., Lee, S.-M., Lee, T., Pope, S.H., Riordan, G.S., Whitlow, M., Science, 242, 1988, 423.
19. Bedzyk, W.D., Weidner, K.M., Denzin, L.K., Johnson, L.S., Hardman, K.D., Pantoliano, M.W., Ansel, E.D., Voss, E.W. Jr., J. Biol. Chem., 265, 1990, 18615.
20. Colcher, D., Bird, R., Roselli, M., Hardman, K.D., Johnson, S., Pope, S., Dodd, S.W., Pantoliano, M.W., Milenic, D.E., Schlom, J., J. Natl. Cancer Inst., 82, 1990, 1191.
21. Iverson, B.L., Iverson, S.A., Roberts, V.A., Getzoff, E.D., Tainer, J.A., Benkovic, S.J., Lerner, R.A., Science, 249, 1990, 659.
22. Gibbs, R.A., Posner, B.A., Filpula, D.R., Dodd, S.W., Finkelman, M.A.J., Lee, T.K., Wroble, M., Whitlow, M., Benkovic, S.J., Proc. Natl. Acad. Sci. U.S.A., 88, 1991, 4001.
23. Glockshuber, R., Malia, M., Pfitzinger, I., Plückthun, A., Biochemistry, 29, 1990, 1362.
24. Skerra, A., Pfitzinger, I., Plückthun, A., Bio/Technology, 9, 1991, 273.
25. L domain encompassed 116 residues (as implied by Condra et al.), the linker lengths for anti-HRV sFv proteins would be 3 residues shorter than the values noted in Table I (group B). Their 11-residue linker would then be only eight residues in length, and their addition of one or two (GGGGS) segments may have increased activity simply by increasing linker length.
26. Chaudhary, V.K., Queen, C., Junghans, R.P., Waldmann, T.A., FitzGerald, D.J., Pastan, I., Nature (London), 339, 1989, 394.
27. Chaudhary, V.K., Batra, J.K., Gallo, M.G., Willingham, M.C., FitzGerald, D.J., Pastan, I., Proc. Natl. Acad. Sci. U.S.A., 87, 1990, 1066.
28. Batra, J.K., Chaudhary, V.K., FitzGerald, D., Pastan, I., Biochem. Biophys. Res. Commun., 171, 1990, 1.
29. Batra, J.K., FitzGerald, D., Gately, M., Chaudhary, V.K., Pastan, I., J. Biol. Chem., 265, 1990, 15198.
30. Kreitman, R.J., Chaudhary, V.K., Waldmann, T., Willingham, M.C., FitzGerald, D.J., Pastan, I., Proc. Nat. Acad. Sci. U.S.A., 87, 1990, 8291.
31. McCartney, J., Lederman, L., Drier, E., Wu, G.-M., Batorsky, R., Cabral-Denison, N., Huston, J.S., Oppermann, H., ICSU Short Rep., 10, 1990, 114.
32. J. S. Huston, M. Mudgett-Hunter, G.-M. Wu, C. Yost, and H. Oppermann, unpublished results (1989).
33. 2 and related linkers to construction of a single-chain murine class I major transplantation antigen, expressed in COS-1 cells.
34. Chaudhary, V.K., Gallo, M.G., FitzGerald, D.J., Pastan, I., Proc. Natl. Acad. Sci. U.S.A., 87, 1990, 9491.
35. Batra, J.K., FitzGerald, D.J., Chaudhary, V.K., Pastan, I., Mol. Cell. Biol., 11, 1991, 2200.
36. McCafferty, J., Griffiths, A.D., Winter, G., Chiswell, D.J., Nature (London), 348, 1990, 552.
37. Frankel, A.E., (eds.) Immunotoxins, 1988, Kluwer Academic Publishers, Boston, 565.
38. Morrison, S.L., Johnson, M.J., Herzenberg, L.A., Oi, V.T., Proc. Natl. Acad. Sci. U.S.A., 81, 1984, 6851.
39. Neuberger, M.S., Williams, G.T., Fox, R.O., Nature (London), 312, 1984, 604.
40. S.-U. Shin and S. L. Morrison, this series, Vol. 178, p. 459.
41. Runge, M.S., Bode, C., Matsueda, G.R., Haber, E., Proc. Natl. Acad. Sci. U.S.A., 84, 1987, 7659.
42. T. W. Love, M. S. Runge, E. Haber, and T. Quertermous, this series, Vol. 178, p. 515.
43. Haber, E., Novotny, J., Springer, T.A., (eds.) Hybridoma Technology in the Biosciences and Medicine, 1985, Plenum, New York, 57.
44. Segal, D.M., Padlan, E.A., Cohen, G.H., Rudikoff, S., Potter, M., Davies, D.R., Proc. Natl. Acad. Sci. U.S.A., 71, 1974, 4298.
45. Satow, Y., Cohen, G.H., Padlan, E.A., Davies, D.R., J. Mol. Biol., 190, 1986, 593.
46. Novotny, J., Bruccoleri, R.E., Newell, J., Murphy, D., Haber, E., Karplus, M., J. Biol. Chem., 258, 1983, 14433.
47. Chothia, C., Novotny, J., Bruccoleri, R., Karplus, M., J. Mol. Biol., 186, 1985, 651.
48. Novotny, J., Haber, E., Proc. Natl. Acad. Sci. U.S.A., 82, 1985, 4592.
49. Riechmann, L., Foote, J., Winter, G., J. Mol. Biol., 203, 1988, 825.
50. Bhat, T.N., Bentley, G.A., Fischmann, T.O., Boulot, G., Poljak, R.J., Nature (London), 347, 1990, 483.
51. Amit, A.G., Mariuzza, R.A., Phillips, S.E.V., Poljak, R.J., Science, 233, 1986, 747.
52. Jones, P.T., Dear, P.H., Foote, J., Neuberger, M.S., Winter, G., Nature (London), 321, 1986, 522.
53. Verhoeyen, M., Milstein, C., Winter, G., Science, 239, 1988, 1534.
54. Riechmann, L., Foote, J., Winter, G., J. Mol. Biol., 203, 1988, 825.
55. Bruggemann, M., Winter, G., Waldmann, H., Neuberger, M.S., J. Exp. Med., 170, 1989, 2153.
56. Kabat, E.A., Wu, T.T., Reid-Miller, M., Perry, H.M., Gottesman, K.S., (eds.) Sequences of Proteins of Immunological Interest, 4th Ed., 1987, U.S. Department of Health and Human Services, Washington, D.C, 804.
57. Ramachandran, G.N., Venkatachalam, C.M., Krimm, S., Biophys. J., 6, 1966, 849.
58. Ramachandran, G.N., Ramakrishnan, C., Sasisekharan, V., J. Mol. Biol., 7, 1963, 95.
59. Panka, D.J., Mudgett-Hunter, M., Parks, D.R., Peterson, L.L., Herzenberg, L.A., Haber, E., Margolies, M.N., Proc. Natl. Acad. Sci. U.S.A., 85, 1988, 3080 This group found that deleting only two FR residues caused nearly a 50-fold increase of binding affinity as well as a significant change in specificity. Observation of this pronounced effect on hapten binding suggests the possibility that, in some situations, fusion of a linker segment between the pair of V domains of a particular Fv could have an effect on binding site properties in the resulting sFv analog.
60. H (Fig. 7A)].
61. Pitt-Rivers, R., Impiombato, F.S.A., Biochem. J., 109, 1968, 825.
62. Reynolds, J.A., Tanford, C., Proc. Natl. Acad. Sci. U.S.A., 66, 1970, 1002.
63. Reynolds, J.A., Tanford, C., J. Biol. Chem., 245, 1970, 5161.
64. Fish, W.W., Reynolds, J.A., Tanford, C., J. Biol. Chem., 245, 1970, 5166.
65. K. Weber, J. R. Pringle, and M. Osborn, this series, Vol. 26, p. 3.
66. See, Y.P., Jackowski, G., Creighton, T.E., (eds.) Protein Structure: A Practical Approach, 1989, IRL Press, Oxford, 1.
67. Roberts, S., Cheetham, J., Rees, A.R., Nature (London), 328, 1987, 731 These researchers combined molecular modeling and site-directed mutagenesis with a Xenopus oocyte expression system to generate a series of mutant antibodies. They discovered a double mutant that showed an 8-fold increase in affinity and improved selectivity for lysozyme. Also discussed in Chapters [6] and [9], this volume.
68. Better, M., Chang, C.P., Robinson, R.R., Horwitz, A.H., Science, 240, 1988, 1041.
69. M. Better and A. H. Horwitz, this series, Vol. 178, p. 476; A. Plückthun and A. Skerra, this series, Vol. 178, p. 497.
70. Plückthun, A., Bio/Technology, 9, 1991, 545.
71. Zurawski, V.R. Jr., Black, P.H., Haber, E., Kennett, R.H., McKearn, T.J., Bechtol, K.B., (eds.) Monoclonal Antibodies. Hybridomas: A New Dimension in Biological Analyses, 1980, Plenum, New York, 19.
72. Short, J.M., Fernandez, J.M., Sorge, J.A., Huse, W.D., Nucleic Acids Res., 16, 1988, 7583.
73. Orlandi, R., Gussow, D.H., Jones, P.T., Winter, G., Proc. Natl. Acad. Sci. U.S.A., 86, 1989, 3833.
74. Sastry, L., Alting-Mees, M., Huse, W.D., Short, J.M., Sorge, J.A., Hay, B.N., Janda, K.D., Benkovic, S.J., Lerner, R.A., Proc. Natl. Acad. Sci. U.S.A., 86, 1989, 5728.
75. Ward, E.S., Gussow, D., Griffiths, A.D., Jones, P.T., Winter, G., Nature (London), 341, 1989, 544.
76. Strohal, R., Kroemer, G., Wick, G., Kofler, R., Nucleic Acids Res., 15, 1987, 2771.
77. Saikai, R.K., Gelfand, D.H., Stoffel, S., Scharf, S.J., Higuchi, R., Horn, G.T., Mullis, K.B., Erlich, H.A., Science, 293, 1988, 487.
78. Chiang, Y.L., Sheng-Dong, R., Brow, M.A., Larrick, J.W., BioTechniques, 7, 1989, 360.
79. Huse, W.D., Sastry, L., Iverson, S.A., Kang, A.S., Alting-Mees, M., Burton, D.R., Benkovic, S.J., Lerner, R.A., Science, 246, 1989, 1275.
80. Davis, G.T., Bedzyk, W.D., Voss, E.W., Jacobs, T.W., Bio/Technology, 9, 1991, 165.
81. Jones, S.T., Bendig, M.M., Bio/Technology, 9, 1991, 88.
82. Jones, S.T., Bendig, M.M., and erratta Bio/Technology, 9, 1991, 579.
83. Kohler, G., Milstein, C., Nature (London), 245, 1975, 495.
84. Milstein, C., Proc. R. Soc. London B, 239, 1990, 1.
85. Parmley, S.F., Smith, G.P., Gene, 73, 1988, 305.
86. Scott, J.K., Smith, G.P., Science, 249, 1990, 386.
87. Devlin, J.J., Panganiban, L.C., Devlin, P.E., Science, 249, 1990, 404.
88. Cwirla, S.E., Peters, E.A., Barrett, R.W., Dower, W.J., Proc. Natl. Acad. Sci. U.S.A., 87, 1990, 6378.
89. Briggs, M.S., Gierasch, L.M., Adv. Protein Chem., 38, 1986, 109.
90. Mitraki, A., King, J., Bio/Technology, 7, 1989, 690.
91. Schein, C.H., Bio/Technology, 7, 1989, 1141.
92. S. M. Andrew, P. Perez, P. J. Nicholls, A. J. T. George, and D. M. Segal, unpublished results (1990); D. Jin, M.-S. Tai, J. S. Huston, and H. Oppermann, unpublished results (1991).
93. Studier, F.W., Moffat, B.A., J. Mol. Biol., 189, 1986, 113.
94. F. W. Studier, A. H. Rosenburg, J. J. Dunn, and J. W. Dubendorff, this series, Vol. 185, p. 60.
95. Buckley, C.E. III, Whitney, P.L., Tanford, C., Proc. Natl. Acad. Sci. U.S.A., 50, 1963, 827.
96. Noelken, M.E., Tanford, C., J. Biol. Chem., 239, 1964, 1828.
97. Rowe, E.S., Tanford, C., Biochemistry, 12, 1973, 4822.
98. Rowe, E.S., Biochemistry, 15, 1976, 905.
99. Rowe, E.S., Ph.D Dissertation, 1971, Duke University.
100. Buchner, J., Rudolph, R., Bio/Technology, 9, 1991, 157.
101. E. Haber Proc. Natl. Acad. Sci. U.S.A. 1964, 52, 1099
102. Whitney, P.L., Tanford, C., Proc. Natl. Acad. Sci. U.S.A., 53, 1965, 524.
103. Saxena, P., Wetlaufer, D.B., Biochemistry, 9, 1971, 5015.
104. Better, M., Weickmann, J., Lin, Y.-L., ICSU Short Rep., 10, 1990, 105.
105. zu Putlitz, J., Kubansek, W.L., Duchene, M., Marget, M., von Specht, B.-U., Domdey, H., Bio/Technology, 8, 1990, 651.
106. Hiatt, A., Cafferkey, R., Bowdish, K., Nature (London), 342, 1989, 76.
107. Brosius, J., Holy, A., Proc. Natl. Acad. Sci. U.S.A., 81, 1984, 6929.
108. DeBoer, H.A., Comstock, L.J., Vasser, M., Proc. Natl. Acad. Sci. U.S.A., 80, 1983, 21.
109. Samuelsson, E., Wadensten, H., Harmanis, M., Moks, T., Uhlén, M., Bio/Technology, 9, 1991, 363.
110. Sophianopoulos, J.A., Durham, S.J., Sophianopoulos, A.J., Ragsdale, H.L., Cropper, W.P., Arch. Biochem. Biophys., 187, 1978, 132.
111. MacMahon, W., Stallings, J., Sgoutas, D., Clin. Chem., 28, 1982, 240.
112. Sophianopoulos, J.A., Sophianopoulos, A.J., MacMahon, W., Arch. Biochem. Biophys., 223, 1983, 350.
113. A. J. Sophianopoulos and J. A. Sophianopoulos, this series, Vol. 117, p. 354.
114. McPherson, G.A., Kinetic, EBDA, LIGAND, Lowry. A Collection of Radioligand Binding Analysis Programs. 1985, Elsevier BIOSOFT, Cambridge.
115. Schildbach, J.F., Panka, D.J., Parks, D.R., Jager, G.C., Novotny, J., Herzenberg, L.A., Mudgett-Hunter, M., Bruccoleri, R.E., Haber, E., Margolies, M.N., J. Biol. Chem., 266, 1991, 4640.
116. M. Mudgett-Hunter, unpublished results (1990).
117. Langone, J.J., Adv. Immunol., 32, 1982, 157.
118. W. F. Stafford III and J. S. Huston, unpublished results (1990).
119. Ikemura, H., Takagi, H., Inouye, M., J. Biol. Chem., 262, 1987, 7859.
120. Keen, N.T., Tamaki, S., J. Bacteriol., 168, 1986, 595.
121. M. S. Tai and F. Warren, unpublished results (1991).
122. Bentley, G.A., Boulot, G., Riottot, M.M., Poljak, R.J., Nature (London), 348, 1990, 254.
123. Davies, D.R., Padlan, E.A., Sheriff, S., Annu. Rev. Biochem., 59, 1990, 439.
124. Kumosinski, T.F., Timasheff, S.N., J. Am. Chem. Soc., 88, 1966, 5635.
125. Huston, J.S., Björk, I., Tanford, C., Biochemistry, 11, 1972, 4256.