Mutational analysis of the affinity maturation of antibody 48G7

Journal of Molecular Biology

Volumn 294, Issue 5, 1999, Pages 1191-1201

  Yang, Priscilla L ^a   Schultz, Peter G ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Affinity maturation; Antibody; Molecular evolution; Somatic hypermutation; Structure function

Indexed keywords

ANTIBODY; HAPTEN;

ANTIBODY AFFINITY; ANTIBODY STRUCTURE; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; GERM LINE; HUMORAL IMMUNITY; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; SOMATIC MUTATION; STRUCTURE ACTIVITY RELATION;

EID: 0033579560     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3197     Document Type: Article

References (42)

1. Allen D., Cumano A., Simon T., Sablitzky F., Rajewsky K. Modulation of antibody binding affinity by somatic mutation. Int. J. Cancer. Supplement. 3:1988;1-8.
2. Alzari P. M., Spinelli S., Mariuzza R. A., Boulot G., Poljak R. J., Jarvis J. M., Milstein C. Three-dimensional structure determination of an anti-2-phenyloxazolone antibody: the role of somatic mutation and heavy/light chain pairing in the maturation of an immune response. EMBO J. 9:1990;3807-3814.
3. Berek C., Griffiths G. M., Milstein C. Molecular events during maturation of the immune response to oxazolone. Nature. 316:1985;412-418.
4. Casson L. P., Manser T. Evaluation of loss and change of specificity resulting from random mutagenesis of an antibody V-H region. J. Immunol. 155:1995a;5647-5654.
5. Casson L. P., Manser T. Random mutagenesis of two complementarity determining region amino acids yields an unexpectedly high frequency of antibodies with increased affinity for both cognate antigen and autoantigen. J. Expt. Med. 182:1995b;743-750.
6. Chen C., Roberts V. A., Stevens S., Brown M., Stenzel-Poore M. P., Rittenberg M. B. Enhancement and destruction of antibody function by somatic mutation: unequal occurrence is controlled by V gene combinatorial associations. EMBO J. 14:1995;2784-2794.
7. Even J., Griffiths G. M., Berek C., Milstein C. Light chain germ-line genes and the immune response to 2-phenyloxazolone. EMBO J. 4:1985;3439-3445.
8. Green N. S., Lin M. M., Scharff M. D. Somatic hypermutation of antibody genes: a hot spot warms up. Bioessays. 20:1998;227-234.
9. Griffiths G. M., Berek C., Kaartinen M., Milstein C. Somatic mutation and the maturation of immune response to 2-phenyl oxazolone. Nature. 312:1984;271-275.
10. Huang Z., Li S., Korngold R. Immunoglobulin superfamily proteins: structure, mechanisms, and drug discovery. Biopolymers. 43:1997;367-382.
11. Jacobs J. W. Catalytic antibodies. Doctoral dissertation, University of California at Berkely. 1990.
12. Jones T. A., Zou J. Y., Cowan S. W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
13. Kabat E. A. Sequences of Proteins of Immunological Interest. 5th edit. NIH publication no. 91-3242, US Dept. of Health and Humans Services Public Health Service National Institutes of Health, Bethesda, MD. 1991.
14. Kimura M. The length of time required for a selectively neutral mutant to reach fixation through random frequency drift in a finite population. Genet. Res. 15:1970;131-133.
15. Kunkel T. A., Roberts J. D., Zakour R. A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:1987;367-382.
16. Lozano F., Rada C., Jarvis J. M., Milstein C. Affinity maturation leads to differential expression of multiple copies of a kappa light-chain transgene. Nature. 363:1993;271-273.
17. Maizels N. Somatic hypermutation: how many mechanisms diversify V region sequences? Cell. 83:1995;9-12.
18. Mariuzza R. A., Boulot G., Guillon V., Poljak R. J., Berek C., Jarvis J. M., Milstein C. Preliminary crystallographic study of the Fab fragments of two monoclonal anti-2-phenyloxazolone antibodies. J. Biol. Chem. 260:1985;10268-10270.
19. Mizutani R., Miura K., Nakayama T., Shimada I., Arata Y., Satow Y. Three-dimensional structures of the Fab fragment of murine N1G9 antibody from the primary immune response and of its complex with (4-hydroxy-3-nitrophenyl)acetate. J. Mol. Biol. 254:1995;208-222.
20. Nakayama T., Arata Y., Shimada I. A multinuclear NMR study of the affinity maturation of anti-NP mouse monoclonal antibodies: comparison of antibody combining sites of primary response antibody N1G9 and secondary response antibody 3B62. Biochemistry. 32:1993;13961-13968.
21. Neuberger M. S., Milstein C. Somatic hypermutation. Curr. Opin. Immunol. 7:1995;248-254.
22. Parhami-Seren B., Wysocki L. J., Margolies M. N., Sharon J. Clustered H chain somatic mutations shared by anti-p-azophenylarsonate antibodies confer enhanced affinity and ablate the cross-reactive idiotype. J. Immunol. 145:1990;2340-2346.
23. Patten P. A., Gray N. S., Yang P. L., Marks C. B., Wedemayer G. J., Boniface J. J., Stevens R. C., Schultz P. G. The immunological evolution of catalysis. Science. 271:1996;1086-1091.
24. Pewzner-Jung Y., Simon T., Eilat D. Structural elements controlling anti-DNA antibody affinity and their relationship to anti-phosphorylcholine activity. J. Immunol. 156:1996;3065-3073.
25. Romesberg F. E., Spiller B., Schultz P. G., Stevens R. C. Immunological origins of binding and catalysis in a Diels-Alderase antibody. Science. 279:1998;1929-1933.
26. Schultz P. G., Lerner R. A. From molecular diversity to catalysis: lessons from the immune system. Science. 269:1995;1835-1842.
27. Sharon J. Structural correlates of high antibody affinity: three engineered amino acid substitutions can increase the affinity of an anti-p-azophenylarsonate antibody 200-fold. Proc. Natl Acad. Sci. USA. 87:1990;4814-4817.
28. Spiller B., Romesber F., Schultz P., Stevens R. The role of affinity maturation in a Diels Alderase catalytic antibody. FASEB J. 11:1997;A1326.
29. Strong R. K., Campbell R., Rose D. R., Petsko G. A., Sharon J., Margolies M. N. Three-dimensional structure of murine anti-p-azophenylarsonate Fab 36-71. 1. X-ray crystallography, site-directed mutagenesis, and modeling of the complex with hapten. Biochemistry. 30:1991;3739-3748.
30. Torigoe H., Nakayama T., Imazato M., Shimada I., Arata Y., Sarai A. The affinity maturation of anti-4-hydroxy-3-nitrophenylacetyl mouse monoclonal antibody: a calorimetric study of the antigen-antibody interaction. J. Biol. Chem. 270:1995;22218-22222.
31. Ulrich H. D. Recombinant catalytic antibodies, thesis. 1996;University of California at Berkeley.
32. Ulrich H. D., Schultz P. G. Analysis of hapten binding and catalytic determinants in a family of catalytic antibodies. J. Mol. Biol. 275:1998;95-111.
33. Ulrich H. D., Patten P. A., Yang P. L., Romesberg F. E., Schultz P. G. Expression studies of catalytic antibodies. Proc. Natl Acad. Sci. USA. 92:1995;11907-11911.
34. Ulrich H. D., Mundorff E., Santarsiero B. D., Driggers E. M., Stevens R. C., Schultz P. G. The interplay between binding energy and catalysis in the evolution of a catalytic antibody. Nature. 389:1997;271-275.
35. Wagner S. D., Neuberger M. S. Somatic hypermutation of immunoglobulin genes. Paul W. E. Annual Review of Immunology. 1996;441-457 Annual Reviews Inc. Palo Alto, California.
36. Wedemayer G. J., Patten P. A., Wang L. H., Schultz P. G., Stevens R. C. Structural insights into the evolution of an antibody combining site (see comments) (published erratum appears in Science, 1997, Sep 5;277(5331):1423). Science. 276:1997a;1665-1669.
37. Wedemayer G. J., Wang L. H., Patten P. A., Schultz P. G., Stevens R. C. Crystal structures of the free and liganded form of an esterolytic catalytic antibody. J. Mol. Biol. 268:1997b;390-400.
38. Wong Y. W., Kussie P. H., Parhami-Seren B., Margolies M. N. Modulation of antibody affinity by an engineered amino acid substitution. J. Immunol. 154:1995;3351-3358.
39. Wysocki L. J., Gridley T., Huang S., Grandea d. A. G., Gefter M. L. Single germline VH and V kappa genes encode predominating antibody variable regions elicited in strain A mice by immunization with p-azophenylarsonate. J. Expt. Med. 166:1987;1-11.
40. Yoshihara Y., Oka S., Ikeda J., Mori K. Immunoglobulin superfamily molecules in the nervous system. Neurosci. Res. 10:1991;83-105.
41. Yuhasz S. C., Parry C., Strand M., Amzel L. M. Structural analysis of affinity maturation: the three-dimensional structures of complexes of an anti-nitrophenol antibodies. Mol. Immunol. 32:1995;1143-1155.
42. Zhang J., Gu X. Correlation between the substitution rate and rate variation among sites in protein evolution. Genetics. 149:1998;1615-1625.