Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains

Protein Science

Volumn 8, Issue 3, 1999, Pages 509-517

  Raffen, Rosemarie ^a   Dieckman, Lynda J ^a   Szpunar, Meredith ^a   Wunschl, Christine ^a   Pokkuluri, Phani R ^a   Dave, Poras ^a   Stevens, Priscilla Wilkins ^a   Cai, Xiaoyin ^a   Schiffer, Marianne ^a   Stevens, Fred J ^a  

^a ARGONNE NATIONAL LABORATORY   (United States)

Author keywords

Amyloid fibril; Immunoglobulin light chain variable domain; Light chain dimer; Protein aggregation; Protein stability; Site directed mutagenesis

Indexed keywords

AMINO ACID; IMMUNOGLOBULIN LIGHT CHAIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMYLOIDOSIS; ARTICLE; FIBER; NONHUMAN; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN STABILITY; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; THERMODYNAMICS;

EID: 0033020141     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.3.509     Document Type: Article

References (49)

1. Bellotti V, Stoppini M, Mangione PP, Fornasieri A, Min L, Merlini G, Ferri G. 1996. Structural and functional characterization of three human immunoglobulin kappa light chains with different pathological implications. Biochem Biophys Acta 1317:161-167.
2. Benditt EP, Eriksen N, Berglund C. 1970. Congo red dichroism with dispersed amyloid fibrils, an extrinsic Cotton effect. Proc Natl Acad Sci USA 66:1044-1051.
3. Booth DR, Sunde M, Bellotti V, Robinson CV, Hutchinson WL, Fraser PE, Hawkins PN, Dobson CM, Radford SE, Blake CCF, Pepys MB. 1997. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 385:787-793.
4. Carra JH, Privalov PL. 1995. Energetics of denaturation and m values of staphylococcal nuclease mutants. Biochemistry 34:2034-2041.
5. Chrunyk BA, Evans J, Wetzel R. 1993. Probing the role of protein folding in inclusion body formation. In: Himmel ME, Georgiou G, eds. Biocatalyst design for stability and specificity. Washington, DC: American Chemical Society, pp 46-58.
6. Colon W, Kelly JW. 1992. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 31:8654-8660.
7. Cupo JF, Pace CN. 1983. Conformational stability of mixed disulfide derivatives of β-lactoglobulin B. Biochemistry 22:2654-2658.
8. Glenner GG, Ein D, Eanes ED, Bladen HA, Terry W, Page DL. 1971. Creation of "amyloid" fibrils from Bence Jones proteins in vitro. Science 174:712-714.
9. Hartshorne NH, Stuart A. 1970. Crystals and the polarizing microscope, 4th ed. London: Edward Arnold Publishers Ltd.
10. L domain. Protein Sci 4:2073-2081.
11. Higuchi R, Krummel B, Saiki RK. 1988. A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions. Nucleic Acids Res 16:7351-7367.
12. Huang D-B, Chang C-H, Ainsworth C, Johnson G, Solomon A, Stevens FJ, Schiffer M. 1997. Variable domain structure of κIV protein Len: High homology to the murine light chain McPC603. Mol Immunol 34:1291-1301.
13. Hurle MR, Helms LR, Li L, Chan W, Wetzel R. 1994. A role for destabilizing amino acid replacements in light-chain amyloidosis. Proc Natl Acad Sci USA 91:5446-5450.
14. Jackson SE, Fersht AR. 1991. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry 30:10428-10435.
15. Kabat EA, Wu TT, Perry HM, Gottesman KS, Foeller C. 1991. Sequences of proteins of immunological interest, 5th ed. NIH publication No. 91-3242. Washington, DC: U.S. Department of Health and Human Services, U.S. Government Printing Office.
16. Klafki HW, Pick AI, Pardowitz I, Cole T, Awni LA, Barnikol HU, Mayer F, Kratzin HD, Hilschmann N. 1993. Reduction of disulfide bonds in an amyloidogenic Bence-Jones protein leads to formation of "amyloid-like" fibrils in vitro. Biol Chem Hoppe-Seyler 374:1117-1122.
17. Klein R, Jaenichen R, Zachau HG. 1993. Expressed human immunoglobulin κ genes and their hypermutation. Eur J Immunol 23:3248-3271.
18. Klunk WE, Pettegrew JW, Abraham DJ. 1989a. Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J Histochem Cytochem 37:1273-1281.
19. Klunk WE, Pettegrew JW, Abraham DJ. 1989b. Two simple methods for quantifying low-affinity dye-substrate binding. J Histochem Cytochem 37:1293-1297.
20. Knapp JA, Pace CN. 1974. Guanidine hydrochloride and acid denaturation of horse, cow and Candida krusei cytochromes c. Biochemistry 13:1289-1294.
21. Kunkel TA, Roberts JD, Zakour RA. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol 154:367-382.
22. Lai Z, Colon W, Kelly JW. 1996. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. Biochemistry 35:6470-6482.
23. LeVine H. 1995. Thioflavine T interaction with amyloid β-sheet structures. Amyloid Int J Exp Clin Invest 2:1-6.
24. Linke RP, Zucker-Franklin D, Franklin EC. 1973. Morphologic, chemical, and immunologic studies of amyloid-like fibrils formed from Bence Jones proteins by proteolysis. J Immunol 111:10-23.
25. Naiki H, Higuchi K, Hosokawa M, Takeda T. 1989. Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye. Thioflavine T. Anal Biochem 177:244-249.
26. Ohage EC, Graml W, Walter M, Steinbacher S, Steipe B. 1997. β-Turn propensities as paradigms for the analysis of structural motifs to engineer protein stability. Protein Sci 6:233-241.
27. Raffen R, Wilkins Stevens P, Boogaard C, Schiffer M, Stevens FJ. 1998. Reengineering immunoglobulin domain interactions by introduction of charged residues. Protein Eng 11:303-309.
28. Rodilla-Sala E, Kratzin HD, Pick AI, Hilschmann N. 1990. Biclonality in patient MAL: One clone producing an amyloidogenic, the other a non-amyloidogenic kappa L-chain. In: Nativig JB, Forre O, Husby G, Husebekk A, Skogen B, Sletten K, Westermark P, eds. Amyloid and amyloidosis 1990. Dordrecht: Kluwer Academic Publishers, pp 161-164.
29. Sanger F, Coulson AR. 1975. A rapid method for determining sequences in DNA by primed synthesis with DNA polymerase. J Mol Biol 94:441-448.
30. Santoro MM, Bolen DW. 1988. Unfolding free energy changes determined by the linear extrapolation method. I. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry 27:8063-8074.
31. Schormann N, Murrell JR, Liepnieks JJ, Benson MD. 1995. Tertiary structure of an amyloid immunoglobulin light chain protein. A proposed model for amyloid fibril formation. Proc Natl Acad Sci USA 92:9490-9494.
32. Shortle D. 1995. Staphylococcal nuclease: A showcase of m-value effects. Adv Protein Chem 46:217-247.
33. Sipe J. 1992. Amyloidosis. Annu Rev Biochem 61:947-975.
34. Solomon A, Weiss DT, Murphy CL, Hmcic R, Wall J. 1998. Light chain-associated amyloid deposits comprised of a novel κ constant domain. Proc Natl Acad Sci USA 95:9547-9551.
35. Soulages JL. 1998. Chemical denaturation: Potential impact of undetected intermediates in the free energy of unfolding and m-values obtained from a two-state assumption. Biophys J 75:484-492.
36. Speed MA, Wang DIC, King J. 1996. Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition. Nat Biotechnol 14:1283-1287.
37. Stevens FJ, Myatt EA, Westholm FA, Weiss, D, Solomon A, Schiffer M. 1995. A molecular model for the formation of amyloid: Immunoglobulin light chains. Biochemistry 34:10697-10702.
38. Stevens FJ, Weiss DT, Solomon A. 1999 Structural basis of light chain-related pathology. In: Zanett M, Copra JD, eds. The antibodies, vol 5. Amsterdam: Harwood Academic Publishers. Forthcoming.
39. Stokes MB, Jagirdar J, Burchstin O, Komacki S, Kumar A, Gallo G. 1997. Nodular pulmonary immunoglobulin light chain deposits with coexistent amyloid and nonamyloid features in an HIV-infected patient. Modern Pathol 10:1059-1065.
40. Stone WJ. 1990. Amyloidosis: A final common pathway for protein deposition in tissues. Blood 75:531-545.
41. Tan M, Epstein W. 1972. Polymer formation during the degradation of human light chain and Bence-Jones proteins by an extract of the lysosomal fraction of normal human kidney. Immunochemistry 9:9-16.
42. Tanford C. 1968. Protein denaturation. Adv Protein Chem 23:121-282.
43. Vieira J, Messing J. 1982. The Puc plasmids, an M13Mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene 19:259-268.
44. Vogelgesang SA, Klipple GL. 1994. The many guises of amyloidosis: Clinical presentations and disease associations. Postgrad Med J 96:119-127.
45. Wetzel R. 1992. Protein aggregation in vivo. Bacterial inclusion bodies and mammalian amyloid. In: Ahern TJ, Manning MC. eds. Stability of protein pharmaceutical. Part B. In vivo pathways of degradation and strategies for protein stabilization. New York: Plenum Press, pp 43-88.
46. Wetzel R. 1994. Mutations and off-pathway aggregation of proteins. Trends Biotechnol 12:193-198.
47. Wetzel R. 1997. Domain stability in immunoglobulin light chain deposition disorders. Adv Protein Chem 50:183-242.
48. Wilkins Stevens P, Raffen R, Hanson DK, Deng Y-L, Berrios-Hammond M, Westholm FA, Murphy C, Eulitz M, Wetzel R, Solomon A, Schiffer M, Stevens FJ. 1995. Recombinant immunoglobulin variable domains generated from synthetic genes provide a system for in vitro characterization of light chain amyloid proteins. Protein Sci 4:421-432.
49. H in single-chain antibody fragments, investigated with mutants engineered for stability. Biochemistry 37:13120-13127.