Physiological IgM class catalytic antibodies selective for transthyretin amyloid

Journal of Biological Chemistry

Volumn 289, Issue 19, 2014, Pages 13243-13258

  Planque, Stephanie A ^a   Nishiyama, Yasuhiro ^a   Hara, Mariko ^a   Sonoda, Sari ^a   Murphy, Sarah K ^a   Watanabe, Kenji ^a   Mitsuda, Yukie ^a   Brown, Eric L ^b   Massey, Richard J ^c   Primmer, Stanley R ^d   O'Nuallain, Brian ^e   Paul, Sudhir ^a  

^a UNIVERSITY OF TEXAS MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF TEXAS SCHOOL OF PUBLIC HEALTH   (United States)

^c Covalent Bioscience Inc ^*  (United States)

^d Supercentenarian Research Foundation   (United States)

^e HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DISEASES; GLYCOPROTEINS; HYDROLYSIS; PEPTIDES; PHYSIOLOGY;

CATALYTIC ANTIBODIES; HEALTHY HUMANS; HYDROLYTIC ACTIVITIES; IMMUNE FUNCTION; SHEET AGGREGATES; SUPERANTIGEN; TOXIC PROTEINS; TRANSTHYRETIN;

ANTIBODIES;

AMYLOID BETA PROTEIN; B LYMPHOCYTE RECEPTOR; CATALYTIC ANTIBODY; GLYCOPROTEIN GP 120; IMMUNOGLOBULIN M ANTIBODY; PREALBUMIN; SUPERANTIGEN; SUPERANTIGEN PROTEIN A; UNCLASSIFIED DRUG;

ADULT; AMYLOIDOSIS; ANTIGEN BINDING; ARTICLE; BETA SHEET; CONTROLLED STUDY; ELECTROPHILICITY; FEMALE; HUMAN; HUMAN CELL; HYDROLYSIS; MALE; NUCLEOPHILICITY; NUCLEOTIDE SEQUENCE; PHAGOCYTOSIS; PRIORITY JOURNAL; PROTEIN FUNCTION;

AGING; AMYLOID; AMYLOIDOSIS; ANTIBODIES; CATALYTIC ANTIBODY; INNATE IMMUNITY; PROTEIN EVOLUTION; SUPERANTIGEN; TRANSTHYRETIN;

ADULT; AMYLOID; ANTIBODIES, CATALYTIC; ANTIBODY SPECIFICITY; FEMALE; HUMANS; IMMUNOGLOBULIN M; MALE; PREALBUMIN; PROTEOLYSIS;

EID: 84900460402     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.557231     Document Type: Article

References (100)

1. Planque, S., Bangale, Y., Song, X. T., Karle, S., Taguchi, H., Poindexter, B., Bick, R., Edmundson, A., Nishiyama, Y., and Paul, S. (2004) Ontogeny of proteolytic immunity: IgM serine proteases. J. Biol. Chem. 279, 14024-14032
2. Paul, S., Karle, S., Planque, S., Taguchi, H., Salas, M., Nishiyama, Y., Handy, B., Hunter, R., Edmundson, A., and Hanson, C. (2004) Naturally occurring proteolytic antibodies: selective immunoglobulin M-catalyzed hydrolysis of HIV gp120. J. Biol. Chem. 279, 39611-39619
3. Gololobov, G., Sun, M., and Paul, S. (1999) Innate antibody catalysis. Mol. Immunol. 36, 1215-1222
4. Sharma, V., Heriot, W., Trisler, K., and Smider, V. (2009) A human germ line antibody light chain with hydrolytic properties associated with multimerization status. J. Biol. Chem. 284, 33079-33087
5. Hifumi, E., Honjo, E., Fujimoto, N., Arakawa, M., Nishizono, A., and Uda, T. (2012) Highly efficient method of preparing human catalytic antibody light chains and their biological characteristics. FASEB J. 26, 1607-1615
6. Le Minoux, D., Mahendra, A., Kaveri, S., Limnios, N., Friboulet, A., Avalle, B., Boquet, D., Lacroix-Desmazes, S., and Padiolleau-Lefèvre, S. (2012) A novel molecular analysis of genes encoding catalytic antibodies. Mol. Immunol. 50, 160-168
7. Taguchi, H., Planque, S., Nishiyama, Y., Symersky, J., Boivin, S., Szabo, P., Friedland, R. P., Ramsland, P. A., Edmundson, A. B., Weksler, M. E., and Paul, S. (2008) Autoantibody-catalyzed hydrolysis of amyloid βpeptide. J. Biol. Chem. 283, 4714-4722
8. Paul, S., Planque, S. A., Nishiyama, Y., Hanson, C. V., and Massey, R. J. (2012) Nature and nurture of catalytic antibodies. Adv. Exp. Med. Biol. 750, 56-75
9. Paul, S., Volle, D. J., Beach, C. M., Johnson, D. R., Powell, M. J., and Massey, R. J. (1989) Catalytic hydrolysis of vasoactive intestinal peptide by human autoantibody. Science 244, 1158-1162
10. Shuster, A. M., Gololobov, G. V., Kvashuk, O. A., Bogomolova, A. E., Smirnov, I. V., and Gabibov, A. G. (1992) DNAhy drolyzing autoantibodies. Science 256, 665-667
11. Buxbaum, J. N. (2003) Diseases of protein conformation: what do in vitro experiments tell us about in vivo diseases? Trends Biochem. Sci. 28, 585-592
12. Buxbaum, J. N., and Reixach, N. (2009) Transthyretin: the servant of many masters. Cell Mol. Life Sci. 66, 3095-3101
13. Takeuchi, M., Mizuguchi, M., Kouno, T., Shinohara, Y., Aizawa, T., Demura, M., Mori, Y., Shinoda, H., and Kawano, K. (2007) Destabilization of transthyretin by pathogenic mutations in the DE loop. Proteins 66, 716-725
14. Quintas, A., Vaz, D. C., Cardoso, I., Saraiva, M. J., and Brito, R. M. (2001) Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants. J. Biol. Chem. 276, 27207-27213
15. Hurshman, A. R., White, J. T., Powers, E. T., and Kelly, J. W. (2004) Transthyretin aggregation under partially denaturing conditions is a downhill polymerization. Biochemistry 43, 7365-7381
16. Kingsbury, J. S., Laue, T. M., Chase, S. F., and Connors, L. H. (2012) Detection of high-molecular-weight amyloid serum protein complexes using biological on-line tracer sedimentation. Anal. Biochem. 425, 151-156
17. Sueyoshi, T., Ueda, M., Jono, H., Irie, H., Sei, A., Ide, J., Ando, Y., and Mizuta, H. (2011) Wild-type transthyretin-derived amyloidosis in various ligaments and tendons. Hum. Pathol. 42, 1259-1264
18. Pepys, M. B. (2006) Amyloidosis. Annu. Rev. Med. 57, 223-241
19. Westermark, P., Bergström, J., Solomon, A., Murphy, C., and Sletten, K. (2003) Transthyretin-derived senile systemic amyloidosis: clinicopathologic and structural considerations. Amyloid 10, 48-54
20. Teixeira, P. F., Cerca, F., Santos, S. D., and Saraiva, M. J. (2006) Endoplasmic reticulum stress associated with extracellular aggregates. Evidence from transthyretin deposition in familial amyloid polyneuropathy. J. Biol. Chem. 281, 21998-22003
21. Connors, L. H., Lim, A., Prokaeva, T., Roskens, V. A., and Costello, C. E. (2003) Tabulation of human transthyretin (TTR) variants. Amyloid 10, 160-184
22. Coelho, T., Adams, D., Silva, A., Lozeron, P., Hawkins, P. N., Mant, T., Perez, J., Chiesa, J., Warrington, S., Tranter, E., Munisamy, M., Falzone, R., Harrop, J., Cehelsky, J., Bettencourt, B. R., Geissler, M., Butler, J. S., Sehgal, A., Meyers, R. E., Chen, Q., Borland, T., Hutabarat, R. M., Clausen, V. A., Alvarez, R., Fitzgerald, K., Gamba-Vitalo, C., Nochur, S. V., Vaishnaw, A. K., Sah, D. W., Gollob, J. A., and Suhr, O. B. (2013) Safety and efficacy of RNAi therapy for transthyretin amyloidosis. N. Engl. J. Med. 369, 819-829
23. Coelho, T., Maia, L. F., Martins Da Silva, A., Waddington Cruz, M., Planté-Bordeneuve, V., Lozeron, P., Suhr, O. B., Campistol, J. M., Conceição, I. M., Schmidt, H. H., Trigo, P., Kelly, J. W., Labaudinière, R., Chan, J., Packman, J., Wilson, A., and Grogan, D. R. (2012) Tafamidis for transthyretin familial amyloid polyneuropathy: a randomized, controlled trial. Neurology 79, 785-792
24. Salloway, S., Sperling, R., Fox, N. C., Blennow, K., Klunk, W., Raskind, M., Sabbagh, M., Honig, L. S., Porsteinsson, A. P., Ferris, S., Reichert, M., Ketter, N., Nejadnik, B., Guenzler, V., Miloslavsky, M., Wang, D., Lu, Y., Lull, J., Tudor, I. C., Liu, E., Grundman, M., Yuen, E., Black, R., and Brashear, H. R. (2014) Two phase 3 trials of bapineuzumab in mild-tomoderate Alzheimer's disease. N. Engl. J. Med. 370, 322-333
25. Su, Y., Jono, H., Torikai, M., Hosoi, A., Soejima, K., Guo, J., Tasaki, M., Misumi, Y., Ueda, M., Shinriki, S., Shono, M., Obayashi, K., Nakashima, T., Sugawara, K., and Ando, Y. (2012) Antibody therapy for familial amyloidotic polyneuropathy. Amyloid 19, 45-46
26. Lindström, V., Ihse, E., Fagerqvist, T., Bergström, J., Nordström, E., Möller, C., Lannfelt, L., and Ingelsson, M. (2014) Immunotherapy targeting α-synuclein, with relevance for future treatment of Parkinson's disease and other Lewy body disorders. Immunotherapy 6, 141-153
27. Mitsuda, Y., Planque, S., Hara, M., Kyle, R., Taguchi, H., Nishiyama, Y., and Paul, S. (2007) Naturally occurring catalytic antibodies: evidence for preferred development of the catalytic function in IgA class antibodies. Mol. Biotechnol. 36, 113-122
28. Sapparapu, G., Planque, S., Mitsuda, Y., McLean, G., Nishiyama, Y., and Paul, S. (2012) Constant domain-regulated antibody catalysis. J. Biol. Chem. 287, 36096-36104
29. Taguchi, H., Planque, S., Sapparapu, G., Boivin, S., Hara, M., Nishiyama, Y., and Paul, S. (2008) Exceptional amyloid βpeptide hydrolyzing activity of nonphysiological immunoglobulin variable domain scaffolds. J. Biol. Chem. 283, 36724-36733
30. Lundberg, E., Olofsson, A., Westermark, G. T., and Sauer-Eriksson, A. E. (2009) Stability and fibril formation properties of human and fish transthyretin, and of the Escherichia coli transthyretin-related protein. FEBS J. 276, 1999-2011
31. Yang, D. T., Joshi, G., Cho, P. Y., Johnson, J. A., and Murphy, R. M. (2013) Transthyretin as both a sensor and a scavenger of β-Amyloid oligomers. Biochemistry 52, 2849-2861
32. Xia, K., Zhang, S., Bathrick, B., Liu, S., Garcia, Y., and Colón, W. (2012) Quantifying the kinetic stability of hyperstable proteins via time-dependent SDS trapping. Biochemistry 51, 100-107
33. Paul, S., Planque, S., Zhou, Y. X., Taguchi, H., Bhatia, G., Karle, S., Hanson, C., and Nishiyama, Y. (2003) Specific HIV gp120-cleaving antibodies induced by covalently reactive analog of gp120. J. Biol. Chem. 278, 20429-20435
34. Beynon, R. J., and Salvesen, G. S. (2001) in Proteolytic Enzymes: A Practical Approach, 2nd Ed. (Beynon, R. J., and Bond, J. S., eds) pp. 317-330, Oxford University Press, Oxford, UK
35. Paul, S., Tramontano, A., Gololobov, G., Zhou, Y. X., Taguchi, H., Karle, S., Nishiyama, Y., Planque, S., and George, S. (2001) Phosphonate ester probes for proteolytic antibodies. J. Biol. Chem. 276, 28314-28320
36. Sousa, M. M., Do Amaral, J. B., Guimarães, A., and Saraiva, M. J. (2005) Up-regulation of the extracellular matrix remodeling genes, biglycan, neutrophil gelatinase-Associated lipocalin, and matrix metalloproteinase-9 in familial amyloid polyneuropathy. FASEB J. 19, 124-126
37. Mody, R., Tramontano, A., and Paul, S. (1994) Spontaneous hydrolysis of vasoactive intestinal peptide in neutral aqueous solution. Int. J. Pept. Protein Res. 44, 441-447
38. Reixach, N., Deechongkit, S., Jiang, X., Kelly, J. W., and Buxbaum, J. N. (2004) Tissue damage in the amyloidoses: transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture. Proc. Natl. Acad. Sci. U. S. A. 101, 2817-2822
39. Sörgjerd, K., Klingstedt, T., Lindgren, M., Kågedal, K., and Hammarström, P. (2008) Prefibrillar transthyretin oligomers and cold stored native tetrameric transthyretin are cytotoxic in cell culture. Biochem. Biophys. Res. Commun. 377, 1072-1078
40. Takeshita, S., Tokutomi, T., Kawase, H., Nakatani, K., Tsujimoto, H., Kawamura, Y., and Sekine, I. (2001) Elevated serum levels of matrix metalloproteinase-9 (MMP-9) in Kawasaki disease. Clin. Exp. Immunol. 125, 340-344
41. Chen, T. Y., Huang, C. C., and Tsao, C. J. (1993) Hemostatic molecular markers in nephrotic syndrome. Am. J. Hematol. 44, 276-279
42. Foguel, D., Suarez, M. C., Ferrão-Gonzales, A. D., Porto, T. C., Palmieri, L., Einsiedler, C. M., Andrade, L. R., Lashuel, H. A., Lansbury, P. T., Kelly, J. W., and Silva, J. L. (2003) Dissociation of amyloid fibrils of α-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities. Proc. Natl. Acad. Sci. U. S. A. 100, 9831-9836
43. Gao, Q. S., Sun, M., Rees, A. R., and Paul, S. (1995) Site-directed mutagenesis of proteolytic antibody light chain. J. Mol. Biol. 253, 658-664
44. Polosukhina, D. I., Kanyshkova, T. G., Doronin, B. M., Tyshkevich, O. B., Buneva, V. N., Boiko, A. N., Gusev, E. I., Nevinsky, G. A., and Favorova, O. O. (2006) Metal-dependent hydrolysis of myelin basic protein by IgGs from the sera of patients with multiple sclerosis. Immunol. Lett. 103, 75-81
45. Baranova, S. V., Buneva, V. N., Kharitonova, M. A., Sizyakina, L. P., Calmels, C., Andreola, M. L., Parissi, V., Zakharova, O. D., and Nevinsky, G. A. (2010) HIV-1 integrase-hydrolyzing IgM antibodies from sera of HIV-infected patients. Int. Immunol. 22, 671-680
46. Kalaga, R., Li, L., O'Dell, J. R., and Paul, S. (1995) Unexpected presence of polyreactive catalytic antibodies in IgG from unimmunized donors and decreased levels in rheumatoid arthritis. J. Immunol. 155, 2695-2702
47. Schurr, J. M., and McLaren, A. D. (1966) Enzyme action: comparison on soluble and insoluble substrate. Science 152, 1064-1066
48. Cruys-Bagger, N., Elmerdahl, J., Praestgaard, E., Borch, K., and Westh, P. (2013) A steady-state theory for processive cellulases. FEBS J. 280, 3952-3961
49. Paul, S., Volle, D. J., Powell, M. J., and Massey, R. J. (1990) Site specificity of a catalytic vasoactive intestinal peptide antibody. An inhibitory vasoactive intestinal peptide subsequence distant from the scissile peptide bond. J. Biol. Chem. 265, 11910-11913
50. Planque, S., Taguchi, H., Burr, G., Bhatia, G., Karle, S., Zhou, Y. X., Nishiyama, Y., and Paul, S. (2003) Broadly distributed chemical reactivity of natural antibodies expressed in coordination with specific antigen binding activity. J. Biol. Chem. 278, 20436-20443
51. Casali, P., and Schettino, E. W. (1996) Structure and function of natural antibodies. Curr. Top. Microbiol. Immunol. 210, 167-179
52. O'Nuallain, B., and Wetzel, R. (2002) Conformational Abs recognizing a generic amyloid fibril epitope. Proc. Natl. Acad. Sci. U. S. A. 99, 1485-1490
53. Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489
54. Graille, M., Stura, E. A., Corper, A. L., Sutton, B. J., Taussig, M. J., Charbonnier, J. B., and Silverman, G. J. (2000) Crystal structure of a Staphylococcus aureus protein A domain complexed with the Fab fragment of a human IgM antibody: structural basis for recognition of B-cell receptors and superantigen activity. Proc. Natl. Acad. Sci. U. S. A. 97, 5399-5404
55. Neshat, M. N., Goodglick, L., Lim, K., and Braun, J. (2000) Mapping the B cell superantigen binding site for HIV-1 gp120 on a V (H) 3 Ig. Int. Immunol. 12, 305-312
56. Goodyear, C. S., and Silverman, G. J. (2005) B cell superantigens: a microbe's answer to innate-like B cells and natural antibodies. Springer Semin. Immunopathol. 26, 463-484
57. Nishiyama, Y., Planque, S., Mitsuda, Y., Nitti, G., Taguchi, H., Jin, L., Symersky, J., Boivin, S., Sienczyk, M., Salas, M., Hanson, C. V., and Paul, S. (2009) Toward effective HIV vaccination: induction of binary epitope reactive antibodies with broad HIV neutralizing activity. J. Biol. Chem. 284, 30627-30642
58. Planque, S. A., Mitsuda, Y., Nishiyama, Y., Karle, S., Boivin, S., Salas, M., Morris, M. K., Hara, M., Liao, G., Massey, R. J., Hanson, C. V., and Paul, S. (2012) Antibodies to a superantigenic glycoprotein 120 epitope as the basis for developing an HIV vaccine. J. Immunol. 189, 5367-5381
59. Spencer, J., and Hall, J. G. (1984) The flow and composition of lymph from the caudal mediastinal lymph node of sheep. Immunology 52, 7-15
60. Rossing, N. (1978) Intra- and extravascular distribution of albumin and immunoglobulin in man. Lymphology 11, 138-142
61. Pilati, C. F. (1990) Macromolecular transport in canine coronary microvasculature. Am. J. Physiol. 258, H748-H753
62. Gomes, R., Sousa Silva, M., Quintas, A., Cordeiro, C., Freire, A., Pereira, P., Martins, A., Monteiro, E., Barroso, E., and Ponces Freire, A. (2005) Argpyrimidine, a methylglyoxal-derived advanced glycation end-product in familial amyloidotic polyneuropathy. Biochem. J. 385, 339-345
63. Liu, L., Komatsu, H., Murray, I. V., and Axelsen, P. H. (2008) Promotion of amyloid β protein misfolding and fibrillogenesis by a lipid oxidation product. J. Mol. Biol. 377, 1236-1250
64. Wang, X., and Stollar, B. D. (1999) Immunoglobulin VH gene expression in human aging. Clin. Immunol. 93, 132-142
65. Gibson, K. L., Wu, Y. C., Barnett, Y., Duggan, O., Vaughan, R., Kondeatis, E., Nilsson, B. O., Wikby, A., Kipling, D., and Dunn-Walters, D. K. (2009) B-cell diversity decreases in old age and is correlated with poor health status. Aging Cell 8, 18-25
66. Gavazzi, G., and Krause, K. H. (2002) Ageing and infection. Lancet Infect. Dis. 2, 659-666
67. Maas, A., Dingjan, G. M., Grosveld, F., and Hendriks, R. W. (1999) Early arrest in B cell development in transgenic mice that express the E41K Bruton's tyrosine kinase mutant under the control of the CD19 promoter region. J. Immunol. 162, 6526-6533
68. Conley, M. E., Dobbs, A. K., Farmer, D. M., Kilic, S., Paris, K., Grigoriadou, S., Coustan-Smith, E., Howard, V., and Campana, D. (2009) Primary B cell immunodeficiencies: comparisons and contrasts. Annu. Rev. Immunol. 27, 199-227
69. Liu, Y. H., Giunta, B., Zhou, H. D., Tan, J., and Wang, Y. J. (2012) Immunotherapy for Alzheimer disease: the challenge of adverse effects. Nat. Rev. Neurol. 8, 465-469
70. Pollack, S. J., Hsiun, P., and Schultz, P. G. (1989) Stereospecific hydrolysis of alkyl esters by antibodies. J. Am. Chem. Soc. 111, 5961-5962
71. Ramsland, P. A., Terzyan, S. S., Cloud, G., Bourne, C. R., Farrugia, W., Tribbick, G., Geysen, H. M., Moomaw, C. R., Slaughter, C. A., and Edmundson, A. B. (2006) Crystal structure of a glycosylated Fab from an IgM cryoglobulin with properties of a natural proteolytic antibody. Biochem. J. 395, 473-481
72. Janda, A., Eryilmaz, E., Nakouzi, A., Cowburn, D., and Casadevall, A. (2012) Variable region identical immunoglobulins differing in isotype express different paratopes. J. Biol. Chem. 287, 35409-35417
73. Haury, M., Sundblad, A., Grandien, A., Barreau, C., Coutinho, A., and Nobrega, A. (1997) The repertoire of serum IgM in normal mice is largely independent of external antigenic contact. Eur. J. Immunol. 27, 1557-1563
74. Köhler, F., Hug, E., Eschbach, C., Meixlsperger, S., Hobeika, E., Kofer, J., Wardemann, H., and Jumaa, H. (2008) Autoreactive B cell receptors mimic autonomous pre-B cell receptor signaling and induce proliferation of early B cells. Immunity 29, 912-921
75. Nissim, A., and Chernajovsky, Y. (2008) in Therapeutic Antibodies: Handbook of Experimental Pharmacology (Chernajovsky, Y., and Nissim, A., eds) pp. 3-18, Springer, Berlin
76. Ponomarenko, N. A., Durova, O. M., Vorobiev, I. I., Belogurov, A. A., Jr., Kurkova, I. N., Petrenko, A. G., Telegin, G. B., Suchkov, S. V., Kiselev, S. L., Lagarkova, M. A., Govorun, V. M., Serebryakova, M. V., Avalle, B., Tornatore, P., Karavanov, A., Morse, H. C., 3rd, Thomas, D., Friboulet, A., and Gabibov, A. G. (2006) Autoantibodies to myelin basic protein catalyze site-specific degradation of their antigen. Proc. Natl. Acad. Sci. U. S. A. 103, 281-286
77. Wootla, B., Dasgupta, S., Dimitrov, J. D., Bayry, J., Lévesque, H., Borg, J. Y., Borel-Derlon, A., Rao, D. N., Friboulet, A., Kaveri, S. V., and Lacroix-Desmazes, S. (2008) Factor VIII hydrolysis mediated by anti-factor VIII autoantibodies in acquired hemophilia. J. Immunol. 180, 7714-7720
78. Wootla, B., Christophe, O. D., Mahendra, A., Dimitrov, J. D., Repessé, Y., Ollivier, V., Friboulet, A., Borel-Derlon, A., Levesque, H., Borg, J. Y., Andre, S., Bayry, J., Calvez, T., Kaveri, S. V., and Lacroix-Desmazes, S. (2011) Proteolytic antibodies activate factor IX in patients with acquired hemophilia. Blood 117, 2257-2264
79. Andrievskaya, O. A., Buneva, V. N., Naumov, V. A., and Nevinsky, G. A. (2000) Catalytic heterogenity of polyclonal RNA-hydrolyzing IgM from sera of patients with lupus erythematosus. Med. Sci. Monit. 6, 460-470
80. Saveliev, A. N., Ivanen, D. R., Kulminskaya, A. A., Ershova, N. A., Kanyshkova, T. G., Buneva, V. N., Mogelnitskii, A. S., Doronin, B. M., Favorova, O. O., Nevinsky, G. A., and Neustroev, K. N. (2003) Amylolytic activity of IgM and IgG antibodies from patients with multiple sclerosis. Immunol. Lett. 86, 291-297
81. Gao, Q. S., Sun, M., Tyutyulkova, S., Webster, D., Rees, A., Tramontano, A., Massey, R. J., and Paul, S. (1994) Molecular cloning of a proteolytic antibody light chain. J. Biol. Chem. 269, 32389-32393
82. Uda, T., and Hifumi, E. (2004) Super catalytic antibody and antigenase. J. Biosci. Bioeng. 97, 143-152
83. Hifumi, E., Morihara, F., Hatiuchi, K., Okuda, T., Nishizono, A., and Uda, T. (2008) Catalytic features and eradication ability of antibody lightchain UA15-L against Helicobacter pylori. J. Biol. Chem. 283, 899-907
84. Coutinho, A., Kazatchkine, M. D., and Avrameas, S. (1995) Natural autoantibodies. Curr. Opin. Immunol. 7, 812-818
85. Bayry, J., Misra, N., Dasgupta, S., Lacroix-Desmazes, S., Kazatchkine, M. D., and Kaveri, S. V. (2005) Natural autoantibodies: immune homeostasis and therapeutic intervention. Expert Rev. Clin. Immunol. 1, 213-222
86. Kaveri, S. V. (2012) Intravenous immunoglobulin: exploiting the potential of natural antibodies. Autoimmun. Rev. 11, 792-794
87. Kohler, H., and Paul, S. (1998) Superantibody activities: new players in innate and adaptive immune responses. Immunol. Today 19, 221-227
88. Graille, M., Harrison, S., Crump, M. P., Findlow, S. C., Housden, N. G., Muller, B. H., Battail-Poirot, N., Sibä, G., Sutton, B. J., Taussig, M. J., Jolivet-Reynaud, C., Gore, M. G., and Stura, E. A. (2002) Evidence for plasticity and structural mimicry at the immunoglobulin light chainprotein L interface. J. Biol. Chem. 277, 47500-47506
89. Maftei, M., Thurm, F., Leirer, V. M., Von Arnim, C. A., Elbert, T., Przybylski, M., Kolassa, I. T., and Manea, M. (2012) Antigen-bound and free β-Amyloid autoantibodies in serum of healthy adults. PLoS One 7, e44516
90. Lesné, S. E., Sherman, M. A., Grant, M., Kuskowski, M., Schneider, J. A., Bennett, D. A., and Ashe, K. H. (2013) Brain amyloid-β oligomers in ageing and Alzheimer's disease. Brain 136, 1383-1398
91. Kalinin, S., Willard, S. L., Shively, C. A., Kaplan, J. R., Register, T. C., Jorgensen, M. J., Polak, P. E., Rubinstein, I., and Feinstein, D. L. (2013) Development of amyloid burden in African Green monkeys. Neurobiol. Aging 34, 2361-2369
92. Lane, T., Loeffler, J. M., Rowczenio, D. M., Gilbertson, J. A., Bybee, A., Russell, T. L., Gillmore, J. D., Wechalekar, A. D., Hawkins, P. N., and Lachmann, H. J. (2013) AA amyloidosis complicating the hereditary periodic fever syndromes. Arthritis Rheum. 65, 1116-1121
93. Abdallah, E., and Waked, E. (2013) Incidence and clinical outcome of renal amyloidosis: a retrospective study. Saudi J. Kidney Dis. Transpl. 24, 950-958
94. Calderón-Garciduenas, L., Franco-Lira, M., Mora-Tiscareño, A., Medina-Cortina, H., Torres-Jardón, R., and Kavanaugh, M. (2013) Early Alzheimer's and Parkinson's disease pathology in urban children: friend versus foe responses: it is time to face the evidence. Biomed. Res. Int. 2013, 161687
95. Millucci, L., Ghezzi, L., Bernardini, G., Braconi, D., Tanganelli, P., and Santucci, A. (2012) Prevalence of isolated atrial amyloidosis in young patients affected by congestive heart failure. Scientific World Journal 2012, 293863
96. Planque, S., Mitsuda, Y., Taguchi, H., Salas, M., Morris, M. K., Nishiyama, Y., Kyle, R., Okhuysen, P., Escobar, M., Hunter, R., Sheppard, H. W., Hanson, C., and Paul, S. (2007) Characterization of gp120 hydrolysis by IgA antibodies from humans without HIV infection. AIDS Res. Hum. Retroviruses 23, 1541-1554
97. Brown, E. L., Nishiyama, Y., Dunkle, J. W., Aggarwal, S., Planque, S., Watanabe, K., Csencsits-Smith, K., Bowden, M. G., Kaplan, S. L., and Paul, S. (2012) Constitutive production of catalytic antibodies to a Staphylococcus aureus virulence factor and effect of infection. J. Biol. Chem. 287, 9940-9951
98. Kreymann, K. G., De Heer, G., Nierhaus, A., and Kluge, S. (2007) Use of polyclonal immunoglobulins as adjunctive therapy for sepsis or septic shock. Crit. Care Med. 35, 2677-2685
99. Xu, H. J., Umapathysivam, K., McNeilage, J., Gordon, T. P., and Roberts-Thomson, P. J. (1992) An enhanced chemiluminescence detection system combined with a modified immunoblot technique for the detection of low molecular weight IgM in sera from healthy adults and neonates. J. Immunol. Methods 146, 241-247
100. Dooley, H., and Flajnik, M. F. (2006) Antibody repertoire development in cartilaginous fish. Dev. Comp. Immunol. 30, 43-56