Enzyme mimicry by the antiidiotypic antibody approach

Kolesnikov, Alexander V.; Kozyr, A. V.; Alexandrova, Elena S.; Koralewski, F.; Демин, А. В.; Титов, М. И.; Avalle, Bérangère; Tramontano, Alfonso; Paul, Sudhir; Thomas, Daniel; Gabibov, Alexander; Friboulet, Alain

doi:10.1073/pnas.200360497

Cited by 110 publications

(76 citation statements)

References 36 publications

(46 reference statements)

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“…The remarkable property of idiotypic mimicry has been exploited to develop anti-idiotypic Abzs; monoclonal Abs were selected by immunizing mice with a monoclonal Ab against the active center of acetylcholinesterase, and a monoclonal anti-idiotypic Ab against carboxypeptidase showed catalytic activity similar to the original antigen [41,42]. Anti-idiotypic DNase Abs were obtained by immunization of rabbits with DNAse I [43].…”

Section: The Origin Of Natural Autoimmune Abzymesmentioning

confidence: 99%

Catalytic antibodies in healthy humans and patients with autoimmune and viral diseases

Nevinsky

Buneva

2003

J Cellular Molecular Medi

126

404

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Antibodies have been first characterized as proteins produced by the immune system solely for binding other molecules, called antigens, with the goal of eliciting immune response. In this classical conception, antibodies act similarly to enzymes in specific binding to different molecules but cannot catalyze their chemical conversion. However, in 1986 the first monoclonal catalytic antibodies against a chemically stable analog of the transition state of a reaction were obtained and termed abzymes (Abzs). At present, artificial monoclonal Abzs catalyzing more than 100 distinct chemical reactions have been obtained. The discovery of IgG specifically hydrolyzing intestinal vasoactive peptide in the blood serum of asthma patients stimulated studies of natural Abzs. Numerous Abzs discovered afterwards in sera of patients with various autoimmune diseases, viral disorders, or in the milk of healthy mothers, are capable of hydrolyzing proteins, DNA, RNA, polysaccharides, or nucleotides, as well as to phosphorylate proteins and lipids. The phenomenon of catalysis by auto-Abzs is more and more in research focus. In this review we summarize new data on Abzs applications in basic science, medicine and biotechnology.

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Section: The Origin Of Natural Autoimmune Abzymesmentioning

confidence: 99%

Catalytic antibodies in healthy humans and patients with autoimmune and viral diseases

Nevinsky

Buneva

2003

J Cellular Molecular Medi

126

404

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“…At the same time, some antiidiotypic Abs against active centers of many enzymes are also catalytically active [8,[12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27][28]. Healthy humans do more often not demonstrate catalytic Abs or their activities are extremely low.…”

Section: Introductionmentioning

confidence: 99%

“…Immunization of autoimmune-prone MRL-lpr/lpr mice with DNA-protein complexes also results in significantly higher production of anti-DNA Abs and abzymes with DNase activity comparing with nonautoimmune CBA and BALB/c healthy mice [29][30][31]. At the same time, artificial antiidiotypic abzymes can be induced by immunization of animals with different enzymes [23][24][25][26][27][28]. It was first suggested that natural SLE DNase Abzs may be antiidiotypic abzymes to topoisomerase I [53].…”

Section: Introductionmentioning

confidence: 99%

Catalytic Antibodies in Norm and Systemic Lupus Erythematosus

Nevinsky¹

2017

Lupus

321

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Systemic lupus erythematosus (SLE) is known as a systemic polyethiologic diffuse autoimmune disease characterized by connective tissue disorganization and the paramount damage of skin and visceral capillaries. Usually, SLE symptoms include high fever, hair loss, mouth ulcers, chest pain, swollen lymph nodes, painful and swollen joints, increased fatigue, and appearance of red rash more often on the face. The exact reason of SLE appearance is not really clear. Detection of catalytic Abs (abzymes) was shown to be the earliest indicator of different AI disease development. Some abzymes are cytotoxic and can play a dangerous negative role in the pathogenesis of AI diseases. SLE is characterized by the appearance of abzymes with several different catalytic functions including hydrolysis of peptides and proteins, DNA, RNA, and oligosaccharides. In addition, monoclonal SLE abzymes are characterized by extraordinary diversity in the affinity to the substrates, physicochemical and catalytic characteristics, optimal conditions of catalysis, cytotoxicity, etc. Production of abzymes in SLE mice is associated with changes in the differentiation of hematopoietic stem cells of bone marrow, increase in lymphocyte proliferation, and significant suppression of cell apoptosis in different organs. In this chapter, abzymes with different catalytic activities in SLE are described.

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“…Many authors have reported the presence of typical serine proteases like catalytic triad (Ser-His-Asp) in the catalytic Abs (Kolesnikov et al, 2000;Tramontano et al, 2000). Apart from this, recently, Ramsland et al (2006) has shown the presence of an atypical catalytic site in the Yvo IgM Abs, isolated form Waldenstrom's macroglobulinaemia.…”

Section: Investigation Of the Catalytic Site Histidine By Affinity Lamentioning

confidence: 99%

Proteolysis activity of IgM antibodies from rheumatoid arthritis patients' sera: evidence of atypical catalytic site

Kamalanathan

Goulvestre²,

Weill³

et al. 2010

J of Molecular Recognition

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The IgM antibodies from rheumatoid arthritis (RA) patients' sera were screened for peptide hydrolyzing activity. Recovery of structurally intact IgM antibodies (Abs), in a single step, was achieved using a weak anion-exchange methacrylate monolith disk. The IgM Abs from patients' sera hydrolyzed the Pro-Phe-Arg-4-methyl-coumaryl-7-amide (PFR-MCA) substrate appreciably compared to the healthy donors. The apparent K m values of IgM Abs from patients' sera were between 0.4 and 0.7 mM. Furthermore, IgM Abs displayed 5 to 10-folds greater proteolysis activity than IgG Abs, recovered from the same pathological serum. The proteolysis activity, as a function, was found to be independent of IgM-RF titer value. Affinity labeling approach targeted at the catalytic site histidine was studied, using a specific irreversible inhibitor, N-a-tosyl-L-lysine chloromethyl ketone (TLCK). Despite modification of catalytic His, observation of serine protease like activity suggest presence of an atypical catalytic framework in a few pathological IgM Abs.

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Enzyme mimicry by the antiidiotypic antibody approach

Cited by 110 publications

References 36 publications

Catalytic antibodies in healthy humans and patients with autoimmune and viral diseases

Catalytic antibodies in healthy humans and patients with autoimmune and viral diseases

Catalytic Antibodies in Norm and Systemic Lupus Erythematosus

Proteolysis activity of IgM antibodies from rheumatoid arthritis patients' sera: evidence of atypical catalytic site

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