Strukturno-funktsional'noe issledovanie kataliticheskogo antiidiotipicheskogo antitela k atsetilkholinésteraze éritrotsitov cheloveka.

Translated title of the contribution: A structure-activity study of a catalytic antiidiotypic antibody to the human erythrocyte acetylcholinesterase

E. S. Aleksandrova, F. Koralevski, M. I. Titov, A. V. Demin, A. V. Kozyr', A. V. Kolesnikov, A. Tramontano, S. Paul, D. Thomas, A. G. Gabibov, N. V. Gnuchev, A. Friboulet

Research output: Contribution to journalArticle

Abstract

The catalytic monoclonal antibody 9A8 (MA 9A8), antiidiotypic to the antibody AE-2 (MA AE2) produced to the active site of acetyl cholinesterase from human erythrocytes, was subjected to a structure-function study. The specific binding of MA 9A8 to MA AE2 (K 2.26 x 10(9) M-1) was shown by the method of surface plasmon resonance, and the functional activity of MA 9A8 was demonstrated. Unlike acetyl cholinesterase, this antibody specifically reacted with the irreversible phosphonate inhibitors of esterases. A peptide map of MA 9A8 was analyzed by MALDI mass spectrometry. The Ser99 residue of its heavy chain was shown to be within the active site of the catalytic antibody. A computer modeling of the MA 9A8 active site suggested the existence of a catalytic dyad formed by Ser99 and His35. A comparison of the tertiary structures of the MA 9A8 and the 17E8 monoclonal antibody, which also exhibited an esterase activity and was produced to the stable analogue of the reaction transition state, indicated a practically complete coincidence of the structures of their presumed active sites.

Original languageUndefined/Unknown
Pages (from-to)118-125
Number of pages8
JournalBioorganicheskaia khimiia
Volume28
Issue number2
StatePublished - Mar 2002
Externally publishedYes

Fingerprint

Catalytic Antibodies
Acetylcholinesterase
Erythrocytes
Monoclonal Antibodies
Catalytic Domain
Cholinesterases
Esterases
Organophosphonates
Surface Plasmon Resonance
Antibodies
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
Surface plasmon resonance
Mass spectrometry
Mass Spectrometry
Peptides

ASJC Scopus subject areas

  • Organic Chemistry
  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Aleksandrova, E. S., Koralevski, F., Titov, M. I., Demin, A. V., Kozyr', A. V., Kolesnikov, A. V., ... Friboulet, A. (2002). Strukturno-funktsional'noe issledovanie kataliticheskogo antiidiotipicheskogo antitela k atsetilkholinésteraze éritrotsitov cheloveka. Bioorganicheskaia khimiia, 28(2), 118-125.

Strukturno-funktsional'noe issledovanie kataliticheskogo antiidiotipicheskogo antitela k atsetilkholinésteraze éritrotsitov cheloveka. / Aleksandrova, E. S.; Koralevski, F.; Titov, M. I.; Demin, A. V.; Kozyr', A. V.; Kolesnikov, A. V.; Tramontano, A.; Paul, S.; Thomas, D.; Gabibov, A. G.; Gnuchev, N. V.; Friboulet, A.

In: Bioorganicheskaia khimiia, Vol. 28, No. 2, 03.2002, p. 118-125.

Research output: Contribution to journalArticle

Aleksandrova, ES, Koralevski, F, Titov, MI, Demin, AV, Kozyr', AV, Kolesnikov, AV, Tramontano, A, Paul, S, Thomas, D, Gabibov, AG, Gnuchev, NV & Friboulet, A 2002, 'Strukturno-funktsional'noe issledovanie kataliticheskogo antiidiotipicheskogo antitela k atsetilkholinésteraze éritrotsitov cheloveka.', Bioorganicheskaia khimiia, vol. 28, no. 2, pp. 118-125.
Aleksandrova ES, Koralevski F, Titov MI, Demin AV, Kozyr' AV, Kolesnikov AV et al. Strukturno-funktsional'noe issledovanie kataliticheskogo antiidiotipicheskogo antitela k atsetilkholinésteraze éritrotsitov cheloveka. Bioorganicheskaia khimiia. 2002 Mar;28(2):118-125.
Aleksandrova, E. S. ; Koralevski, F. ; Titov, M. I. ; Demin, A. V. ; Kozyr', A. V. ; Kolesnikov, A. V. ; Tramontano, A. ; Paul, S. ; Thomas, D. ; Gabibov, A. G. ; Gnuchev, N. V. ; Friboulet, A. / Strukturno-funktsional'noe issledovanie kataliticheskogo antiidiotipicheskogo antitela k atsetilkholinésteraze éritrotsitov cheloveka. In: Bioorganicheskaia khimiia. 2002 ; Vol. 28, No. 2. pp. 118-125.
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abstract = "The catalytic monoclonal antibody 9A8 (MA 9A8), antiidiotypic to the antibody AE-2 (MA AE2) produced to the active site of acetyl cholinesterase from human erythrocytes, was subjected to a structure-function study. The specific binding of MA 9A8 to MA AE2 (K 2.26 x 10(9) M-1) was shown by the method of surface plasmon resonance, and the functional activity of MA 9A8 was demonstrated. Unlike acetyl cholinesterase, this antibody specifically reacted with the irreversible phosphonate inhibitors of esterases. A peptide map of MA 9A8 was analyzed by MALDI mass spectrometry. The Ser99 residue of its heavy chain was shown to be within the active site of the catalytic antibody. A computer modeling of the MA 9A8 active site suggested the existence of a catalytic dyad formed by Ser99 and His35. A comparison of the tertiary structures of the MA 9A8 and the 17E8 monoclonal antibody, which also exhibited an esterase activity and was produced to the stable analogue of the reaction transition state, indicated a practically complete coincidence of the structures of their presumed active sites.",
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AU - Titov, M. I.

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AU - Kolesnikov, A. V.

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AU - Paul, S.

AU - Thomas, D.

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