A structure-function study of a catalytic antiidiotypic antibody to the human erythrocyte acetyl cholinesterase

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

1 Citation (Scopus)

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 × 109 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 languageEnglish (US)
Pages (from-to)124-125
Number of pages2
JournalBioorganicheskaya Khimiya
Volume28
Issue number2
StatePublished - 2002
Externally publishedYes

Fingerprint

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

Keywords

  • Abzymes of acetyl cholinesterase
  • Antiidiotypic antibodies
  • Phosphonates
  • Surface plasmon resonance

ASJC Scopus subject areas

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

Cite this

Aleksandrova, E. S., Koralevski, F., Titov, M. I., Demin, A. V., Kozyr, A. V., Kolesnikov, A. V., ... Friboulet, A. (2002). A structure-function study of a catalytic antiidiotypic antibody to the human erythrocyte acetyl cholinesterase. Bioorganicheskaya Khimiya, 28(2), 124-125.

A structure-function study of a catalytic antiidiotypic antibody to the human erythrocyte acetyl cholinesterase. / 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: Bioorganicheskaya Khimiya, Vol. 28, No. 2, 2002, p. 124-125.

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, 'A structure-function study of a catalytic antiidiotypic antibody to the human erythrocyte acetyl cholinesterase', Bioorganicheskaya Khimiya, vol. 28, no. 2, pp. 124-125.
Aleksandrova ES, Koralevski F, Titov MI, Demin AV, Kozyr AV, Kolesnikov AV et al. A structure-function study of a catalytic antiidiotypic antibody to the human erythrocyte acetyl cholinesterase. Bioorganicheskaya Khimiya. 2002;28(2):124-125.
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. / A structure-function study of a catalytic antiidiotypic antibody to the human erythrocyte acetyl cholinesterase. In: Bioorganicheskaya Khimiya. 2002 ; Vol. 28, No. 2. pp. 124-125.
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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 × 109 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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T1 - A structure-function study of a catalytic antiidiotypic antibody to the human erythrocyte acetyl cholinesterase

AU - Aleksandrova, E. S.

AU - Koralevski, F.

AU - Titov, M. I.

AU - Demin, A. V.

AU - Kozyr, A. V.

AU - Kolesnikov, A. V.

AU - Tramontano, A.

AU - Paul, S.

AU - Thomas, D.

AU - Gabibov, A. G.

AU - Gnuchev, N. V.

AU - Friboulet, A.

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AB - 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 × 109 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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