Peptide containing the universal antigenic determinant of tryptophanyl-tRNA synthetases

T. A. Zargarova, A. A. Zargarov, I. A. Bolotina, S. F. Beresten, O. O. Favorova

V. A. Engelhardt Institute of Molecular Biology, Academy of Sciences of the USSR, Moscow; M. M. Shemyakin Institute of Bioorganic Chemistry, Academy of Sciences of the USSR, Moscow

Abstract: Among clostripain hydrolysate peptides of beef pancreas tryptophanyl-tRNA synthe-tase the peptide Ile-Ser-Phe-Pro-Ala-Ile-Asn-Gln-Phe-Ala-Ala-Pro-Ser-Gln-Phe-Ser-Ile-Arg •was revealed which contains the continuous antigenic determinant for monoclonal antibody Ami. This antibody specifically cross-reacts with tryptophanyl-tRNA synthetases of procaryotes, eucaryotes and archebacteriae. The synthetic peptide with identical amino acid sequence plus N-terminal Arg residue (S-peptide), being immobilized on enzyme immunoassay (EIA) microtitration plate, also binds with Ami. Ami affinity constant (M-1) measured by non-competitive EIA was (3.0+0.3)·107 for S peptide and (1.4±0.3)·109 for the native enzyme. The sequence of immunoreactive peptide adopts with high probability the secondary structure including β-turn(s) and antiparallel β-sheet composed of inverted repeats. At the same time, the analysis of circular dichroism spectrum |m the far UV) of the peptide dissolved in water comes closest to 16% (β-turn and only 8% β-sheet. The binding of Ami with peptide was not observed in aqueous solution.

Russian Journal of Bioorganic Chemistry 1990, 16 (9):1259-1267

Full Text (PDF, in Russian)