Медицинская иммунология (Jan 2024)

Features of ragweed pollen effect on humans in terms of peptidomics

  • U. V. Yanchenko,
  • N. S. Alyahnovich,
  • O. E. Semernick,
  • A. A. Lebedenko

DOI
https://doi.org/10.15789/1563-0625-TFO-2596
Journal volume & issue
Vol. 26, no. 1
pp. 151 – 158

Abstract

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The E antigen of Ambrosia artemisiifolia (Amb a1) is the most potent ragweed allergen. In 97% of patients with ragweed pollen allergy, IgE antibodies to the Amb a1 are detected in blood serum, being associated with a positive skin prick test for the Amb a 1 allergen. In humans, the tryptase alpha/beta 1 (TPSAB1) enzyme is simultaneously released from mast cells resulting from contact of sensitized person with this allergen. Absence of tryptase inhibitor in humans is the typical feature of this enzyme. We have attempted to determine the most significant points of TPSAB1effects after its splitting into peptide fragments. Peptidase cleavage was carried out using the Bioscan 9.14 computer program ODO NICP Resan (Belarus), and the US National Center for Biotechnology Information (NCBI) database. The international one-letter amino acid sequence code was used for calculations and presentation of results. The data on peptide interactions with human proteins were obtained using the SwissTargetPrediction program. The test specimen was as follows: Ambrosia artemisiifolia antigen E (Amb a1) GenBank: AAA32665.1. Cleavage of the sample was carried out from position 1 to the last amino acid (No. 396). The length of split fragments is not specified. The studied enzyme was Homo sapiens tryptase alpha/beta 1 (TPSAB1) Gene ID: 7177, updated: 13-May-2022; enzyme type: endopeptidase. Split positions: 1 r|x and 2 k|x. The following amino acid sequence was analyzed: Ambrosia artemisiifolia antigen E (Amb a1) GenBank: AAA32665.1. It has been found that the E antigen from Ambrosia artemisiifolia (Amb a1) contains 396 amino acid residues. The 40 peptide fragments of the split sample were obtained. The ligand-receptor interaction was analyzed for peptides with a length of 2 to 4 amino acid residues, which had the strongest regulatory potential (p1-4 mgik, p56-57 gk, p127-129 ldk, p143-145 gak, p274-276 mpr). It has been shown that each peptide from the Amb a1 sequence acts as a ligand for specific receptors mediating the effects upon certain mechanisms in the patient’s body. Further study of these interactions enables identification of the most significant proteins (enzymes), which, upon impact of E antigen from Ambrosia artemisiifolia (Amb a 1) may lead to changed functional activity of regulatory systems in humans suffering from allergies.

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