Molecular mimicry of the receptor-binding domain of the SARS-CoV-2 spike protein: from the interaction of spike-specific antibodies with transferrin and lactoferrin to the antiviral effects of human recombinant lactoferrin

Autor: A. V. Sokolov, I. N. Isakova-Sivak, D. A. Mezhenskaya, V. A. Kostevich, N. P. Gorbunov, A. Yu. Elizarova, V. A. Matyushenko, Yu. M. Berson, N. A. Grudinina, N. N. Kolmakov, Y. A. Zabrodskaya, A. S. Komlev, I. V. Semak, A. I. Budevich, L. G. Rudenko, V. B. Vasilyev
Rok vydání: 2022
Předmět:
Zdroj: Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine.
ISSN: 1572-8773
Popis: The pathogenesis of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection involves dysregulations of iron metabolism, and although the mechanism of this pathology is not yet fully understood, correction of iron metabolism pathways seems a promising pharmacological target. The previously observed effect of inhibiting SARS-CoV-2 infection by ferristatin II, an inducer of transferrin receptor 1 (TfR1) degradation, prompted the study of competition between Spike protein and TfR1 ligands, especially lactoferrin (Lf) and transferrin (Tf). We hypothesized molecular mimicry of Spike protein as cross-reactivity of Spike-specific antibodies with Tf and Lf. Thus, strong positive correlations (R
Databáze: OpenAIRE