Function of lectins in the efficiency of ferritin nanoparticle vaccines

Introduction: Viral infections constitute a serious public health and social problem worldwide, especiallyduring the recent COVID-۱۹ pandemic caused by the betacoronavirus SARS-CoV-۲. Display of antigens onferritin generally elicits a more robust neutralizing antibody response against the target pathogen as comparedto immunization with the antigen alone. The ferritin-RBD nanoparticle vaccine induced not only a persistentRBD specific antibody response but also long-term protective memory. Because the ferritin nanoparticlevaccine uses glycosylated RBD (receptor binding domain) in its structure, it may be recognized and getsinefficient by human lectins. Lectins are glycan-binding proteins, present ubiquitously in all forms of life. Inthis study, molecular docking to examine the lectin binding site on the ferritin nanoparticle vaccine proteinused.Material & Methods: The lectin protein structure was obtained from the protein data bank (PDB id: ۵b۱w).haddock ۲.۴ server was used to dock the lectin and ferritin nanoparticle vaccine complex together andbiomolecular visualization of the complex was carried out by pymol.Results: The structure of the full length human lectin was obtained in complex with RBD-ferritinnanoparticle. Lectin (residues:۵۱-۶۴) binds close to the RBD-ferritin interface (residues: ۴۱-۴۹) and Haddockscore (۳.۷ +/- ۱۲.۱) and RMSD value (۱۰.۹ Å) of the molecular docking showed that this connection has lowstability and it does not interfere with ferritin and RBD binding. The results suggesting that efficiency offerritin nanoparticle vaccine may Not be affected by human lectins.Conclusions: Binding of human lectin to the RBD-ferritin nanoparticle shows that although the binding siteof the lectin is near to the RBD and ferritin interface it does not inhibit the ferritin-RBD binding.