Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Genome-Wide Mining of Selaginella moellendorffii for Hevein-Like Lectins and Their Potential Molecular Mimicry with SARS-CoV2 Spike Glycoprotein

Ahmed Alsolami
ORCID logo ,
Amina I Dirar
,
Emadeldin H. E Konozy
ORCID logo ,
Makarim El-fadil M Osman
,
Mohanad A Ibrahim
,
Khalid Farhan Alshammari
,
Fawwaz Alshammari
,
Meshari Alazmi
,
Kamaleldin B Said
* ORCID logo
Version 1 : Received: 18 April 2023 / Approved: 19 April 2023 / Online: 19 April 2023 (07:44:58 CEST)

A peer-reviewed article of this Preprint also exists.

Alsolami, A.; Dirar, A.I.; Konozy, E.H.E.; Osman, M.E.-F.; Ibrahim, M.A.; Alshammari, K.F.; Alshammari, F.; Alazmi, M.; Said, K.B. Genome-Wide Mining of Selaginella moellendorffii for Hevein-like Lectins and Their Potential Molecular Mimicry with SARS-CoV-2 Spike Glycoprotein. Curr. Issues Mol. Biol. 2023, 45, 5879-5901. Alsolami, A.; Dirar, A.I.; Konozy, E.H.E.; Osman, M.E.-F.; Ibrahim, M.A.; Alshammari, K.F.; Alshammari, F.; Alazmi, M.; Said, K.B. Genome-Wide Mining of Selaginella moellendorffii for Hevein-like Lectins and Their Potential Molecular Mimicry with SARS-CoV-2 Spike Glycoprotein. Curr. Issues Mol. Biol. 2023, 45, 5879-5901.

Abstract

Multidisciplinary research efforts on potential COVID-19 vaccine and therapeutic candidates have increased since the pandemic outbreak of SARS-CoV-2 in 2019. This search has become imperative due to the increasing emergences and limited widely available medicines. The presence of bioactive anti-SARS-CoV-2 molecules was examined from various plant sources. Among them is a group of proteins called lectins that can bind carbohydrate moieties. In this article, we present ten novel, chitin-specific Hevein-like lectins that were derived from Selaginella moellendorffii v1.0's genome. The capacity of these lectin homologs to bind with the spike protein of SARS-CoV-2 was examined. Using the HDOCK server, 3D-modeled Hevein-domains were docked to the spike protein's receptor binding domain (RBD). The Smo446851, Smo125663, and Smo99732 interacted with Asn343-located complex N-glycan and RBD residues, respectively, with binding free energies of -17.5, -13.0, and -26.5 Kcal/mol. The normal-state analyses via torsional coordinate association for the Smo99732-RBD complex using iMODS is characterized by overall higher stability and minimum deformity than the other lectin complexes. The three lectins interacting with carbohydrates were docked against five individual mutations that frequently occur in major SARS-CoV-2 variants. These were in the spike protein’s receptor-binding motif (RBM), while Smo125663 and Smo99732 only interacted with the spike glycoprotein in a protein-protein manner. The precursors for the Hevein-like homologs underwent additional characterization and their expressional profile in different tissues was studied. These in-silico findings offered potential lectin candidates targeting key N-glycan sites crucial to the virus's virulence and infection.

Keywords

Hevein-lectins; Selaginella moellendorffii; SARS-CoV-2, Spike protein; Docking; Variants

Subject

Medicine and Pharmacology, Medicine and Pharmacology

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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