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Biomolecules
Special Issues
Molecular Mechanism and Detection of SARS-CoV-2
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Molecular Mechanism and Detection of SARS-CoV-2

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 31 July 2025 | Viewed by 151

Special Issue Editor

Dr. Zaki A. Sherif

E-Mail Website
Guest Editor
Department of Biochemistry & Molecular Biology, Howard University College of Medicine, Washington, DC 20059, USA
Interests: liver cancer; SARS-CoV-2 pathogenesis

Special Issue Information

Dear Colleagues,

The COVID-19 pandemic has highlighted the critical importance of understanding SARS-CoV-2's molecular mechanisms and detection methods. This special issue will focus on the latest advances in understanding viral pathogenesis, host-pathogen interactions, and diagnostic approaches for SARS-CoV-2 infection.

SARS-CoV-2 is characterized as a positive-sense single-stranded RNA virus that primarily enters host cells through spike protein-mediated mechanisms. The virus demonstrates sophisticated methods of immune evasion and utilizes the ACE2 receptor for cellular entry, leading to various pathological outcomes. Recent research has revealed novel insights into viral protein interactions, structural biology, and potential therapeutic targets.

This special issue aims to compile cutting-edge research on molecular mechanisms underlying SARS-CoV-2 infection, host immune responses, emerging variants, and advanced detection methods. We welcome original research articles, reviews, and perspectives that contribute to our understanding of viral pathogenesis and improve diagnostic capabilities.

Dr. Zaki A. Sherif
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biomolecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • SARS-CoV-2 spike protein
  • ACE2 receptor
  • viral pathogenesis
  • host-viral protein interactions
  • molecular diagnostics
  • RNA virus replication
  • immune response
  • viral structural proteins
  • pathobiology
  • RT-PCR detection

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Further information on MDPI's Special Issue policies can be found here.

Published Papers (1 paper)

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Research

17 pages, 1965 KiB  
Article
The Role of Long-Range Non-Specific Electrostatic Interactions in Inhibiting the Pre-Fusion Proteolytic Processing of the SARS-CoV-2 S Glycoprotein by Heparin
by Yi Du, Yang Yang, Son N. Nguyen and Igor A. Kaltashov
Biomolecules 2025, 15(6), 778; https://doi.org/10.3390/biom15060778 - 28 May 2025
Viewed by 9
Abstract
The proteolytic processing of the SARS-CoV-2 spike glycoprotein by host cell membrane-associated proteases is a key step in both the entry of the invading virus into the cell and the release of the newly generated viral particles from the infected cell. Because of [...] Read more.
The proteolytic processing of the SARS-CoV-2 spike glycoprotein by host cell membrane-associated proteases is a key step in both the entry of the invading virus into the cell and the release of the newly generated viral particles from the infected cell. Because of the critical importance of this step for the viral infectivity cycle, it has been a target of extensive efforts aimed at identifying highly specific protease inhibitors as potential antiviral agents. An alternative strategy to disrupt the pre-fusioviden processing of the SARS-CoV-2 S glycoprotein aims to protect the substrate rather than directly inhibit the proteases. In this work, we focused on furin, a serine protease located primarily in the Golgi apparatus, but also present on the cell membrane. Its cleavage site within the S glycoprotein is located within the stalk region of the latter and comprises an arginine-rich segment (SPRRARS), which fits the definition of the Cardin–Weintraub glycosaminoglycan recognition motif. Native mass spectrometry (MS) measurements confirmed the binding of a hexadecameric peptide representing the loop region at the S1/S2 interface and incorporating the furin cleavage site (FCS) to heparin fragments of various lengths, as well as unfractionated heparin (UFH), although at the physiological ionic strength, only UFH remains tightly bound to the FCS. The direct LC/MS monitoring of FCS digestion with furin revealed a significant impact of both heparin fragments and UFH on the proteolysis kinetics, although only the latter had IC50 values that could be considered physiologically relevant (0.6 ± 0.1 mg/mL). The results of this work highlight the importance of the long-range and relatively non-specific electrostatic interactions in modulating physiological and pathological processes and emphasize the multi-faceted role played by heparin in managing coronavirus infections. Full article
(This article belongs to the Special Issue Molecular Mechanism and Detection of SARS-CoV-2)
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