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Article Abstract
Background And Aims: The human Rhinovirus, a positive-sense, single-stranded RNA virus within the Enterovirus genus of the Picornaviridae family, is the most prevalent viral pathogen in humans and the primary cause of the common cold (Verywell Health 2024). Virus-host interactions, particularly receptor-mediated adhesion, are pivotal in viral pathogenesis. Competitive inhibition and the use of anti-adhesive agents have emerged as potential strategies to prevent viral docking. This study aims to explore the structural biology of rhinovirus receptors, specifically the canyon-like depressions involved in host cell recognition, and investigate molecular approaches to minimize infection and reduce recovery time.
Methods: A comprehensive structural analysis of human Rhinovirus 14 was conducted, focusing on its unique surface depressions (canyons) surrounding the five-fold axes. Literature was reviewed for monoclonal antibody interactions via hybridoma technology, as well as anti-adhesive agents like alginic acid, gelatin, chitosan, and carboxymethyl cellulose. Molecular docking simulations were referenced to evaluate the potential of organic compounds to disrupt viral adhesion.
Results: The canyon regions on the viral capsid were confirmed as receptor-binding sites that are structurally shielded from antibody access, allowing the virus to evade immune detection. Anti-adhesive agents demonstrated theoretical efficacy in competitively inhibiting receptor-ligand interactions at these sites. Monoclonal antibodies, while effective in certain contexts, showed limited access to conserved binding residues due to spatial constraints. Organic compounds with flexible conformational geometry showed potential in blocking receptor sites by steric hindrance.
Conclusion: The structural characteristics of human Rhinovirus 14 play a crucial role in immune evasion and receptor binding. While current treatments are limited by the virus's high mutation rate, anti-adhesive strategies offer a promising avenue to inhibit early-stage infection and reduce recovery time. Further experimental validation of these agents is necessary to develop effective antiviral therapeutics.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC12326439 | PMC |
| http://dx.doi.org/10.1002/hsr2.70922 | DOI Listing |
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