Maitra Srinjoy, Rajak Jenifer, Ghoshal Agnik, Roy Bedaprana, Ghosh Shoham, Mitra Arup Kumar, Kumer Ajoy, Dhara Bikram
Department of Microbiology St. Xavier's College (Autonomous) Kolkata India.
Department of Chemistry IUBAT-International University of Business Agriculture & Technology Dhaka Bangladesh.
Health Sci Rep. 2025 Aug 6;8(8):e70922. doi: 10.1002/hsr2.70922. eCollection 2025 Aug.
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.
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.
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.
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.
人鼻病毒是微小核糖核酸病毒科肠道病毒属的一种正义单链RNA病毒，是人类最常见的病毒病原体，也是普通感冒的主要病因（Verywell Health 2024）。病毒与宿主的相互作用，尤其是受体介导的黏附，在病毒发病机制中起着关键作用。竞争性抑制和使用抗黏附剂已成为预防病毒对接的潜在策略。本研究旨在探索鼻病毒受体的结构生物学，特别是参与宿主细胞识别的峡谷样凹陷，并研究将感染降至最低并缩短恢复时间的分子方法。
对人鼻病毒14进行了全面的结构分析，重点关注其围绕五重轴的独特表面凹陷（峡谷）。查阅了有关通过杂交瘤技术进行单克隆抗体相互作用的文献，以及藻酸、明胶、壳聚糖和羧甲基纤维素等抗黏附剂的文献。参考分子对接模拟来评估有机化合物破坏病毒黏附的潜力。
病毒衣壳上的峡谷区域被确认为受体结合位点，其结构可防止抗体进入，使病毒能够逃避免疫检测。抗黏附剂在竞争性抑制这些位点的受体-配体相互作用方面显示出理论功效。单克隆抗体虽然在某些情况下有效，但由于空间限制，对保守结合残基的 access 有限。具有灵活构象几何形状的有机化合物显示出通过空间位阻阻断受体位点的潜力。
人鼻病毒14的结构特征在免疫逃逸和受体结合中起着关键作用。虽然目前的治疗方法受到病毒高突变率的限制，但抗黏附策略为抑制早期感染和缩短恢复时间提供了一条有前景的途径。要开发有效的抗病毒疗法，有必要对这些药物进行进一步的实验验证。
