麻疹病毒是具有非分段负义RNA基因组的包膜病毒。病毒表面有两种包膜糖蛋白,即血凝素(H)和膜融合蛋白(F),负责病毒进入易感宿主细胞。H与其细胞受体之间的特异性相互作用是成功感染病毒的关键步骤。确定麻疹病毒的传染性和组织嗜性。到目前为止,已经鉴定出三种H受体,包括补体调节分子CD46、信号淋巴细胞活化分子(SLAM)和细胞粘附分子Nectin-4。这里,我们回顾了我们对病毒H蛋白识别这些受体机制的分子理解,旨在促进抗病毒药物设计和基于麻疹病毒的溶瘤治疗的未来研究。
Measles virus is an enveloped virus with a non-segmented negative-sense RNA genome. Two envelope glycoproteins on the viral surface, namely hemagglutinin (H) and membrane fusion protein (F), are responsible for the virus entry into susceptible host cells. The specific interaction between H and its cellular receptors is a key step in successful virus infection, determining the infectivity and tissue tropism of the measles virus. Thus far, three H receptors have been identified, including the complement regulatory molecule CD46, the signaling lymphocyte activation molecule (SLAM) and the cell adhesion molecule Nectin-4. Here, we reviewed our molecular understanding on the recognition mechanism of these receptors by the viral H protein, aiming to promote future studies on antiviral drug design and measles virus-based oncolytic therapy.