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病毒-受体相互作用:细胞入侵的关键。

Virus-Receptor Interactions: The Key to Cellular Invasion.

机构信息

Department of Molecular and Biomedical Sciences, The University of Maine, Orono, ME 04469-5735, USA.

出版信息

J Mol Biol. 2018 Aug 17;430(17):2590-2611. doi: 10.1016/j.jmb.2018.06.024. Epub 2018 Jun 18.

Abstract

Virus-receptor interactions play a key regulatory role in viral host range, tissue tropism, and viral pathogenesis. Viruses utilize elegant strategies to attach to one or multiple receptors, overcome the plasma membrane barrier, enter, and access the necessary host cell machinery. The viral attachment protein can be viewed as the "key" that unlocks host cells by interacting with the "lock"-the receptor-on the cell surface, and these lock-and-key interactions are critical for viruses to successfully invade host cells. Many common themes have emerged in virus-receptor utilization within and across virus families demonstrating that viruses often target particular classes of molecules in order to mediate these events. Common viral receptors include sialylated glycans, cell adhesion molecules such as immunoglobulin superfamily members and integrins, and phosphatidylserine receptors. The redundancy in receptor usage suggests that viruses target particular receptors or "common locks" to take advantage of their cellular function and also suggests evolutionary conservation. Due to the importance of initial virus interactions with host cells in viral pathogenesis and the redundancy in viral receptor usage, exploitation of these strategies would be an attractive target for new antiviral therapeutics.

摘要

病毒-受体相互作用在病毒宿主范围、组织嗜性和病毒发病机制中起着关键的调节作用。病毒利用巧妙的策略来附着于一个或多个受体,克服质膜屏障,进入并利用必要的宿主细胞机制。病毒的附着蛋白可以被视为通过与细胞表面上的“受体”相互作用来解锁宿主细胞的“钥匙”,这些锁钥相互作用对于病毒成功入侵宿主细胞至关重要。在病毒家族内和跨病毒家族中,病毒-受体的利用出现了许多共同的主题,这表明病毒通常针对特定类别的分子来介导这些事件。常见的病毒受体包括唾液酸化聚糖、细胞粘附分子,如免疫球蛋白超家族成员和整合素,以及磷脂酰丝氨酸受体。受体利用的冗余性表明病毒针对特定的受体或“常见的锁”,以利用其细胞功能,并暗示了进化上的保守性。由于初始病毒与宿主细胞相互作用在病毒发病机制中的重要性,以及病毒受体利用的冗余性,利用这些策略将是新抗病毒治疗的有吸引力的目标。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c383/7094595/79d6549db52e/fx1_lrg.jpg

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