HSV1 glycoprotein D utilizes an LY6-like binding domain to inhibit alpha7 nicotinic receptors.

Sabina Yeasmin, Kavita Sharma, Christopher Nicolet, Laura DeCristofano, Yeganeh Ataian, Arina Ranjit, Ali Aghazadeh-Habashi, Dong Xu, Marvin Schulte
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Abstract

Herpes virus1(HSV1) is a neurotropic virus that has been linked to Alzheimer's disease. An In-silico structural homology search using α -Bgtx, identified structural homology between HSV1 gD and the nicotinic receptor neurotoxin α-Bgtx. SPR binding studies using acetylcholine binding protein from Lymnaea stagnalis, and functional two electrode voltage clamp studies of α7 nAChRs demonstrate the ability of HSV1 to interact directly with nAChRs. Molecular docking studies support the binding of a neurotoxin-like binding loop in HSV1 to a binding site similar to the neurotoxin binding domain. Interaction of HSV1 with nAChRs provides novel insights into a potential mechanism of action of HSV and its potential role in Alzheimer's disease.

HSV1糖蛋白D利用ly6样结合域抑制α 7烟碱受体。
疱疹病毒1(HSV1)是一种嗜神经病毒,与阿尔茨海默病有关。利用α-Bgtx对HSV1基因进行了结构同源性研究,发现HSV1基因gD与烟碱受体神经毒素α-Bgtx具有结构同源性。SPR结合研究使用了来自lynaea滞海的乙酰胆碱结合蛋白,以及α7 nachr的功能性双电极电压钳研究表明HSV1能够直接与nachr相互作用。分子对接研究支持HSV1中神经毒素样结合环与类似神经毒素结合域的结合位点结合。HSV1与nAChRs的相互作用为HSV的潜在作用机制及其在阿尔茨海默病中的潜在作用提供了新的见解。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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