The Ebola virus (EBOV) hijacks normal physiological processes by apoptotic mimicry in order to be taken up by the cell it infects. The initial adhesion of the virus to the cell is based on the interaction between T-cell immunoglobulin and mucin domain protein, TIM, on the cell-surface and phosphatidylserine (PS) on the viral outer surface. Therefore, it is important to understand the interaction between EBOV/PS and TIM, with selective blocking of the interaction as a potential therapy. Recent experimental studies have shown that for TIM-dependent EBOV entry, a Mucin-like Domain (MLD) with a length of at least 120 amino acids is required, possibly due to the increase of area of the PS-coated surface sampled. We examine this hypothesis by modeling the process of TIM-PS adhesion using a coarse-grained molecular model. We find that the strength of bound PS–TIM pairs is essentially independent of TIM length. TIMs with longer MLDs have higher average binding strengths because of an increase in the probability of binding between EBOV and TIM proteins. Similarly, we find that for larger persistence length (less flexible) the average binding force decreases, again because of a reduction in the probability of binding.

中文翻译：

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类似于粘蛋白的域的长度通过增加结合概率来增强细胞埃博拉病毒的粘附。

埃博拉病毒（EBOV）通过凋亡模仿模仿正常的生理过程，以被其感染的细胞吸收。病毒与细胞的最初粘附是基于T细胞免疫球蛋白与细胞表面粘蛋白域蛋白TIM和病毒外表面磷脂酰丝氨酸（PS）之间的相互作用。因此，重要的是要了解EBOV / PS和TIM之间的相互作用，并将相互作用的选择性阻断作为一种潜在的治疗方法。最近的实验研究表明，对于TIM依赖的EBOV进入，可能需要长度至少为120个氨基酸的类粘蛋白样结构域（MLD），这可能是由于采样的PS涂层表面面积增加所致。我们通过使用粗粒度分子模型对TIM-PS粘附过程进行建模来检验该假设。我们发现绑定的PS–TIM对的强度本质上与TIM长度无关。MLD更长的TIM具有更高的平均结合强度，因为EBOV和TIM蛋白之间结合的可能性增加了。同样，我们发现，对于较大的持久性长度（较不灵活），平均绑定力也会降低，这也是因为绑定的可能性降低了。