Length of mucin-like domains enhances cell-Ebola virus adhesion by increasing binding probability
Length of mucin-like domains enhances cell-Ebola virus adhesion by increasing binding probability
复制标题
粘蛋白样结构域的长度通过增加结合概率来增强细胞与埃博拉病毒的粘附
DOI：
10.1016/j.bpj.2021.01.025
复制
发表时间：
2021
影响因子：
3.4
通讯作者：
Jagota, Anand
中科院分区：
文献类型：
--
作者：
Cui, Xinyu;Lapinski, Nicole;Zhang, Xiaohui;Jagota, Anand
The Ebola virus (EBOV) hijacks normal physiological processes by apoptotic mimicry 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 and 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 with a length of at least 120 amino acids is required, possibly because of 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 individual bound PS-TIM pairs is essentially independent of TIM length. TIMs with longer mucin-like domains collectively 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.
