Yousafi Qudsia, Azhar Maria, Khan Muhammad Saad, Mehmood Asim, Saleem Shahzad, Sajid Muhammad Wasim, Hussain Abrar, Kamal Mohammad Amjad
Dept. Biosciences, COMSATS University Islamabad, Sahiwal, Pakistan.
King Fahd Medical Research Center, King Abdulaziz University, P. O. Box 80216, Jeddah 21589, Saudi Arabia.
Saudi J Biol Sci. 2020 May;27(5):1396-1402. doi: 10.1016/j.sjbs.2019.11.034. Epub 2019 Dec 2.
The cytoplasmic dynein light chain 1 (DYNLL1) is an important constituent of motor proteins complex. In human it is encoded by gene. It is involved in cargo transport functions and interacts with many viral proteins with the help of short linear consensus motif sequence (K/R) XTQT. Viral proteins bind to DYNLL1 through its consensus short linear motif (SLiM) sequence to reach the target site in the cell and cause different infections in the host. It is still unknown if bacterial proteins also contain the same conserved SLiMs sequence through which they bind to this motor protein and cause infections. So, it is important to investigate the role of DYNLL1 in human bacterial infections. The interaction partner proteins of DYNLL1 against conserved viral motif sequences were predicted through PDBSum. Pairwise sequence alignment, between viral motif sequence and that of predicted proteins, was performed to identify conserved region in predicted interaction partners. Docking between the DYNLL1 and new pathogenic interaction partners was performed, by using PatchDock, to explore the protein-protein binding quality. Interactions of docked complexes were visualized by DimPlot. Three pathogenic bacterial proteins ., enterochelin esterase (3MGA), protective antigen (3J9C) and putative lipoprotein (4KT3) were selected as candidate interaction partners of DYNLL1. The putative lipoprotein (4KT3) showed low quality binding with DYNLL1. So, enterochelin esterase (3MGA) and protective antigen (3J9C) were speculated to be involved in human bacterial infections by using DYNLL1 to reach their target sites.
细胞质动力蛋白轻链1（DYNLL1）是运动蛋白复合体的重要组成部分。在人类中，它由基因编码。它参与货物运输功能，并借助短线性共有基序序列（K/R）XTQT与许多病毒蛋白相互作用。病毒蛋白通过其共有短线性基序（SLiM）序列与DYNLL1结合，从而到达细胞内的靶位点并在宿主中引发不同感染。目前尚不清楚细菌蛋白是否也含有相同的保守SLiM序列，通过该序列它们与这种运动蛋白结合并导致感染。因此，研究DYNLL1在人类细菌感染中的作用很重要。通过PDBSum预测了DYNLL1针对保守病毒基序序列的相互作用伴侣蛋白。对病毒基序序列和预测蛋白的序列进行成对序列比对，以确定预测相互作用伴侣中的保守区域。使用PatchDock对DYNLL1与新的致病性相互作用伴侣进行对接，以探索蛋白质-蛋白质结合质量。通过DimPlot可视化对接复合物的相互作用。选择三种致病性细菌蛋白，即肠螯合素酯酶（3MGA）、保护性抗原（3J9C）和假定脂蛋白（4KT3）作为DYNLL1的候选相互作用伴侣。假定脂蛋白（4KT3）与DYNLL1的结合质量较低。因此，推测肠螯合素酯酶（3MGA）和保护性抗原（3J9C）通过利用DYNLL1到达其靶位点而参与人类细菌感染。
