Abstract：
Yersinia pestis, the causative agent of plague, is capable of evading the human immune system response by recruiting the plasma circulating vitronectin proteins, which act as a shield and avoid its lysis. Vitronectin recruitment is mediated by its interaction with the bacterial transmembrane protein Ail, protruding from the Y. pestis outer membrane. By using all-atom long-scale molecular dynamic simulations of Ail embedded in a realistic model of the bacterial membrane, we have shown that vitronectin forms a stable complex, mediated by interactions between the disordered moieties of the two proteins. The main amino acids driving the complexation have also been evidenced, thus favoring the possible rational design of specific peptides which, by inhibiting vitronectin recruitment, could act as original antibacterial agents.
摘要：
鼠疫耶尔森氏菌,鼠疫的病原体，能够通过招募血浆循环玻连蛋白来逃避人体免疫系统的反应，充当盾牌并避免其溶解。玻连蛋白募集是通过其与细菌跨膜蛋白Ail的相互作用介导的，从鼠疫杆菌外膜突出。通过使用所有原子的长期分子动力学模拟Ail嵌入在一个现实的细菌膜模型，我们已经证明玻连蛋白形成稳定的复合物，由两种蛋白质的无序部分之间的相互作用介导。驱动络合的主要氨基酸也得到了证明，因此有利于特定肽的合理设计，通过抑制玻连蛋白募集，可以作为原始的抗菌剂。
