Vasseur Laurine, Barbault Florent, Monari Antonio
ITODYS, Université Paris Cité and CNRS, Paris, F-75006, France.
Chemistry. 2025 Aug 13;31(45):e00874. doi: 10.1002/chem.202500874. Epub 2025 Jul 25.
Bacterial resistance and nosocomial infections are serious threats compromising public health in numerous countries. Acinetobacter baumannii has been identified as one of the most serious pathogens, due to its potential virulence and the development of multiple resistance. In this contribution by using all-atom molecular dynamics simulation, we analyze the structure and the properties of the OmpA protein, which is present in the bacterial external membrane. We also analyze the structure of possible protein/protein complexes formed between OmpA and the human fibronectin, which may ultimately lead to the immune escape of the bacteria. We provide a plausible structure of the complex, also identifying suitable amino acids mediating the interaction, and thus, constituting suitable drug targets to disrupt the complex formation.
细菌耐药性和医院感染是许多国家公共卫生面临的严重威胁。鲍曼不动杆菌已被确认为最严重的病原体之一，因其潜在的毒力和多重耐药性的发展。在本论文中，我们通过全原子分子动力学模拟，分析了存在于细菌外膜中的外膜蛋白A（OmpA）的结构和性质。我们还分析了OmpA与人纤连蛋白之间可能形成的蛋白质/蛋白质复合物的结构，这可能最终导致细菌的免疫逃逸。我们提供了该复合物的合理结构，还确定了介导相互作用的合适氨基酸，从而构成了破坏复合物形成的合适药物靶点。
