Department of Genome Sciences University of Washington School of Medicine 850 Republican Street, Brotman Building, Room 154 Seattle , Washington 98109 , United States.
J Am Soc Mass Spectrom. 2020 Feb 5;31(2):190-195. doi: 10.1021/jasms.9b00021. Epub 2019 Nov 21.
Molecular interactions between two different classes of β-lactamase enzymes and outer membrane protein A (OmpA) were studied by in vivo chemical cross-linking of a multi-drug-resistant strain of AB5075. Class A β-lactamase blaGES-11 and Class D β-lactamase Oxa23, responsible for hydrolysis of different types of β-lactam antibiotics, were found to be cross-linked to similar lysine sites of the periplasmic domain of outer membrane protein OmpA, despite low sequence homology between the two enzymes. The findings from in vivo XL-MS suggest that the interacting surfaces between both β-lactamase enzymes and OmpA are conserved during molecular evolution, and the OmpA C-terminus domain serves an important function of anchoring different types of β-lactamase enzymes in the periplasmic space.
通过对多药耐药株 AB5075 的体内化学交联研究,研究了两种不同类别的β-内酰胺酶和外膜蛋白 A(OmpA)之间的分子相互作用。负责水解不同类型β-内酰胺抗生素的类 Aβ-内酰胺酶 blaGES-11 和类 Dβ-内酰胺酶 Oxa23 被发现与外膜蛋白 OmpA 的周质域的类似赖氨酸位点交联,尽管两种酶之间的序列同源性较低。体内 XL-MS 的研究结果表明,在分子进化过程中,两种β-内酰胺酶与 OmpA 之间的相互作用表面是保守的,OmpA C 末端结构域在周质空间中锚定不同类型的β-内酰胺酶方面发挥着重要作用。