Department of Biological Sciences, Birla Institute of Technology & Science, Pilani, K. K. Birla Goa Campus, NH17B, Zuarinagar, Goa, 403726, India.
Department of Biosciences, Metabolic Engineering Lab, Jamia Millia Islamia, New Delhi, 110025, India.
Future Microbiol. 2022 Dec;17:1455-1473. doi: 10.2217/fmb-2022-0169. Epub 2022 Nov 10.
Pathogenic invasion of is critically dependent on host plasminogen activation. The pathophysiological implications of the interactions between recombinant enolase and host plasminogen were investigated. The effects of mutation and small synthetic peptide inhibitors on interactions were assessed. , the recombinant enolase exists as a catalytically active fragile octamer and a robust dimer. The dimer interacts with the host plasminogen on the surface. The interaction of host plasminogen and enolase might mediate bacterial adherence to the host, activate the plasminogen with the help of plasminogen activators and prevent α-antiplasmin-mediated inhibition of plasmin. Incorporating mutant and synthetic peptides inhibited the interactions and their associated pathophysiological consequences.
是病原体入侵的关键依赖于宿主纤溶酶原激活。本研究旨在探讨 重组烯醇酶与宿主纤溶酶原相互作用的病理生理意义。评估了突变和小合成肽抑制剂对相互作用的影响。结果表明，在生理条件下， 重组烯醇酶以催化活性脆弱的八聚体和稳定的二聚体形式存在。二聚体与宿主纤溶酶原在表面相互作用。宿主纤溶酶原与 烯醇酶的相互作用可能介导细菌与宿主的黏附，在纤溶酶原激活物的帮助下激活纤溶酶原，并防止 α2-抗纤溶酶抑制纤溶酶。包含突变和合成肽的抑制剂抑制了相互作用及其相关的病理生理后果。
