Gründel Anne, Jacobs Enno, Dumke Roger
Technische Universität Dresden, Medizinische Fakultät Carl Gustav Carus, Institut für Medizinische Mikrobiologie und Hygiene, Fetscherstrasse 74, 01307 Dresden, Germany.
Technische Universität Dresden, Medizinische Fakultät Carl Gustav Carus, Institut für Medizinische Mikrobiologie und Hygiene, Fetscherstrasse 74, 01307 Dresden, Germany.
Int J Med Microbiol. 2016 Dec;306(8):675-685. doi: 10.1016/j.ijmm.2016.09.001. Epub 2016 Sep 3.
Mycoplasma pneumoniae is a major cause of community-acquired respiratory infections worldwide. Due to the strongly reduced genome, the number of virulence factors expressed by this cell wall-less pathogen is limited. To further understand the processes during host colonization, we investigated the interactions of the previously confirmed surface-located glycolytic enzymes of M. pneumoniae (pyruvate dehydrogenase A-C [PdhA-C], glyceraldehyde-3-phosphate dehydrogenase [GapA], lactate dehydrogenase [Ldh], phosphoglycerate mutase [Pgm], pyruvate kinase [Pyk] and transketolase [Tkt]) to the human extracellular matrix (ECM) proteins fibrinogen (Fn), fibronectin (Fc), lactoferrin (Lf), laminin (Ln) and vitronectin (Vc), respectively. Concentration-dependent interactions between Fn and Vc and all eight recombinant proteins derived from glycolytic enzymes, between Ln and PdhB-C, GapA, Ldh, Pgm, Pyk and Tkt, between Lf and PdhA-C, GapA and Pyk, and between Fc and PdhC and GapA were demonstrated. In most cases, these associations are significantly influenced by ionic forces and by polyclonal sera against recombinant proteins. In immunoblotting, the complex of human plasminogen, activator (tissue-type or urokinase plasminogen activator) and glycolytic enzyme was not able to degrade Fc, Lf and Ln, respectively. In contrast, degradation of Vc was confirmed in the presence of all eight enzymes tested. Our data suggest that the multifaceted associations of surface-localized glycolytic enzymes play a potential role in the adhesion and invasion processes during infection of human respiratory mucosa by M. pneumoniae.
肺炎支原体是全球社区获得性呼吸道感染的主要病因。由于基因组大幅缩减，这种无细胞壁病原体表达的毒力因子数量有限。为了进一步了解宿主定植过程，我们分别研究了先前已证实的肺炎支原体表面糖酵解酶（丙酮酸脱氢酶A - C [PdhA - C]、甘油醛 - 3 - 磷酸脱氢酶[GapA]、乳酸脱氢酶[Ldh]、磷酸甘油酸变位酶[Pgm]、丙酮酸激酶[Pyk]和转酮醇酶[Tkt]）与人类细胞外基质（ECM）蛋白纤维蛋白原（Fn）、纤连蛋白（Fc）、乳铁蛋白（Lf）、层粘连蛋白（Ln）和玻连蛋白（Vc）之间的相互作用。证实了Fn与Vc以及所有八种源自糖酵解酶的重组蛋白之间、Ln与PdhB - C、GapA、Ldh、Pgm、Pyk和Tkt之间、Lf与PdhA - C、GapA和Pyk之间以及Fc与PdhC和GapA之间存在浓度依赖性相互作用。在大多数情况下，这些结合受到离子力和抗重组蛋白多克隆血清的显著影响。在免疫印迹中，人纤溶酶原、激活剂（组织型或尿激酶型纤溶酶原激活剂）与糖酵解酶的复合物分别无法降解Fc、Lf和Ln。相反，在所有八种测试酶存在的情况下证实了Vc的降解。我们的数据表明，表面定位的糖酵解酶的多方面结合在肺炎支原体感染人类呼吸道黏膜期间的黏附和侵袭过程中发挥潜在作用。
