A multifunctional enolase mediates cytoadhesion and interaction with host plasminogen and fibronectin in Mycoplasma hyorhinis

• DOI: 10.1186/s13567-022-01041-0
• Publication Date: 2022-03-25T12:37:33Z
• Authors: Jia Wang; Yanfei Yu; Yao Li; Shiyang Li; Li Wang; Yanna Wei; Yuzi Wu; Bala Pillay; Ademola Olufolaha...; Thamsanqa E. Chiliza; Guoqing Shao; Zhixin Feng; Qiyan Xiong
• Keywords: Enolase

Mycoplasma hyorhinis may cause systemic inflammation of pigs, typically polyserositis and arthritis, is also associated with several types human cancer. However, the pathogenesis M. colonizing breaching respiratory barrier to establish infection poorly understood. Glycolytic enzymes are important moonlighting proteins virulence-related factors in various bacteria. In this study, we investigated functions a glycolytic critical enzyme, enolase spread hyorhinis. Bacterial surface localization was confirmed by flow cytometry colony hybridization assay. Recombinant (rEno) found adhere pig kidney (PK-15) cells, anti-rEno serum significantly decreased adherence. The enzyme bind host plasminogen fibronectin, interactions were specific strong, dissociation constant (KD) values 1.4 nM 14.3 nM, respectively, from plasmon resonance analysis. Activation rEno-bound its ability hydrolyze plasmin-specific substrates degrade reconstituted extracellular matrix. To explore key sites during these interactions, C-terminal lysine residues replaced leucine, resulting single-site double-site mutants show reduced interaction far-Western blotting tests. binding affinities all fibronectin as well. Collectively, results imply that moonlights an adhesin hyorhinis, interacts fibronectin. two C-terminus for multiple activities.