Interaction of triosephosphate isomerase from Staphylococcus aureus with plasminogen

Abstract

Triosephosphate isomerase (TPI; EC 5. 3. 1. 1) displayed on the cell surface of Staphylococcus aureus acts as an adhesion molecule that binds to the capsule of Cryptococcus neoformans, a fungal pathogen. This study investigated the function of TPI on the cell surface of S. aureus and its interactions with biological substances such as fibronectin, fibrinogen, plasminogen, and thrombin were investigated. Binding of TPI to plasminogen was demonstrated by both surface plasmon resonance analysis and Far-Western blotting. It is suggested that lysine residues contribute to this binding because the interaction was inhibited by ε-aminocaproic acid. Activation of plasminogen to plasmin by staphylokinase or tissue plasminogen activator decreased in the presence of TPI, whereas TPI was degraded by plasmin. In other experiments, intact S. aureus cells had the ability to both increase and decrease plasminogen activation depending on the number of cells. Several molecules expressed on the surface of S. aureus were predicted to interact with plasminogen, resulting in its increased or decreased activation. These findings indicate that S. aureus sometimes localizes and sometimes disseminates in the host, depending on the molecules expressed under various conditions.

The Glycolytic Enzyme Triosephosphate Isomerase of Trichomonas vaginalis Is a Surface-Associated Protein Induced by Glucose That Functions as a Laminin- and Fibronectin-Binding Protein

“…These results are consistent with some of the functions identified for TIM on the surfaces of other pathogens (14,53), such as P. brasiliensis (16) S. aureus (17), L. plantarum (57), and Mycoplasma gallisepticum (58). Recently, the TIM protein was also identified in the surface proteome of E. histolytica (49) and in the cell wall proteome of C. albicans (50); however, the specific surface function of TIM in E. histolytica has not been described yet.…”

“…For example, it is an adhesin for epithelial cells and a laminin (Lm)-and Fn-binding protein during the parasitic phase of Paracoccidioides brasiliensis (16). Similarly, TIM is a Plg-binding protein in Staphylococcus aureus (17). Moreover, TIM has extracellular functions in parasitic helminths; i.e., it is secreted during infection by Brugia malayi and Schistosoma mansoni and acts as an antibody target during infection, and it has been considered a potential target for drug and/or vaccine development (18)(19)(20).…”

The Cell Surface Proteome of Entamoeba histolytica

“…However, less than 2% of amoebae died during the biotin labeling procedure, which almost excludes this possibility. For enolase, fructose-1,6-biphosphate aldolase, triosephosphate isomerase and GAPDH a surface association was described in several organisms including Paracoccidioides brasiliensis , Streptococcus suis, Trichomonas vaginalis, Lactobacillus plantarum 299v, Mycobacterium tuberculosis, Candida albicans, and Staphylococcus aureus (64–70). Interestingly, like also seen for E. histolytica these proteins are anchorless and the mechanism by which they reach the cell surface is unknown.…”

Molecular identification, immunolocalization, and characterization of Clonorchis sinensis triosephosphate isomerase

“…b Western blotting analysis of CsTIM at different stages of C. sinensis visualized using ECL method (Guillou et al 2007;Wilson 2012), and S. japonicum (Liu et al 2009). What is more, it can take part in the recognition of cell surface and extracellular matrix glycoproteins in some pathogens (Karkowska-Kuleta et al 2011;Furuya and Ikeda 2011;Furuya and Ikeda 2009;Pereira et al 2007). Therefore, CsTIM may participate in host-parasite interaction.…”