IbeA is an important invasion determinant contributing to Escherichia coli K1 entry into brain microvascular endothelial cells (BMEC) that is a key step in the pathogenesis of E. coli meningitis. Our previous studies ...IbeA is an important invasion determinant contributing to Escherichia coli K1 entry into brain microvascular endothelial cells (BMEC) that is a key step in the pathogenesis of E. coli meningitis. Our previous studies have shown that IbeA-induced signaling and E. coli K1 invasion is mediated by two IbeA-binding proteins, vimentin, which is constitutively present in the surface of human BMECs (HBMECs), and PSF, which is inducibly expressed in both mesenchymal (endothelium) and non-mesenchymal (epithelium) cells. However, it is unknown whether p54nrb, a PSF partner protein, could contribute to the pathogenesis of E. coli K1 meningitis. Here, we reported that a 54-kDa protein was identified by copurification with PSF through IbeA-affinity chromatography as an IbeA-binding protein, which is identical to p54nrb. Both p54nrb and PSF are RNA-binding proteins and share significant sequence homology. The specific interaction between IbeA and p54nrb was confirmed by Western blot and ligand overlay assays. Recombinant p54nrb blocked E. coli K1 invasion of human BMEC very effectively. Overexpressed p54nrb as a GFP fusion protein in the transfected 293T cells significantly enhanced E. coli K1 invasion. Furthermore, higher levels of surface p54nrb in the transfected 293T cells were detected by flow cytometry. These results suggest that the IbeA invasion protein of E. coli K1 interacts with p54nrb for bacterial invasion of human BMEC.展开更多
We theoretically study nonlinear thermoelectric transport through a topological superconductor nanowire hosting Majorana bound states(MBSs) at its two ends, a system named as Majorana nanowire(MNW). We consider that t...We theoretically study nonlinear thermoelectric transport through a topological superconductor nanowire hosting Majorana bound states(MBSs) at its two ends, a system named as Majorana nanowire(MNW). We consider that the MNW is coupled to the left and right normal metallic leads subjected to either bias voltage or temperature gradient. We focus our attention on the sign change of nonlinear Seebeck and Peltier coefficients induced by mechanisms related to the MBSs, by which the possible existence of MBSs might be proved. Our results show that for a fixed temperature difference between the two leads, the sign of the nonlinear Seebeck coefficient(thermopower) can be reversed by changing the overlap amplitude between the MBSs or the system equilibrium temperature, which are similar to the cases in linear response regime. By optimizing the MBS–MBS interaction amplitude and system equilibrium temperature, we find that the temperature difference may also induce sign change of the nonlinear thermopower. For zero temperature difference and finite bias voltage, both the sign and magnitude of nonlinear Peltier coefficient can be adjusted by changing the bias voltage or overlap amplitude between the MBSs. In the presence of both bias voltage and temperature difference, we show that the electrical current at zero Fermi level and the states induced by overlap between the MBSs keep unchanged, regardless of the amplitude of temperature difference. We also find that the direction of the heat current driven by bias voltage may be changed by weak temperature difference.展开更多
文摘IbeA is an important invasion determinant contributing to Escherichia coli K1 entry into brain microvascular endothelial cells (BMEC) that is a key step in the pathogenesis of E. coli meningitis. Our previous studies have shown that IbeA-induced signaling and E. coli K1 invasion is mediated by two IbeA-binding proteins, vimentin, which is constitutively present in the surface of human BMECs (HBMECs), and PSF, which is inducibly expressed in both mesenchymal (endothelium) and non-mesenchymal (epithelium) cells. However, it is unknown whether p54nrb, a PSF partner protein, could contribute to the pathogenesis of E. coli K1 meningitis. Here, we reported that a 54-kDa protein was identified by copurification with PSF through IbeA-affinity chromatography as an IbeA-binding protein, which is identical to p54nrb. Both p54nrb and PSF are RNA-binding proteins and share significant sequence homology. The specific interaction between IbeA and p54nrb was confirmed by Western blot and ligand overlay assays. Recombinant p54nrb blocked E. coli K1 invasion of human BMEC very effectively. Overexpressed p54nrb as a GFP fusion protein in the transfected 293T cells significantly enhanced E. coli K1 invasion. Furthermore, higher levels of surface p54nrb in the transfected 293T cells were detected by flow cytometry. These results suggest that the IbeA invasion protein of E. coli K1 interacts with p54nrb for bacterial invasion of human BMEC.
基金Project supported by the National Natural Science Foundation of China(Grant No.12264037)the Innovation Team of Colleges and Universities in Guangdong Province(Grant No.2021KCXTD040)+2 种基金Guangdong Province Education Department(Grant No.2023KTSCX174)the Key Laboratory of Guangdong Higher Education Institutes(Grant No.2023KSYS011)Science and Technology Bureau of Zhongshan(Grant No.2023B2035)。
文摘We theoretically study nonlinear thermoelectric transport through a topological superconductor nanowire hosting Majorana bound states(MBSs) at its two ends, a system named as Majorana nanowire(MNW). We consider that the MNW is coupled to the left and right normal metallic leads subjected to either bias voltage or temperature gradient. We focus our attention on the sign change of nonlinear Seebeck and Peltier coefficients induced by mechanisms related to the MBSs, by which the possible existence of MBSs might be proved. Our results show that for a fixed temperature difference between the two leads, the sign of the nonlinear Seebeck coefficient(thermopower) can be reversed by changing the overlap amplitude between the MBSs or the system equilibrium temperature, which are similar to the cases in linear response regime. By optimizing the MBS–MBS interaction amplitude and system equilibrium temperature, we find that the temperature difference may also induce sign change of the nonlinear thermopower. For zero temperature difference and finite bias voltage, both the sign and magnitude of nonlinear Peltier coefficient can be adjusted by changing the bias voltage or overlap amplitude between the MBSs. In the presence of both bias voltage and temperature difference, we show that the electrical current at zero Fermi level and the states induced by overlap between the MBSs keep unchanged, regardless of the amplitude of temperature difference. We also find that the direction of the heat current driven by bias voltage may be changed by weak temperature difference.
