ABSTRACT
The interaction between co-stimulatory ligands and their receptors of T cells and antigen presenting cells is crucial for the activation or resting of the immune cells. The tumor necrosis factor receptor superfamily and CD28-B7 family contain many such regulatory molecules. Herpesvirus entry mediator (HVEM), also named as tumor necrosis factor superfamily member 14, is noted for its pivotal role in regulating immune responses through binding LIGHT as a ligand to develop T-cell immunity, and in interacting with B and T lymphocyte attenuator (BTLA) as a receptor to negatively regulate T-cell responses. In antitumor immunity, increasing amount of evidence demonstrates that HVEM is an indispensable receptor on lymphocyte for LIGHT to co-stimulate tumor antigen-specific CTL. This article discusses the role of HVEM in regulating immune response and antitumor-immunity.
ABSTRACT
The fusion protein of Humanized mouse anti-human fibrin ScFv and the low molecular weight urokinase (IIn-UK) contained seven disulfide bonds and formed inclusion body while expressing in normal E. coli strain. By coexpressing DsbC and using the special E. coli strain Origami(DE3) which was trxB/gor double mutant, the fusion protein IIn-UK was functionally expressed in the cytoplasm of E. coli. The expressed fusion protein in the soluble fraction was purified by using affinity chromatography specific against urokinase. The purified fusion protein could combine the thrombus in vitro, and the specific activity of urokinase reached 80,000 IU/mg fusion protein. The result showed that the fusion protein retained the activity of two moieties, and this study laid a foundation for further research of targeting thrombolytic agent.