Native versus recombinant high-mobility group B1 proteins: functional activity in vitro.

To compare the functional activity of native HMGB1 proteins from eukaryotic sources with HMGB1 from prokaryotic sources the cDNAs of human and murine HMGB1 were cloned and the proteins expressed in bacteria. Tissue-derived HMGB1 from calf thymus and HMGB1 secreted from Chinese hamster ovary (CHO) cells were purified. Human whole blood, THP-1 cells, and NIH/3T3 cells were exposed to HMGB1 proteins and the induction of tumor necrosis factor-alpha (TNF-alpha) release in whole blood and monocytic THP-1 cells and a proliferation assay in NIH/3T3 cells were used to study functional activity of HMGB1s in vitro.

Immunochemical detection of prion protein on dipsticks prepared with crystalline bacterial cell-surface layers.

Background: Transmissible spongiform encephalopathy (TSE) represents a spectrum of diseases affecting humans and animals. A definitive diagnosis of TSEs is only possible by postmortem identification of pathologic prion protein in brain tissue that has been treated with protease. The pathologic protein is detected by Western blot analysis or ELISA methods.