In vitro spleen cell cytokine responses of adult mice immunized with a recombinant PorA (major outer membrane protein [MOMP]) from Campylobacter jejuni.

No information on the cytokine profile to be used as a marker of Campylobacter jejuni infection protection. For this study, we used the outer membrane protein (MOMP [Pora]) as a vaccine for the protection and spleen cell cytokine as a marker of protection.

We cloned and expressed Pora from C. jejuni111 and mice immunized with intraperitoneal route. Subsequently, the mice orally challenged with C. jejuni 111.

live vaccine-induced protection as evidenced by a decrease in fecal excretion C. jejuni111. Cytokines were measured in vitro after stimulation of spleen cells with MOMP. Levels of pro-inflammatory cytokines, IL-12, TNF-α, IL-17A and IL-17F are similar in the control and test mice. Levels of pro-inflammatory cytokines, IL-2 and IFN-γ were higher in mice than in control mice test, and the level of pro-inflammatory cytokines, IL-8 and IL-1β was higher in the test mice than in control mice.

In between the two anti-inflammatory cytokines, the same level of IL-10 but higher for IL-4 in the test mice than in control mice. The ratio of pro-inflammatory anti-inflammatory cytokines showed a bias towards anti-inflammatory response in support of the production of antibodies that reflect the role of antibodies in immunity.

Cytokine patterns of production by spleen cells can be used as a marker of protection in a mouse model.

A New Efficient Method for Production of Recombinant Antitumor Cytokine TRAIL and Its Receptor-Selective Variant DR5-B.

The cytokine TRAIL induces apoptosis in tumor cells of various origin without affecting normal cells. clinical trials of TRAIL receptors (DR4 and DR5) agonist (recombinant TRAIL or death receptor antibodies) have largely failed because most human tumors are resistant to them. Today, the second generation of targeted agents in TRAIL-R with improved efficiency have been developed. To this end, we have developed DR5-B, selective TRAIL variants interact with DR5. We have developed a new efficient method for the production of TRAIL and DR5-B uses this protein expression in Escherichia coli strain B. Shuffle protein fractions isolated from the cytoplasm of cells and purified to a high degree of homogeneity using metal-affinity and ion exchange chromatography. The results of the protein is 211 and 173 mg from one liter of cell culture for DR5-B and TRAIL, respectively, which significantly exceed the results obtained by other methods. DR5-B kill tumor cells of different origins is more efficient and faster than TRAIL. The resulting preparation can be used for the study of TRAIL signaling pathways and in preclinical and clinical trials as an antitumor agent.