2 in a row. Breakthrough, Tongji University Gobao And others found the host for the new type of mycobacterium tuberculosis immune regulation mechanism.

Inature Mycobacterium tuberculosis is an intracellular pathogen, which uses a variety of strategies to interfere with the signal transduction function of host immune molecules.many other bacterial pathogens use the ubiquitination system of host protein to promote the pathogenesis, but whether the system regulates the protein ubiquitination of Mycobacterium tuberculosis protein is not clear.on January 15, 2020, GE Baoxue of Tongji University and Rao Zihe of Shanghai University of science and technology published an online publication entitled "host mediated ubiquitation of a mycobacterial protein suppresses" in nature This study found that host E3 ubiquitin ligase anapc2 (core subunit of late promoter complex / loop) interacts with Mycobacterium protein rv0222, and promotes the attachment of ubiquitin chain of lysine 11 to lysine 76 of rv0222, thus inhibiting the expression of proinflammatory cytokines.in conclusion, the findings identified a previously unrecognized mechanism by which Mycobacterium tuberculosis can inhibit host immunity and provided insights into the development of effective immune modulators against Mycobacterium tuberculosis.in addition, on October 25, 2018, GE Baoxue of Tongji University, Mao Zhiyong and other research groups jointly published the topic "nuclear CGAs suppresses DNA repair and promoters" on nature This study revealed that nuclear CGAs inhibits homologous recombination mediated repair and promotes tumor growth. Therefore, CGAs is a potential target for cancer prevention and treatment (click read).Mycobacterium tuberculosis is an intracellular pathogen that uses a variety of strategies to interfere with the signal transduction function of host immune molecules.many other bacterial pathogens use the ubiquitination system of host protein to promote the pathogenesis, but whether the system regulates the protein ubiquitination of Mycobacterium tuberculosis protein is not clear.here, the researchers report that the host E3 ubiquitin ligase anapc2 (the core subunit of late promoter complex / loop) interacts with Mycobacterium protein rv0222 and promotes the attachment of lysine 11 linked ubiquitin chain to lysine 76 of rv0222, thus inhibiting proinflammatory cytokine expression.the inhibitory effect of rv0222 on proinflammatory response was eliminated by specific short hairpin RNA.in addition, the mutation of ubiquitination site on rv0222 can weaken the inhibitory effect of rv0222 on proinflammatory cytokines and reduce the virulence during infection in mice.in terms of mechanism, the ubiquitination of lysine 11 connection of rv0222 by anapc2 promoted the recruitment of protein tyrosine phosphatase SHP1 to the adaptor protein TRAF6, thus preventing the ubiquitination of lysine 63 and the activation of TRAF6.the findings of this study identified a previously unknown mechanism by which Mycobacterium tuberculosis can inhibit host immunity, and provided insights into the development of effective immune modulators against Mycobacterium tuberculosis.reference message: