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Vinyl‐substituted hydridopolycarbosilane (VHPCS) is widely studied for its low viscosity, abundance of active functional groups, rapid curing, and high ceramic yield. The curing reactions mainly involve the free radical polymerization of vinyl and hydrosilylation reactions, but these reactions typically require high temperatures such as 160–250°C. The curing behavior of VHPCS‐17 with a tert‐butyl peroxybenzoate/Nickel acetylacetonate (TBPB/NIAA) system is investigated using differential scanning calorimetry and in situ Fourier transform infrared. The properties of VHPCS‐17 with different initiator systems and VHPCS with different vinyl contents (under TBPB/NIAA system) are studied using thermogravimetric analysis and x‐ray diffraction. The results demonstrate that the TBPB/NIAA system can facilitate the free radical polymerization of vinyl; moreover, this system decreases the peak temperature of the curing reaction from 251 to 141°C and increases the ceramic yield from 80.49% to 89.88%. The ceramic yield of cured VHPCS increases gradually, reaching 89.88% when the vinyl content is 17%. The grain size of β‐SiC decreases continuously with the increase in vinyl content, while the high‐temperature oxidation‐resistant properties of SiC ceramics obtained from different VHPCSs are not negatively affected. [ABSTRACT FROM AUTHOR]

Internal N6-methyladenosine (m6A) modifications are among the most abundant modifications of messenger RNA, playing a critical role in diverse biological and pathological processes. However, the functional role and regulatory mechanism of m6A modifications in the immune response to Mycobacterium tuberculosis infection remains unknown. Here, we report that methyltransferase-like 14 (METTL14)-dependent m6A methylation of NAPDH oxidase 2 (Nox2) mRNA was crucial for the host immune defense against M. tuberculosis infection and that M. tuberculosis-secreted antigen EsxB (Rv3874) inhibited METTL14-dependent m6A methylation of Nox2 mRNA. Mechanistically, EsxB interacted with p38 MAP kinase and disrupted the association of TAB1 with p38, thus inhibiting the TAB1-mediated autophosphorylation of p38. Interaction of EsxB with p38 also impeded the binding of p38 with METTL14, thereby inhibiting the p38-mediated phosphorylation of METTL14 at Thr72. Inhibition of p38 by EsxB restrained liquid–liquid phase separation (LLPS) of METTL14 and its subsequent interaction with METTL3, preventing the m6A modification of Nox2 mRNA and its association with the m6A-binding protein IGF2BP1 to destabilize Nox2 mRNA, reduce ROS levels, and increase intracellular survival of M. tuberculosis. Moreover, deletion or mutation of the phosphorylation site on METTL14 impaired the inhibition of ROS level by EsxB and increased bacterial burden or histological damage in the lungs during infection in mice. These findings identify a previously unknown mechanism that M. tuberculosis employs to suppress host immunity, providing insights that may empower the development of effective immunomodulators that target M. tuberculosis. [ABSTRACT FROM AUTHOR]

Internal N 6 -methyladenosine (m 6 A) modifications are among the most abundant modifications of messenger RNA, playing a critical role in diverse biological and pathological processes. However, the functional role and regulatory mechanism of m 6 A modifications in the immune response to Mycobacterium tuberculosis infection remains unknown. Here, we report that methyltransferase-like 14 (METTL14)-dependent m 6 A methylation of NAPDH oxidase 2 (Nox2) mRNA was crucial for the host immune defense against M. tuberculosis infection and that M. tuberculosis-secreted antigen EsxB (Rv3874) inhibited METTL14-dependent m 6 A methylation of Nox2 mRNA. Mechanistically, EsxB interacted with p38 MAP kinase and disrupted the association of TAB1 with p38, thus inhibiting the TAB1-mediated autophosphorylation of p38. Interaction of EsxB with p38 also impeded the binding of p38 with METTL14, thereby inhibiting the p38-mediated phosphorylation of METTL14 at Thr72. Inhibition of p38 by EsxB restrained liquid-liquid phase separation (LLPS) of METTL14 and its subsequent interaction with METTL3, preventing the m 6 A modification of Nox2 mRNA and its association with the m 6 A-binding protein IGF2BP1 to destabilize Nox2 mRNA, reduce ROS levels, and increase intracellular survival of M. tuberculosis. Moreover, deletion or mutation of the phosphorylation site on METTL14 impaired the inhibition of ROS level by EsxB and increased bacterial burden or histological damage in the lungs during infection in mice. These findings identify a previously unknown mechanism that M. tuberculosis employs to suppress host immunity, providing insights that may empower the development of effective immunomodulators that target M. tuberculosis., (© 2024. The Author(s).)