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• W2029116670 abstract "TIR (Toll/interleukin-1 receptor) domain-containing proteins play a crucial role in innate immunity in eukaryotes. Brucella is a highly infectious intracellular bacterium that encodes a TIR domain protein (TcpB) to subvert host innate immune responses to establish a beneficial niche for pathogenesis. TcpB inhibits NF-κB (nuclear factor κB) activation and pro-inflammatory cytokine secretions mediated by TLR (Toll-like receptor) 2 and TLR4. In the present study, we have demonstrated that TcpB modulates microtubule dynamics by acting as a stabilization factor. TcpB increased the rate of nucleation as well as the polymerization phases of microtubule formation in a similar manner to paclitaxel. TcpB could efficiently inhibit nocodazole- or cold-induced microtubule disassembly. Microtubule stabilization by TcpB is attributed to the BB-loop region of the TIR domain, and a point mutation affected the microtubule stabilization as well as the TLR-suppression properties of TcpB." @default.
• W2029116670 created "2016-06-24" @default.
• W2029116670 creator A5054973028 @default.
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• W2029116670 date "2011-09-14" @default.
• W2029116670 modified "2023-09-27" @default.
• W2029116670 title "Modulation of microtubule dynamics by a TIR domain protein from the intracellular pathogen <i>Brucella melitensis</i>" @default.
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• W2029116670 doi "https://doi.org/10.1042/bj20110577" @default.
• W2029116670 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3513345" @default.
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