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Structure of the mouse Toll-like receptor 13 ectodomain in complex with a conserved sequence from bacterial 23S ribosomal RNA has been presented.
S. pyogenes is initially recognized in a phagocytosis-independent manner by TLR2 and subsequently by TLR13 upon internalization.
TLR13 expressed by immune cells detects bacterial RNA with exquisite sequence specificity.
These data lend support to the conclusion that TLR13 participates in group B streptococcus recognition, although blockade of the function of this receptor can be compensated for by other endosomal toll (zeige TLR4 Proteine)-like receptors.
TLR13 activation contributes to the innate response to Gram-positive bacteria, identifying TLR13 as a receptor for bacterial RNA.
these results show that the orphan receptor (zeige NR1D2 Proteine) TLR13 in mice recognizes a conserved 23S ribosomal RNA (rRNA) sequence that is the binding site of macrolide, lincosamide, and streptogramin group (MLS) antibiotics (including erythromycin) in bacteria. Notably
the potential role of the novel Toll (zeige TLR4 Proteine)-like receptor tlr13 in the recognition of viral infection.
These findings reveal the mechanism of Tlr13 gene regulation, thereby providing insight into the function of Tlr13 in the immune response to pathogen.
Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. Acts via MYD88 and TRAF6, leading to NF-kappa-B. activation, cytokine secretion and the inflammatory response (By similarity).
, Toll-like receptor 13