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. 2022 Feb 14;9:820962. doi: 10.3389/fcvm.2022.820962

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Copyright © 2022 Bezhaeva, Karper, Quax and de Vries.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Membrane TLRs and their accessory molecules. Cell surface TLR1, TLR2, TLR4, and TLR6 are essential for the recognition of exogenous and endogenous ligands. TLR1/2, TLR2/6 heterodimers and TLR4/TLR4 homodimer utilize MyD88-dependent pathway to control inflammatory responses via activation of NF-κB and AP-1 transcription factors, endosomal TLR4 activates TRAM/TRIF-dependent pathway resulting in type I IFN responses. CD36 induces the assembly of the TLR4/6 and TLR2/6 heterodimers. CD14 can be secreted as a soluble molecule (sCD14) or a membrane bound protein (mCD14) and is involved in ligand delivery to several TLRs. LPS-binding protein (LBP) binds to lipopolysaccharide (LPS) and presents it to CD14. MD2 is necessary for TLR4 to bind to LPS and homodimerize. RP105-MD1 complex has a structural similarity to TLR4-MD2 and exerts dual regulatory activity on TLR4 and TLR2 -regulated inflammatory response. Dectin-1 facilitates TLR2 signaling whereas TRIL interacts with ligands to activate TLR4 signaling. Vitronectin enhances TLR2 and TLR4-mediated responses. Created with BioRender.com.