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- W1512715938 abstract "Abstract Toll-like receptors recognize diverse conserved pathogen-associated molecular patterns (PAMPs). TLR2 has the broadest ligands repertoire, including bacterial lipidated and non-lipidated proteins such as porins. TLR2/porins interaction is possibly based on electrostatic attraction. PorB porin, expressed by all Neisseriae, has significant strain-specific sequence variability within the putative TLR2-binding regions. PorB from commensal N.lactamica (NL) and pathogenic N.meningitidis (NM) bind to TLR2 in vitro with different specificity and induce inflammatory responses of different magnitude. Whole NM is also more potent than NL in inducing cell activation. A TLR2-binding signature sequence in the PorB surface exposed loops might influence specific interaction with TLR2 and activation of signaling pathways. Exchange of NM PorB for NL PorB in NM induces attenuated inflammatory responses. To identify PorB/TLR2 interactive domains (and possibly TLR1) and to provide a mechanistic explanation for their different activity, we have expressed PorB mutants with altered loops sequences and show a gradient of cell activation. However, hybrid PorB mutants bind to TLR2 in vitro. This possibly suggests that the reduced activity of PorB mutant could be due to non-functional TLR2 heterodimerization with TLR1." @default.
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- W1512715938 date "2012-05-01" @default.
- W1512715938 modified "2023-09-23" @default.
- W1512715938 title "TLR2 molecular recognition of PorB from commensal Neisseria lactamica (180.6)" @default.
- W1512715938 doi "https://doi.org/10.4049/jimmunol.188.supp.180.6" @default.
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