Sentence examples for binding to host PRRs from inspiring English sources

Limited insight into the 3D structure of ligand PRR complexes, as well as knowledge on ligand structural requirements for plant immune activation, suggests that small ligand epitopes are crucial for binding to host PRRs (Liu et al., 2012b; Sun et al., 2013).

It is generally little understood whether and how microbial patterns derived from complex extracellular assemblies, such as bacterial cell walls, are accessible to host PRRs for host immune activation in eukaryotes.

For example, binding to heat shock proteins, induction of autophagy and binding to intracellular PRRs can all activate the innate immune system [ 37, 44- 46].

Whereas PAMPs activate their cognate PRRs to elicit pro-inflammatory signalling, ACAMPs binding to PRRs induces anti-inflammatory responses (Jeannin et al, 2008).

In the resting cell, tandem SH3 domains in p47 phox (referred to as the bis-SH3 domain) bind to an auto-inhibitory region (AIR), preventing the bis-SH3 domain from binding to the PRR of p22 phox.

Phosphorylation-independent disruption of the intramolecular interaction facilitates NOXO1 binding to the PRR of p22 phox.

The vertebrate p67 phox and NOXA1 orthologs all have the C-terminal SH3 domain that, in human, mediates binding to the PRR of p47 phox and NOXO1, respectively.

In the inner ear, bacteria multiply uncontrolled and after autolysis bacterial components are released, binding to pathogen recognition receptors (PRRs) present on immunocompetent endothelial cells and fibrocytes [ 29].

FimH mediates binding to mannose containing host receptors.

In addition, OMVs are known to possess LPS and bacterial DNA that function as ligands for host PRRs [44], [45].

According to the previous model of interactions of Vav1 and Fyn with the M2 PRR, it was difficult to understand how the M2/Fyn/Vav1 complex could be assembled, since Fyn and Vav1 will be binding to the same M2 PRR.