Seiichi Inamura

TL;DR: NOD2 mediates the host response to bacterial muropeptides derived from peptidoglycan, an activity that is important for protection against Crohn's disease and has implications for understanding adjuvant function and effective vaccine development.

TL;DR: The data together with those reported by other groups reveal that only lipoproteins/lipopeptides are sensed at physiologically concentrations by TLR2 at picomolar levels, which implies that the activity of all other putative bacterial compounds so far reported asTLR2 agonists was most likely due to contaminating highly active natural lipoproteinins and/or lipopeptide.

TL;DR: It is reported that human PGRP-L is a Zn2+-dependent N-acetylmuramoyl-l-alanine amidase, an enzyme that hydrolyzes the amide bond between MurNAc and l-Ala of bacterial PGN and this function is conserved in prokaryotes, insects, and mammals.

TL;DR: It is revealed that TLR2 was not stimulated by the series of synthetic PG partial structures, whereas Nod2 recognizes the partial structures containing the MDP moiety.

TL;DR: A novel synthetic Lys-PGN fragment functions as a competitive inhibitor of the natural PGN-induced melanization reaction by using a T-4P2-coupled column and purified the Tenebrio molitor PGN recognition protein (Tm-PGRP) without causing activation of the prophenoloxidase.