Peptidoglycan recognition protein S (PGRP-S)

Peptidoglycan recognition protein S (PGRP-S) is a soluble pattern recognition receptor of the innate immune system that binds bacterial peptidoglycans, a major component of bacterial cell walls, especially from Gram-positive bacteria[1][2][3][4][7]. Highly conserved from insects to mammals, PGRP-S is localized in the granules of human neutrophils and secreted into serum following immune cell activation[2][4]. Upon binding peptidoglycan, PGRP-S can enhance phagocytosis of bacteria by macrophages, increase monocyte/macrophage activation, upregulate surface markers such as CD14, CD80, and CD86, and promote secretion of pro-inflammatory cytokines, contributing to host defense against bacterial infections[2]. It may also protect immune cells from peptidoglycan-induced apoptosis and modulate inflammation[2]. While PGRP-S is not itself bactericidal under some tested conditions, it acts synergistically with other antimicrobial proteins. Structurally, PGRP-S shares overall folding characteristics with other members of the PGRP family and contains binding sites for both peptidoglycan and potentially other host effector molecules[1][3]. No drugs are currently known to directly target PGRP-S, but it is an area of interest as a potential biomarker and modulator for infection and inflammation[2][4][7].

Other names

PGRP-SPGLYRP1Peptidoglycan recognition protein shortPeptidoglycan recognition protein 1

Binds bacterial peptidoglycan, modulates immune cell activity, enhances immune signaling, increases phagocytosis and activation of macrophages