Peptidoglycan recognition protein 3 (PGLYRP3)

Peptidoglycan recognition protein 3 (PGLYRP3) is a secreted, glycosylated pattern recognition receptor that binds to peptidoglycan, a major component of bacterial cell walls, with a preference for fragments derived from Gram-positive cocci[1][2]. It is part of the innate immune system and plays a key role in the first line of defense against infections by directly killing or inhibiting certain bacteria and modulating inflammatory responses[1][2][3]. PGLYRP3 is mainly expressed in epithelial tissues such as the skin, eye, tongue, throat, and esophagus, and is upregulated by bacterial stimuli[1]. Although it belongs to the N-acetylmuramoyl-L-alanine amidase 2 family, PGLYRP3 does not have enzymatic amidase activity but functions through direct interaction with bacterial cell wall components[1][2]. It forms disulfide-linked homodimers or heterodimers (with PGLYRP4), and disruptions in PGLYRP3 expression can influence microbiome composition, susceptibility to infection, and inflammation[1][2]. No approved drugs currently directly target PGLYRP3, but its role in innate immunity and host–microbe interactions makes it a topic of interest in studies of infections, inflammation, and microbiome-associated diseases[1][2][3].

Other names

Peptidoglycan recognition protein 3PGLYRP3PGRPIAPGLYRPIalphaPGRP-I-alphaPGRP-IαPeptidoglycan recognition protein I-alphaPeptidoglycan recognition protein intermediate alphapeptidoglycan recognition protein I alpha precursorPGRP-Ialphapeptidoglycan recognition protein I alphapeptidoglycan recognition protein intermediate alpha

Binds to bacterial peptidoglycan, interfering with its biosynthesis and maturation, leading to bacterial death or inhibition[1][2][3].