Peptidoglycan recognition protein 2 (PGLYRP2)

Peptidoglycan recognition protein 2 (PGLYRP2) is a secreted, liver-expressed enzyme belonging to the N-acetylmuramoyl-L-alanine amidase family, acting as a pattern recognition receptor in the innate immune system. It specifically hydrolyzes the amide bond between N-acetylmuramic acid and L-alanine in bacterial peptidoglycan, aiding in the neutralization of bacterial components and damping excessive immune reactions. Unlike some related proteins, PGLYRP2 has limited direct bactericidal activity but modulates immune responses, particularly by influencing chemokine networks such as CCL5, critical for immune cell recruitment in tumors. Recent studies reveal roles for PGLYRP2 in antitumor immunity (especially in the liver) and in direct antiviral defense by binding and sequestering viral DNA (notably hepatitis B virus), positioning it as a potential biomarker or therapeutic target in both infectious and oncological contexts. Deficiency or epigenetic silencing of PGLYRP2 is associated with increased risk or progression of hepatocellular carcinoma, highlighting its importance in immune surveillance of the liver.

Other names

N-acetylmuramoyl-L-alanine amidasePGLYRP2PGLYRPLPGRPLUNQ3103/PRO10102PGRP-LPeptidoglycan recognition protein longpeptidoglycan recognition protein Lpeptidoglycan recognition protein L precursorpeptidoglycan recognition protein-likeTAGL-liketagLtagL-alphatagl-betaHMFT0141

Hydrolysis of peptidoglycan, rendering bacterial components inactive and modulating immune signaling. Immune modulation by influencing chemokine (CCL5) transcription in the tumor context. Direct binding to viral (HBV) DNA, inhibiting viral replication by sequestration and interference with nucleocapsid assembly.