肽聚糖识别蛋白(PGRPs或PGLYRPs)是先天免疫分子，包含一个保守的肽聚糖结合2型酰胺酶结构域，与噬菌体和细菌2型酰胺酶同源(Kang D et al. 1998;刘灿等2001;Royet J and Dziarski R 2007;Royet J et al. 2011;Dziarski R et al. 2016)。哺乳动物有四个pgrp家族(PGLYRP1、2,3和4)，它们以细胞类型或组织特异性的方式差异表达。PGLYRP2(也称为PGRP-L)在肝脏中组成性表达，并以非二硫联二聚体的形式分泌到血液中(Liu C et al. 2001;张勇等2005;De Pauw P et al. 1995;Hoijer MA et al. 1996)。 PGLYRP2 expression can be also induced in the skin and intestine upon exposure to bacteria or pro-inflammatory cytokines (Wang H et al. 2005; Li X et al. 2006). The constitutive expression of PGLYRP2 in the liver and induced expression in epithelial cells is regulated by different transcription factors, the binding sequences for which are located in different regions of the pglyrp2 promoter (Li X et al. 2006). PGRP2 binds to bacterial cell wall peptidoglycan and functions as N‑acetylmuramoyl‑L‑alanine amidase that hydrolyzes the amide bond between the MurNAc and L‑alanine in peptidoglycan (Wang ZM et al. 2003; Zhang Y et al. 2005). The minimal peptidoglycan fragment hydrolyzed by PGLYRP2 is MurNAc-tripeptide (Wang ZM et al. 2003). PGLYRP2 has a conserved Zn(2+)‑binding site in the peptidoglycan‑binding groove, which is also present in bacteriophage type 2 amidases, and PGLYRP2 requires Zn(2+) for its amidase activity (Wang ZM et al. 2003). The amidase activity of mammalian PGLYRP2 is though to eliminate the pro‑inflammatory peptidoglycan and, therefore, prevent over‑activation of the immune system and excessive inflammation (Hoijer MA et al. 1997; Royet J and Dziarski R 2007). In addition to its amidase activity, PGLYRP2 also has antibacterial activity against both Gram-positive and Gram-negative bacteria and Chlamydia (Bobrovsky P et al. 2016), similar to PGLYRP1, PGLYRP3, and PGLYRP4 (Lu X et al. 2006; Wang M et al. 2007).