PGLYRP4


Description

The PGLYRP4 (peptidoglycan recognition protein 4) is a protein-coding gene located on chromosome 1.

Peptidoglycan recognition protein 4 (PGLYRP4, formerly PGRP-Iβ) is an antibacterial and anti-inflammatory innate immunity protein that in humans is encoded by the PGLYRP4 gene.

PGLYRP4 (formerly PGRP-Iβ), a member of a family of human Peptidoglycan Recognition Proteins (PGRPs), was discovered in 2001 by Roman Dziarski and coworkers who cloned and identified the genes for three human PGRPs, PGRP-L, PGRP-Iα, and PGRP-Iβ (named for long and intermediate size transcripts), and established that human genome codes for a family of 4 PGRPs: PGRP-S (short PGRP or PGRP-S) and PGRP-L, PGRP-Iα, and PGRP-Iβ. Subsequently, the Human Genome Organization Gene Nomenclature Committee changed the gene symbols of PGRP-S, PGRP-L, PGRP-Iα, and PGRP-Iβ to PGLYRP1 (peptidoglycan recognition protein 1), PGLYRP2 (peptidoglycan recognition protein 2), PGLYRP3 (peptidoglycan recognition protein 3), and PGLYRP4 (peptidoglycan recognition protein 4), respectively, and this nomenclature is currently also used for other mammalian PGRPs.

PGLYRP4 has similar expression to PGLYRP3 (peptidoglycan recognition protein 3) but not identical. PGLYRP4 is constitutively expressed in the skin, in the eye, in the mucous membranes in the tongue, throat, and esophagus, in the salivary glands and mucus-secreting cells in the throat, and at a much lower level in the remaining parts of the intestinal tract. Bacteria and their products increase the expression of PGLYRP4 in keratinocytes and oral epithelial cells. Mouse PGLYRP4 is also differentially expressed in the developing brain and this expression is influenced by the intestinal microbiome. PGLYRP4 is secreted and forms disulfide-linked dimers.

PGLYRP4, similar to PGLYRP3, has two peptidoglycan-binding type 2 amidase domains (also known as PGRP domains), which are not identical (have 34% amino acid identity in humans) and do not have amidase enzymatic activity. PGLYRP4 is secreted, it is glycosylated, and its glycosylation is required for its bactericidal activity.

PGLYRP4 is a pattern recognition receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. It exhibits bactericidal activity against Gram-positive bacteria, potentially by interfering with peptidoglycan biosynthesis. PGLYRP4 also binds to Gram-negative bacteria and has bacteriostatic activity against them. It plays a role in innate immunity.

PGLYRP4 is also known as PGLYRPIbeta, PGRP-Ibeta, PGRPIB, SBBI67.

Associated Diseases



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