PGLYRP3
PGLYRP3 (peptidoglycan recognition protein 3, also known as PGRPIA, PGLYRPIalpha and PGRP-Ialpha) is a secreted pattern receptor that binds bacterial peptidoglycan. It acts as an antimicrobial protein and contributes to innate immunity. Browse Assay Genie's current range of PGLYRP3 research reagents below, or read on for the biology behind the target.
PGLYRP3 is a pattern receptor that binds murein peptidoglycans (PGN), a ubiquitous component of bacterial cell walls. It binds PGN from Gram-positive bacteria and has bactericidal activity towards them, and the proposed mechanism is interference with peptidoglycan biosynthesis. It also binds Gram-negative bacteria, towards which it has bacteriostatic activity rather than killing. These properties place it among the effector molecules of innate immunity, which recognise conserved microbial structures rather than specific antigens.
The PGLYRP3 gene encodes a protein that belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. UniProt lists the protein as secreted, consistent with a role in recognising bacteria outside the cell. Together with PGLYRP1 and PGLYRP2, it is part of the HGNC gene group of peptidoglycan recognition proteins, and the mouse ortholog is Pglyrp3.
The older names PGRPIA, PGLYRPIalpha and PGRP-Ialpha appear in the literature alongside the current symbol. Researchers studying the PGLYRP3 gene or protein typically do so in the context of antimicrobial defence and host recognition of bacterial cell wall components.
PGLYRP3 is part of the innate immune system and recognises peptidoglycan, making it a subject for studies of host pattern recognition.
It is bactericidal towards Gram-positive bacteria, possibly by interfering with peptidoglycan biosynthesis, which makes it relevant to antibacterial mechanism research.
PGLYRP3 binds both Gram-positive and Gram-negative bacteria, with bactericidal and bacteriostatic effects respectively, informing work on differential bacterial responses.
As a member of the peptidoglycan recognition proteins, PGLYRP3 supports comparative work across the family and the amidase 2 family.
PGLYRP3 is a secreted pattern receptor that binds murein peptidoglycans of Gram-positive bacteria and has bactericidal activity towards them, possibly by interfering with peptidoglycan biosynthesis. It also binds Gram-negative bacteria, with bacteriostatic activity, and plays a role in innate immunity.
The HGNC-approved symbol is PGLYRP3, for peptidoglycan recognition protein 3. Aliases and previous symbols include PGRPIA, PGLYRPIalpha and PGRP-Ialpha. Searching under all of these names helps when reviewing older literature on this protein.
A mouse ortholog, Pglyrp3, is recorded for the human gene. PGLYRP3 belongs to the N-acetylmuramoyl-L-alanine amidase 2 family and sits with PGLYRP1 and PGLYRP2 in the peptidoglycan recognition protein group. Check the datasheet of any product for its validated reactivity.
Other peptidoglycan recognition proteins involved in bacterial recognition and innate immunity.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q96LB9; product specifications from Assay Genie datasheets.