Peptidoglycan recognition proteins: a novel family of four human innate immunity pattern recognition molecules.

Article Details

Citation

Liu C, Xu Z, Gupta D, Dziarski R

Peptidoglycan recognition proteins: a novel family of four human innate immunity pattern recognition molecules.

J Biol Chem. 2001 Sep 14;276(37):34686-94. Epub 2001 Jul 18.

PubMed ID
11461926 [ View in PubMed
]
Abstract

The innate immune system recognizes microorganisms through a series of pattern recognition receptors that are highly conserved in evolution. Insects have a family of 12 peptidoglycan recognition proteins (PGRPs) that recognize peptidoglycan, a ubiquitous component of bacterial cell walls. We report cloning of three novel human PGRPs (PGRP-L, PGRP-Ialpha, and PGRP-Ibeta) that together with the previously cloned PGRP-S, define a new family of human pattern recognition molecules. PGRP-L, PGRP-Ialpha, and PGRP-Ibeta have 576, 341, and 373 amino acids coded by five, seven, and eight exons on chromosomes 19 and 1, and they all have two predicted transmembrane domains. All mammalian and insect PGRPs have at least three highly conserved C-terminal PGRP domains located either in the extracellular or in the cytoplasmic (or in both) portions of the molecules. PGRP-L is expressed in liver, PGRP-Ialpha and PGRP-Ibeta in esophagus (and to a lesser extent in tonsils and thymus), and PGRP-S in bone marrow (and to a lesser extent in neutrophils and fetal liver). All four human PGRPs bind peptidoglycan and Gram-positive bacteria. Thus, these PGRPs may play a role in recognition of bacteria in these organs.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Peptidoglycan recognition protein 3Q96LB9Details
N-acetylmuramoyl-L-alanine amidaseQ96PD5Details