Alternative titles; symbolsPEPTIDOGLYCAN RECOGNITION PROTEIN, LONG; PGRPLHGNC Approved Gene Symbol: PGLYRP2Cytogenetic location: 19p13.12 Genomic coordinates...
Alternative titles; symbols
HGNC Approved Gene Symbol: PGLYRP2
Cytogenetic location: 19p13.12 Genomic coordinates (GRCh38): 19:15,468,644-15,479,500 (from NCBI)
Peptidoglycan recognition proteins, such as PGRPL, are part of the innate immune system and recognize peptidoglycan, a ubiquitous component of bacterial cell walls.
▼ Cloning and Expression
By searching an EST database for homologs of PGRPS (PGLYRP1; 604963), followed by PCR of a pooled cDNA library and a liver cDNA library, Liu et al. (2001) cloned full-length PGRPL. The deduced 576-amino acid precursor protein contains an N-terminal signal peptide, followed by 2 transmembrane segments and an extracellular C terminus containing PGRP domains III, II, and I. PGRPL shares 40%, 33%, and 32% identity with PGRPS, PGRPI-alpha (608197), and PGRPI-beta (608198), respectively. RNA dot blot analysis detected strong PGRPL expression in adult liver and weak expression in fetal liver. Northern blot analysis detected 2.1- and 0.8-kb transcripts expressed in adult and fetal liver. PCR also detected low expression in transverse colon, lymph nodes, heart, thymus, pancreas, descending colon, stomach, and testis. Transiently transfected COS-7 and human embryonic kidney cells expressed PGRPL as a Triton X-100-soluble membrane protein with an apparent molecular mass of 65 kD.
▼ Gene Function
Liu et al. (2001) determined that recombinant PGRPL expressed by COS-7 cells and human embryonic kidney cells bound to gram-positive bacteria, B. subtilis and M. luteus, with high affinity.
Xu et al. (2004) determined that murine Pgrpl is a secreted serum protein that can form multimers, most likely homodimers.
▼ Gene Structure
Liu et al. (2001) determined that the PGRPL gene contains 5 exons.
By genomic sequence analysis, Liu et al. (2001) mapped the PGRPL gene to chromosome 19.
▼ Animal Model
Xu et al. (2004) created Pgrpl-deficient mice. They found that Pgrpl contributed little to systemic challenge using gram-negative bacteria, gram-positive bacteria, or yeast. Peritoneal macrophages from Pgrpl-deficient mice produced decreased amounts of the inflammatory cytokines Il6 (147620) and Tnfa (191160) when stimulated with E. coli or lipopolysaccharide, but comparable amounts when stimulated with S. aureus, C. albicans, or their cell wall components. The cells produced similar amounts of cytokines when challenged with gram-positive or gram-negative peptidoglycans. Xu et al. (2004) concluded that, in contrast to its critical role in immunity in flies, Pgrpl is largely dispensable for mammalian immunity against bacteria and fungi.