Disease relevance of Pglyrp1

• Neutrophils from PGRP-S-/- mice have normal phagocytic uptake of bacteria but are defective in intracellular killing and digestion of relatively nonpathogenic gram-positive bacteria [1].
• We show that mouse PGRP-S is present in neutrophil tertiary granules and that PGRP-S-deficient (PGRP-S-/-) mice have increased susceptibility to intraperitoneal infection with gram-positive bacteria of low pathogenicity but not with more pathogenic gram-positive or gram-negative bacteria [1].
• Mammalian peptidoglycan recognition protein TagL inhibits Listeria monocytogenes invasion into epithelial cells [2].
• To elucidate its functions, a mouse member of the peptidoglycan recognition proteins family, TagL, was stably expressed in colon adenocarcinoma HT29 cells, and its effect on the invasion and intracellular growth of the enteroinvasive pathogenic bacterium Listeria monocytogenes was assessed [2].
• A homology search revealed that the homologs of silkworm PGRP are present in mice, nematodes, and bacteriophages [3].

High impact information on Pglyrp1

• Insect peptidoglycan recognition protein-S (PGRP-S), a member of a family of innate immunity pattern recognition molecules conserved from insects to mammals, recognizes bacterial cell wall peptidoglycan and activates 2 antimicrobial defense systems, prophenoloxidase cascade and antimicrobial peptides through Toll receptor [1].
• We have isolated from M. sexta hemolymph a group of proteins (hemolin, peptidoglycan recognition proteins, beta-1,3-glucan recognition proteins, and C-type lectins), which serve as a surveillance mechanism by binding to microbial surface molecules (e.g. peptidoglycan, lipopolysaccharide, lipoteichoic acid, and beta-1,3-glucan) [4].
• We cloned cDNA encoding PGRP from the silkworm fat body cDNA library [3].
• Northern blot analysis showed that the PGRP gene is constitutively expressed in the fat body, epithelial cell, and hemocytes of naive silkworms [3].
• The soluble form of Tag7 triggers apoptosis in mouse L929 cells in vitro and does not involve NF-kappaB activation [5].

Biological context of Pglyrp1

• The potential function of these PGRP proteins as pattern recognition receptors and their distinctive cellular distribution suggests a complex coordination among specialized cells of the FAE in triggering mucosal immunity and innate immune responses [6].

Anatomical context of Pglyrp1

• Peptidoglycan recognition protein expression in mouse Peyer's Patch follicle associated epithelium suggests functional specialization [6].
• METHODS: Transiently or stably genetically modified mouse tumor cell lines expressing Tag7 were used [7].
• CONCLUSIONS: We can conclude that secretion of the Tag7 protein by genetically modified cells can induce mobilization of antigen-presenting cells and innate effectors [7].
• We have previously isolated a novel mouse gene tag7/PGRP that was shown to be involved in the innate component of the immune system, and its insect homologue is an upstream mediator of Toll signaling in Drosophila [7].

Other interactions of Pglyrp1

• Here we describe a splicing pattern of the tagL gene, mouse member of tag7/PGRP family [8].
• Toll-like receptor 2-dependent bacterial sensing does not occur via peptidoglycan recognition [9].

Analytical, diagnostic and therapeutic context of Pglyrp1

• Immunotherapy with autologous tumor cells engineered to secrete Tag7/PGRP, an innate immunity recognition molecule [7].
• RT-PCR and immunocytochemistry assays were used to show that murine HSCs expressed specific mRNA transcripts and proteins for LPS and lipoteichoic acid (LTA) receptor systems and peptidoglycan recognition proteins [10].

References