Disease relevance of Pglyrp2

• All detected splice variant isoforms of TagL bound Gram-positive, Gram-negative bacteria and peptidoglycan [1].
• Using gene targeting to create PGRP-L-deficient mice, we demonstrate little contribution by PGRP-L to systemic challenge using gram-negative bacteria (Escherichia coli, slightly less susceptible), Gram-positive bacteria (Staphylococcus aureus), or yeast (Candida albicans) [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 [3].

High impact information on Pglyrp2

• Peritoneal macrophages from PGRP-L-deficient mice produced decreased amounts of the inflammatory cytokines interleukin 6 and tumor necrosis factor alpha when stimulated with E. coli or lipopolysaccharide, but comparable amounts when stimulated with S. aureus, C. albicans, or their cell wall components [2].
• Here we describe a splicing pattern of the tagL gene, mouse member of tag7/PGRP family [1].
• Accordingly to the predicted transmembrane domains, mouse TagL may be secreted as inducible proteins or retained on intracellular membranes [1].
• Efficient phagosome escaping but not efficient invasion helped bacteria to overplay TagL [3].
• Molecular cloning of a new mouse gene tagL containing a lysozyme-like domain [4].

References