However, the mechanism by which PGRPs are able to kill bacteria had not been determined.
The research team led by Roman Dziarski, professor of microbiology and immunology at Indiana University School of Medicine - Northwest, found that the PGRPs are able to induce a suicide response in the targeted bacteria.
The PGRPs accomplish the mission by binding to specific sites in bacterial cell walls in ways that exploit a bacterial defense mechanism known as protein-sensing two-component systems.
These systems, which normally enable the bacteria to detect and eject malformed proteins, interpret the PGRPs as just such malformed proteins.
PGN may promote localized inflammation in non-mucosal sites by stimulating the production of PGRPs. Among four known human sub-types of PGRP, PGLYRP-1 is expressed primarily in PMN granules, likely functioning as an antibacterial protein.
In addition, all PGRP protect cells from PGN-nduced apoptosis.
PGRPs are a family of pattern recognition receptors (PRRs) that bind to, and in some cases hydrolyze the peptidoglycans (PGNs) of bacterial cell walls (Nylund et al., 2017).
Later, the names for human PGRPs are changed by the Human Genome Organization Gene Nomenclature Committee to PGLYRP1, PGLYRP2, PGLYRP3, and PGLYRP4, respectively, and this nomenclature has been adopted for all mammalian PGRPs (Cong et al., 2009).
PGRPs influence host-pathogen interactions not only through their antibacterial or peptidoglycan hydrolytic properties (Yang et al., 2017), but also through their pro-inflammatory and anti-inflammatory properties that are independent of their hydrolytic and antibacterial activities (Wang et al., 2016a).