PGN-SAndi ultrapure peptidoglycan - NOD2 Agonist

Insoluble Peptidoglycan from Staphylococcus aureus

PGN-SAndi is an ultrapure preparation of peptidoglycan (PGN) from the Gram-positive Staphylococcus aureus.

PGN is a major component of the bacterial cell wall. It is mainly single-layered in Gram-negative bacteria (e.g. E. coli) and multi-layered in Gram-positive bacteria (e.g. B. subtilis). PGN is a large polymeric molecule made of glycan strands connected by short peptides. PGN structure varies among bacterial species at the level of sugar polymers, and of cross-linked amino acids. In Gram-positive bacteria, the amino-acid side chain structure consists of L-alanine, D-glutamate, L-lysine, and D-alanine. In Gram-negative bacteria, the L-Lysine is replaced by meso-diaminopimelic acid (mDAP or meso-DAP) [1].

PGN, either intact or fragmented, is sensed by the innate immune system through different PRRs (pattern recognition receptors). PGN is known to be a potent activator of NF-κB and TNF-α through TLR2, although it has been reported that PGN agonist activity for TLR2 is likely relying on other commonly co-purified molecules, such as cell wall lipoproteins and lipoteichoic acids (LTAs). The role of TLR2 in the direct recognition of PGN remains controversial, and the discrepancies among studies may arise from the purification methods as well as from the variation in PGN structure in the different bacterial species [1-2].

PGN-SAndi ultrapure from S. aureus is an insoluble preparation of PGN purified by detergent lysis and hydrolysis under basic conditions to eliminate lipophilic constituents. This PGN preparation does not activate TLR2-transfected HEK293 cells, but it still activates NOD2-transfected cells. 

KEY FEATURES OF PGN-SAndi:

• Ultrapure preparation of peptidoglycan from Staphylococcus aureus
• Insoluble
• Functionally tested using cellular reporter assays
• NOD2 agonist

References:

1. Wolf A.J. & Underhill D.M., 2018. Peptidoglycan recognition by the innate immune system. Nat. Rev. Immunol. 18(4):243-254.
2. Travassos.LH. et al., 2004. Toll-like receptor 2-dependent bacterial sensing does not occur via peptidoglycan recognition. EMBO Rep. 5(10):1000-1006.