PGN-SA peptidoglycan preparation - TLR2 Agonist

Peptidoglycan from S. aureus

PGN-SA  is a peptidoglycan (PGN) preparation from the Gram-positive bacterium Staphylococcus aureus.

PGN, a major component of the bacterial cell wall, is a large polymeric molecule made of glycan strands connected by short peptides. It is mainly single-layered in Gram-negative bacteria (e.g. E. coli) and multi-layered in Gram-positive bacteria (e.g. B. subtilis). The structure of PGN varies among bacterial species at both 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, whereas n 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 agonistic 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].

Key Features of PGN-SA:

• Preparation of peptidoglycan from Staphylococcus aureus
• Functionally-tested using cellular reporter assays
• Potent TLR2 agonist

InvivoGen also offers ultrapure PGNs as NOD1/NOD2 agonists, and which do not activate TLR2 nor TLR4.

Reference:

1. Wolf A.J. & Underhill D.M., 2018. Peptidoglycan recognition by the innate immune system. Nat. Rev. Immunol. 18(4):243-254.