Lysozymes are ancient and important components of the innate immune system of animals that hydrolyse peptidoglycan, the major bacterial cell wall polymer. Various mechanisms have evolved by which bacteria can evade this bactericidal enzyme, one being the production of lysozyme inhibitors. MliC (membrane bound lysozyme inhibitor of c-type lysozyme) of E. coli and Pseudomonas aeruginosa, possess lysozyme inhibitory activity and confer increased lysozyme tolerance upon expression in E. coli [1]. Structural analyses show that the invariant loop of MliC plays a crucial role in the inhibition of the lysozyme by its insertion into the active site cleft of the lysozyme, where the loop forms hydrogen and ionic bonds with the catalytic residues [2]. [1]. 18369469. A new family of lysozyme inhibitors contributing to lysozyme tolerance in gram-negative bacteria. Callewaert L, Aertsen A, Deckers D, Vanoirbeek KG, Vanderkelen L, Van Herreweghe JM, Masschalck B, Nakimbugwe D, Robben J, Michiels CW;. PLoS Pathog. 2008;4:e1000019. [2]. 19028453. Structural basis for the recognition of lysozyme by MliC, a periplasmic lysozyme inhibitor in Gram-negative bacteria. Yum S, Kim MJ, Xu Y, Jin XL, Yoo HY, Park JW, Gong JH, Choe KM, Lee BL, Ha NC;. Biochem Biophys Res Commun. 2009;378:244-248. (from Pfam)
- Date:
- 2024-10-16