What component of the bacterial cell wall is specifically targeted by lysozyme?

Lysozyme specifically targets peptidoglycan, which is a crucial component of the bacterial cell wall. This enzyme acts by hydrolyzing the β-1,4-glycosidic bonds between the N-acetylglucosamine and N-acetylmuramic acid subunits that make up the peptidoglycan layer, leading to the weakening of the cell wall. This action ultimately results in cell lysis, particularly in Gram-positive bacteria, which have a thick peptidoglycan layer. Understanding this mechanism is essential when discussing the inherent resistance of various bacteria to lysozyme, particularly those with modifications to their peptidoglycan structure or those that possess outer membranes preventing enzyme access.

The other components mentioned do not serve as targets for lysozyme; lipopolysaccharides, found predominantly in the outer membrane of Gram-negative bacteria, contribute to structural integrity but do not involve enzymatic cleavage by lysozyme. Teichoic acids are polysaccharides found in the cell wall of Gram-positive bacteria, also unrelated to lysozyme activity. Protein membranes have various functions but are not directly affected by lysozyme. Therefore, focusing on peptidoglycan highlights its vulnerability to lysozyme