Autolysin (Atl) (Atl)

Autolysins are a diverse class of endogenous bacterial enzymes, including N-acetylmuramoyl-L-alanine amidases and glucosaminidases, that catalyze the hydrolysis of peptidoglycan in the cell wall [1.1.1, 1.3.1]. They are essential for fundamental bacterial processes such as cell wall turnover, cell division, and the separation of daughter cells [1.2.1, 1.4.3]. In pathogenic species like Staphylococcus aureus and Streptococcus pneumoniae, autolysins (such as Atl and LytA) also function as virulence factors by facilitating biofilm formation, host tissue adhesion, and the concealment of inflammatory peptidoglycan fragments from the host immune system [1.2.1, 1.2.3, 1.5.2]. As therapeutic targets, autolysins are central to the action of traditional bactericidal antibiotics like beta-lactams, which trigger uncontrolled autolysis to kill bacteria [1.3.1, 1.3.3]. Conversely, novel small-molecule inhibitors like complestatin and corbomycin target these enzymes to prevent cell wall remodeling, thereby inhibiting growth and attenuating virulence [1.3.1, 1.5.2]. Additionally, exogenous phage-derived autolysins, known as lysins or enzybiotics, are being developed as highly specific, fast-acting antimicrobial agents capable of rapidly lysing multi-drug resistant pathogens [1.4.1, 1.4.2].

Other names

Peptidoglycan hydrolaseMurein hydrolaseCell wall hydrolaseLytAAtlAAtlEN-acetylmuramoyl-L-alanine amidaseEndo-beta-N-acetylglucosaminidase

Autolysins are targeted through three primary mechanisms: (1) activation of endogenous autolysins by bactericidal antibiotics (e.g., beta-lactams, vancomycin) to induce cell lysis; (2) direct enzymatic degradation of the bacterial cell wall by exogenous lysins (enzybiotics like exebacase); and (3) inhibition of autolysin-mediated cell wall remodeling by specific inhibitors (e.g., complestatin, corbomycin) to arrest growth and reduce virulence [1.3.1, 1.3.3, 1.4.1, 1.4.2, 1.5.2].