Adaptive remodeling of cell wall peptidoglycan architecture in Dermacoccus abyssi HZAU 226 under lysozyme-induced stress

Lysozyme is widely used as a natural food biopreservative, yet the emergence of lysozyme-resistant microorganisms poses severe threats to food safety. As the structural backbone and direct target of lysozyme, peptidoglycan is crucial in determining bacterial susceptibility. Here, we combined atomic force microscopy and ultra-performance liquid chromatography to investigate how the tolerant food spoilage bacterium Dermacoccus abyssi HZAU 226 remodels its peptidoglycan under lysozyme stress. Elevated lysozyme concentrations induced significant cellular elongation and markedly increased surface roughness. Structurally, the cell wall architecture became increasingly porous and disordered, primarily due to reduced peptidoglycan cross-linking. Chemically, this stress triggered elevated muropeptide monomer abundance, diminished multimers, and significantly enhanced O -acetylation. Mechanistically, these integrated modifications paradoxically resulted in a stiffer and more adhesive cell surface. These findings reveal a multi-faceted adaptive strategy at the nanoscale, explaining bacterial persistence and offering a roadmap for improving lysozyme-based food preservation.