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Human lysozyme is a recombinant antimicrobial enzyme (1,4-beta-N-acetylmuramidase) that serves as a critical component of the human innate immune system, naturally found in secretions such as breast milk, tears, and saliva. It functions by hydrolyzing the beta-1,4-glycosidic bonds in the peptidoglycan of bacterial cell walls, leading to bacterial lysis. As a therapeutic, human lysozyme is being developed to modulate the gut microbiome and enhance intestinal mucosal immunity. Specifically, it is undergoing Phase I clinical trials for the prevention of graft-versus-host disease (GVHD) in patients undergoing allogeneic hematopoietic stem cell transplantation. For these applications, the protein is typically expressed in transgenic systems, such as the milk of genetically engineered goats or in rice (*Oryza sativa*). Additionally, human lysozyme is a significant model in the study of systemic hereditary amyloidosis (SHA), a condition characterized by the misfolding and aggregation of lysozyme variants into amyloid fibrils.
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