The LYG2 gene is located on chromosome 2q11.2 . The recombinant human LYG2 protein is a heat-resistant 20-kD protein obtained from yeast . It contains a SLT domain, which is present in bacterial lytic transglycosylase and eukaryotic lysozymes . This domain catalyzes the cleavage of the beta-1,4-glycosidic bond, contributing to its bacteriolytic function .
LYG2 is predominantly expressed in the human eye, particularly in the lacrimal gland, and to a lesser extent in the testis . Using RT-PCR, high expression levels of LYG2 were detected in the eye, while weak expression was observed in the testis . SDS-PAGE and mass spectrometric analysis have identified LYG2 in human tears .
Recombinant human LYG2 has been shown to inhibit the growth of gram-positive bacteria but does not affect gram-negative bacteria or Candida albicans . Interestingly, the addition of lysozyme C (LYZ) does not enhance LYG2 activity . This specificity suggests that LYG2 plays a unique role in the immune defense mechanism against certain bacterial infections.
The regulatory mechanisms governing LYG2 expression and activity are not fully understood. However, its tissue-specific expression and bacteriolytic activity indicate that it may be tightly regulated to function effectively in innate immunity.