Characterization and expression of HLysG2, a basic goose-type lysozyme from the human eye and testis.

Lysozyme plays an important role in human innate immunity by causing bacterial cell lysis. We describe for the first time, the actual performance of human lysozyme g-like 2 (HLysG2), a mammalian g-type lysozyme. RT-PCR revealed that the HLysG2 gene was transcribed in eye and testis tissues. A spot was detected from human tears using 2D gel electrophoresis and was identified as HLysG2 using MALDI-TOF/TOF MS and a MASCOT search with a matching score of 140 and 27% sequence coverage of the whole amino acid sequence. To gain insight into the in vitro antimicrobial activities of HLysG2, the mature peptide-coding region was cloned into Pichia pastoris for heterogeneous expression. Recombinant HLysG2, had an optimal at pH 6.0 and 30 °C, reached the peak activity of 1.2 × 10(4)U/mg at the sodium ion concentration of 75 mM and showed a higher salt tolerance than human c-type lysozyme (HLysC). Recombinant HlysG2 inhibited Gram-positive bacterial growth and did not inhibit Gram-negative bacterial and Candida albicans growth. Results indicated that HLysG2 is a potent antibacterial protein that may play a role in the innate immunity of the human eye.

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