Study of response of Swiss Webster mice to light subunit of mushroom tyrosinase

Abstract

The light subunit of mushroom, Agaricus bisporus, tyrosinase (LSMT), has been identified as an extrinsic component of the enzyme. Its function is unknown, but it can cross an epithelial cell layer, which suggests that it can be absorbed by the intestine. A similar capability has been demonstrated for the HA-33 component of the progenitor toxin from Clostridium botulinum, which is the closest structural homolog of LSMT. Unlike HA-33, LSMT appears to be non-immunogenic as shown by preliminary tests in Swiss Webster mice. We investigated the immunogenicity and histopathology of LSMT in mice to determine its safety in vivo. LSMT did not evoke generation of antibodies after prolonged periods of intraperitoneal administration. Histopathological observations confirmed the absence of responses in organs after twelve weekly administrations of LSMT. We found that LSMT is not toxic and is less immunogenic than the C. botulinum HA-33 protein, which supports further research and development for pharmaceutical application.

Key words:

• histopathology
• immune tolerance
• lectin-like protein
• light subunit
• mushroom
• ORF239342
• tyrosinase

Acknowledgments

This work was supported by the Ministry of Research, Science, Technology, and Higher Education, Republic of Indonesia through Excellent Research Program 2015–2018 (Contract No. 1059.10/I1.C03/KU/2015) and Dexa Laboratories of Biomolecular Sciences, Dexa Medica.

Declaration of interest: The authors report no conflicts of interest. The authors alone are responsible for the content and writing of this paper.