Study of response of Swiss Webster mice to light subunit of mushroom tyrosinase |
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| Authors: | WT Ismaya A Efthyani DS Retnoningrum X Lai BW Dijkstra RR Tjandrawinata |
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| Institution: | 1. Dexa Laboratories of Biomolecular Sciences, JABABEKA II Industrial Estate, Cikarang;2. Research group of Pharmaceutics, School of Pharmacy, Bandung Institute of Technology, Bandung;3. Research group of Biotechnology, School of Pharmacy, Bandung Institute of Technology, Bandung, Indonesia;4. European Synchrotron Radiation Facility, Grenoble, France;5. Laboratory of Biophysical Chemistry, University of Groningen, Groningen, The Netherlands |
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| 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. |
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| Keywords: | histopathology immune tolerance lectin-like protein light subunit mushroom ORF239342 tyrosinase |
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