![]() ![]() Recently, we decoded the whole genome structure of the venomous habu snake ( Protobothrops flavoviridis) and analyzed its transcriptomic data by next-generation sequencing, revealing that the production mechanisms of various venomous proteins are associated with accelerated evolution and alternative splicing ( Shibata et al., 2018 Ogawa et al., 2019 Ogawa and Shibata, 2020). Venomous snakes contain various bioactive peptides and proteins in their venom ( Doley and Kini, 2009). Approximately 5.4 million people worldwide are estimated to suffer from snakebites annually, causing around 81,000 to 138,000 deaths and around three times permanently disabilities ( World Health Organization, 2021). Snake envenomation is a major cause of death and long-term disability in developing countries. To our knowledge, this is the first report of a function of a catalytically inactive snake serine protease. Additionally, we identified the unique properties and a novel synergistic function of pseudoenzyme TLf2 as a myonecrosis-enhancing factor. As a target protein for antivenom immunoglobulins with anti-myonecrotic activity, we identified a thrombin-like serine protease, TLSP2 (TLf2), which was an inactive proteolytic isoform due to the replacement of the active site, His43 with Arg. To compare the properties of an antivenom having anti-myonecrotic activity with those of conventional antivenom with no anti-myonecrotic activity, this study applied focused proteomics analysis of habu venom proteins using 2D gel electrophoresis. Antivenom immunoglobulins are an effective therapy for snakebites, and antivenom was recently developed with effective suppressive activity against myonecrosis induced by snake venom. In Japan, the venom of the habu snake ( Protobothrops flavoviridis) causes severe permanent damage due to its myonecrotic toxins. Snakebites are one of the major causes of death and long-term disability in the developing countries due to the presence of various bioactive peptides and proteins in snake venom.
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