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• W2961765089 abstract "The receptor for advanced glycation end products (RAGE) recognizes Ca++-binding proteins, such as members of the S100 protein family released by dead or devitalized tissues, and plays an important role in inflammatory responses. We recently identified the Ca++-binding protein, venestatin, secreted from the rodent parasitic nematode, Strongyloides venezuelensis. We herein characterized recombinant venestatin, which is abundantly produced by the silkworm-baculovirus expression system (silkworm-BES), particularly in its interaction with RAGE. Venestatin from silkworm-BES possessed a binding capacity with Ca++ ions and vaccine immunogenicity against S. venezuelensis larvae in mice, which is similar to venestatin produced by the E. coli expression system (EES). Venestatin from silkworm-BES had a higher affinity for human recombinant RAGE than that from EES, and their affinities were Ca++-dependent. RAGE in the mouse lung co-immunoprecipitated with venestatin from silkworm-BES administered intranasally, indicating that it bound endogenous mouse RAGE. The present results suggest that venestatin from silkworm-BES affects RAGE-mediated pathological processes." @default.
• W2961765089 created "2019-07-23" @default.
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• W2961765089 date "2019-11-01" @default.
• W2961765089 modified "2023-09-24" @default.
• W2961765089 title "Characterization of the RAGE-binding protein, Strongyloides venestatin, produced by the silkworm-baculovirus expression system" @default.
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• W2961765089 doi "https://doi.org/10.1016/j.meegid.2019.103964" @default.
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