Characterization of the RAGE-binding protein, Strongyloides venestatin, produced by the silkworm-baculovirus expression system

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. •We produced Strongyloides venestatin using silkworm-baculovirus expression.•Venestatin has Ca++-binding capacity and vaccine immunogenicity against larvae.•Venestatin has a higher affinity for RAGE than that expressed by E. coli.•Endogenous RAGE interacts with the venestain.•Venestatin may have effects on RAGE-mediated pathological processes.