TY - JOUR
T1 - Characterization of the RAGE-binding protein, Strongyloides venestatin, produced by the silkworm-baculovirus expression system
AU - Tsubokawa, Daigo
AU - Lee, Jae Man
AU - Hatta, Takeshi
AU - Mikami, Fusako
AU - Maruyama, Haruhiko
AU - Arakawa, Takeshi
AU - Kusakabe, Takahiro
AU - Tsuji, Naotoshi
N1 - Funding Information:
This work was supported by JSPS KAKENHI Grant Number 18 K15140, and by grants from the Kitasato University Integrative Research Program of the Graduate School of Medical Sciences and OHYAMA HEALTH FOUNDATION INC.
Funding Information:
This work was supported by JSPS KAKENHI Grant Number 18 K15140 , and by grants from the Kitasato University Integrative Research Program of the Graduate School of Medical Sciences and OHYAMA HEALTH FOUNDATION INC .
Publisher Copyright:
© 2019 Elsevier B.V.
PY - 2019/11
Y1 - 2019/11
N2 - 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.
AB - 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.
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U2 - 10.1016/j.meegid.2019.103964
DO - 10.1016/j.meegid.2019.103964
M3 - Article
C2 - 31302241
AN - SCOPUS:85069507894
SN - 1567-1348
VL - 75
JO - Infection, Genetics and Evolution
JF - Infection, Genetics and Evolution
M1 - 103964
ER -
