Structural basis for the interaction of diapause hormone with its receptor in the silkworm, Bombyx mori

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
Zhangfei ShenNaiming Zhou

Abstract

Diapause hormone (DH) is a 24-aa amidated neuropeptide that elicits the embryonic diapause of the silkworm, Bombyx mori ( Bommo), via sensitive and selective interaction with its receptor, Bommo DH receptor ( Bommo-DHR). Previous studies of the structure-activity relationship of Bommo-DH were all based on an in vivo diapause-induction bioassay, which has provided little information on the structure of Bommo-DHR or its iteration with DH. Here, to unveil the interaction of Bommo-DH with its receptor, N-terminally truncated analogs and alanine-scanning mutants of Bommo-DH were chemically synthesized and functionally evaluated by using a Cy5.5-labeled Bommo-DH competitive binding assay and Bommo-DHR-based functional assays, including cAMP assay and Ca2+ mobilization assay. Our study demonstrates that the C-terminal residues of Arg23 and Leu24 of Bommo-DH are essential for the binding and activation of Bommo-DHR, and that Trp19 and Phe20 also contribute to the functional activity of Bommo-DH. In contrast, when Gly21 or Pro22 were replaced with alanine, both mutants exhibited binding and signaling activities that were indistinguishable from the wild-type peptide. Furthermore, our homology modeling and molecular dynamics simulations, ...Continue Reading

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Citations

May 28, 2020·Frontiers in Physiology·Umut Toprak
Apr 27, 2020·Archives of Insect Biochemistry and Physiology·Umut ToprakGözde Güney
Jun 3, 2021·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Nannan LiuShikai Liu

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