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Updated: Sep 27, 2026

Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
Dual-action MINPP1 effectors enable Riptortus pedestris to overcome phytic acid antinutritional defense and suppress
Yuxia Yang1,2, Xin Zhou1,2, Lanping Ding1,2
1State Key Laboratory of Agricultural and Forestry Biosecurity, College of Plant Protection, Nanjing Agricultural University, Nanjing, China.
Abstract:
Phytic acid (IP6) serves as the primary phosphorus reservoir in plant seeds and functions as a potent antinutritional defense to inhibit herbivore growth. Despite this formidable barrier, the bean bug Riptortus pedestris preferentially feeds on IP6-rich leguminous seeds, yet the molecular mechanisms underlying this dietary adaptation have remained elusive. Here, we demonstrate that R. pedestris overcomes this nutritional defense by co-opting the ancient, highly conserved multiple inositol polyphosphate phosphatase 1 (MINPP1) family. We identified four RPMINPP1 paralogs abundantly expressed in both the salivary glands and the midgut. Using 3 1P NMR spectroscopy, we showed that these enzymes completely dephosphorylate IP6 to inorganic phosphate. Functional analyses revealed a sophisticated dual-action detoxification strategy: salivary RPMINPP1 is secreted into host tissues to degrade IP6 in planta, whereas midgut-localized RPMINPP1Ls mediate IP6 hydrolysis in vivo. RNA interference experiments confirmed that RPMINPP1Ls are essential for insect feeding and survival on soybean hosts. Remarkably, RPMINPP1 also functions as a broad-spectrum suppressor of pattern-triggered immunity (PTI) triggered by diverse elicitors, acting independently of its catalytic activity. Collectively, our findings uncover a dual-pronged strategy in which an herbivore repurposes MINPP1 family effectors to simultaneously neutralize phytic acid-based antinutritional defense and suppress host plant immunity.
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