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Updated: Oct 18, 2025

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
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Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation

Wei He1, Gangjin Yu2, Tianpeng Li1

  • 1State Key Laboratory of Bioreactor Engineering, East China University of Science and Technologygrid.28056.39, Shanghai Collaborative Innovation Center for Biomanufacturing (SCICB), Shanghai, China.

Mbio
|October 5, 2021
PubMed
Summary

The periplasmic chaperone Spy protects outer membrane proteins (OMPs) in Gram-negative bacteria and compensates for other chaperones. Spy uses a unique mechanism, allowing OmpX to form a partially folded structure, aiding antimicrobial development.

Keywords:
chaperonefolding stressnuclear magnetic resonance spectroscopyouter membrane protein biogenesisprotein-protein interaction

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