HSC71 acetylation confers protection against Spiroplasma eriocheiris infection by inhibiting apoptosis and promoting ROS production in arthropods.

Acetylation of HSC71 at lysine 579 in crabs protects against Spiroplasma eriocheiris infection by increasing ROS and limiting pathogen propagation.

• Why it matters: HSP70 post-translational modifications are important for innate immunity, but how specific acetylation events tune resistance during intracellular infection is unclear.
• What they did: Crat acetylated HSC71 at K579, preventing ubiquitination by promoting CHIP dissociation and stabilizing HSC71; SIRT1 inhibition with EX-527 increased HSC71 acetylation and ROS.
• The result: In HSC71- or Crat-deficient crabs, hemocyte apoptosis increased and mortality rose after S. eriocheiris challenge, while EX-527 reduced susceptibility; in Drosophila S2 cells, EX-527 increased HSPA8 acetylation, weakened SOD binding, elevated ROS, and restricted intracellular proliferation.

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