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Lactylation Reprogramming in the Bone Infection Microenvironment Identifies PGK1 K361 as a Potential Therapeutic

Han-Jun Qin1,2, Si-Ying He2, Ting-Hui Xiao1,2

  • 1Division of Orthopaedic Trauma, Department of Orthopaedic Surgery, Shenzhen People's Hospital (The First Affiliated Hospital, Southern University of Science and Technology; The Second Clinical Medical College, Jinan University), Shenzhen, China.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)
|January 28, 2026
PubMed
Summary

Lysine lactylation (Kla) is elevated in bone infections. Targeting PGK1 lactylation at K361 shows promise for treating infection-induced bone healing dysfunction by regulating mitophagy and ferroptosis.

Keywords:
bone infectionferroptosislysine lactylationmitophagyphosphoglycerate kinase 1 (PGK1)

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Area of Science:

  • Biochemistry
  • Orthopedics
  • Cell Biology

Background:

  • Bone infections present significant orthopedic challenges, impacting bone healing and function.
  • Lysine lactylation (Kla) is a post-translational modification with an unclear role in bone infection.

Purpose of the Study:

  • To investigate the role of lysine lactylation in bone infection.
  • To explore PGK1 lactylation as a therapeutic target for infection-induced osteogenic dysfunction.

Main Methods:

  • Global quantitative proteomics to identify lactylated sites.
  • In vitro and in vivo studies using adenoviral and adeno-associated viruses to modify PGK1.
  • Analysis of patient proteomic data.

Main Results:

  • Kla levels are significantly higher in infected bone tissues.
  • Identified 491 Kla sites on 201 proteins, with PGK1 K361 identified as a key site.
  • PGK1 K361 lactylation activates VDAC3, initiating mitophagy and ferroptosis in osteoblasts.

Conclusions:

  • PGK1 K361 lactylation is a novel mechanism contributing to osteogenic impairment in bone infections.
  • Targeting PGK1 K361 lactylation offers a potential therapeutic strategy for bone infection complications.