Global analysis of protein lysine lactylation profiles in the marine bacterium Photobacterium damselae subsp. damselae

Yongxiang Yu; Haozhe Liu; Chunyuan Wang; Yingeng Wang; Xiaojun Rong; Meijie Liao; Bin Li; Xingling Yi; Zheng Zhang

doi:10.3389/fmicb.2025.1539893

Global analysis of protein lysine lactylation profiles in the marine bacterium Photobacterium damselae subsp. damselae

Front Microbiol. 2025 Jun 17:16:1539893. doi: 10.3389/fmicb.2025.1539893. eCollection 2025.

Authors

Yongxiang Yu^{1

2}, Haozhe Liu¹, Chunyuan Wang¹, Yingeng Wang^{1

2}, Xiaojun Rong^{1

2}, Meijie Liao^{1

2}, Bin Li^{1

2}, Xingling Yi³, Zheng Zhang^{1

2}

Affiliations

¹ State Key Laboratory of Mariculture Biobreeding and Sustainable Goods, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao, Shandong, China.
² Laboratory for Marine Fisheries Science and Food Production Processes, Laoshan Laboratory, Qingdao, Shandong, China.
³ Weimi Biotechnology Co., Ltd., Hangzhou, Zhejiang, China.

Abstract

Lysine lactylation (K _lac ) is a recently discovered post-translational modification (PTM) widespread across species, playing a crucial role in cellular processes and associated with pathological conditions. Photobacterium damselae subsp. damselae, a marine bacterium within the Vibrionaceae family, is a notable pathogen in aquaculture, offering a valuable model for investigating the evolution of pathogenicity from environmental ancestors and assessing the impact of genetic diversity-generating mechanisms on bacterial populations. Therefore, we conducted the first systematic analysis of K _lac modification in P. damselae using highly sensitive proteomic techniques. A total of 1,352 K _lac modification sites were identified on 486 proteins. The analysis of GO annotations and KEGG pathways for the identified K _lac -modified proteins revealed their widespread distribution in subcellular compartments, indicating their involvement in diverse cellular functions and metabolic pathways, particularly in ribosome and protein biosynthesis, as well as central carbon metabolism. Furthermore, 20 highly connected K _lac protein clusters were extracted from the global protein-protein interaction (PPI) network, indicating that K _lac modification tends to occur on proteins associated with specific functional clusters. These findings enhance our understanding of the functional role of K _lac modification and provide a dataset for further exploration of its impact on the physiology and biology of P. damselae.

Keywords: Photobacterium damselae subsp. damselae; lysine lactylation (Klac); post-translational modification (PTM); protein-protein interaction (PPI) network; proteomics.