Dataset Information

Azeliragon for the treatment of Staphylococcus aureus proteome

ABSTRACT: Azeliragon for the treatment of Staphylococcus aureus proteome

ORGANISM(S): Staphylococcus Aureus

SUBMITTER: Zhijian Yu

PROVIDER: PXD069935 | iProX | Mon Oct 27 00:00:00 GMT 2025

REPOSITORIES: iProX

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Publications

Repurposing Azeliragon as a novel antibacterial agent against methicillin-resistant Staphylococcus aureus via combined membrane phospholipids and cell wall targeting.

Ma Junhua J Xia Yuqing Y Lin Jintuan J Chen Chengchun C Meng Qingyin Q Yu Zhijian Z Ouyang Lili L Chai Bao B Bai Bing B Hou TieYing T Wen Zewen Z

Communications biology 20260514

Methicillin-resistant Staphylococcus aureus (MRSA) poses a persistent clinical threat due to limited therapeutic options and the rapid emergence of resistance. Azeliragon, an orally bioavailable Receptor for Advanced Glycation End-products (RAGE) inhibitor previously tested in human trials, was identified as a potential antibacterial agent against MRSA through high-throughput screening. It exhibited potent antibacterial activity against clinical S. aureus isolates (MIC<sub>50</sub> = 6.25 μM/3.3 ...[more]

PMID: 42135462

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Project description:The genome sequence is the “blue-print of life”, but proteomics is required to relate this blue-print of life to the actual physiology of living cells. Because of their low complexity – only about 2.000 proteins make a Staphylococcus aureus cell viable – bacteria are excellent model systems to identify the entire protein assembly of a living organism. Many of the studies on physiological proteomics of bacteria, however, still rely on 2D gel-based technologies that visualize only a minor part of the proteome. In this study it will be shown that the majority of proteins expressed in the Gram-positive human pathogen S. aureus can be identified and even quantified by a combination of gel-based and gel-free approaches, the latter having undergone formidable improvements over the last 10 years. S. aureus has been the model of choice for our proteomic studies, because it combines high pathogenicity with increasing antibiotic resistance, which calls for new leads in the development of anti-staphylococcal therapy. On the way towards the entire proteome of S. aureus, we analysed four subproteomic fractions: cytosolic proteins, membrane-bound proteins, cell-surface associated and extracellular proteins, the two latter fractions containing most of the virulence factors. To obtain quantitative results, we compared growing cells and non-growing/stationary phase cells using the 15N metabolic labelling approach. With almost 2.000 proteins, 80 % of the expressed proteome was identified and even quantified in growing and non-growing cells. A comprehensive inventory of the entire protein assembly during the two physiologically distinct states is presented, which integrates data ranging from gene expression to subcellular localization. Three major protein classes were distinguished: (i) Proteins induced in the stationary phase only (ii) Vegetative proteins, no longer synthesized but stable in the stationary phase (iii) Vegetative proteins, no longer required in non-growing cells and finally degraded. This quantitative proteomics approach for growing/non-growing cells, which represents a proof-of-principle for whole-cell physiological proteomics, can now be extended to address particular infection-relevant physiological states. Importantly, the present model study represents the highest coverage of a bacterial proteome so far (except low complexity bacteria). It thus paves the way towards a new understanding of cell physiology and pathophysiology of S. aureus and related pathogenic bacteria, opening a new era in infection-related research on this crucial pathogen.

Dataset Information

Azeliragon for the treatment of Staphylococcus aureus proteome

Publications

Repurposing Azeliragon as a novel antibacterial agent against methicillin-resistant Staphylococcus aureus via combined membrane phospholipids and cell wall targeting.

Similar Datasets

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