ArticleGlycobiology2022
Crystal structure of the Propionibacterium acnes surface sialidase, a drug target for P. acnes-associated diseases.
Article in Glycobiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Bacterial exo-α-sialidases subvert the complement system through desialylation.bioRxiv : the preprint server for biology · 2026Article
- Computational methodology and molecular dynamics analysis of andrographolide bioactivity againstFrontiers in chemistry · 2025Article
- Review
- Advances in polymeric nano-delivery systems targeting hair follicles for the treatment of acne.Drug delivery · 2024Review
- Functional and structural analyses reveal that a dual domain sialidase protects bacteria from complement killing through desialylation of complement factors.PLoS pathogens · 2023Article
- Structural and enzymatic characterization of the sialidase SiaPG from Porphyromonas gingivalis.Acta crystallographica. Section F, Structural biology communications · 2023Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Propionibacterium acnes, though generally considered part of the normal flora of human skin, is an opportunistic pathogen associated with acne vulgaris as well as other diseases, including endocarditis, endophthalmitis and prosthetic joint infections. Its virulence potential is also supported by knowledge gained from its sequenced genome. Indeed, a vaccine targeting a putative cell wall-anchored P. acnes sialidase has been shown to suppress cytotoxicity and pro-inflammatory cytokine release induced by the organism, and is proposed as an alternative treatment for P. acnes-associated diseases. Here, we report the crystal structures of the surface sialidase and its complex with the transition-state mimic Neu5Ac2en. Our structural and kinetic analyses, together with insight from a glycan array screen, which probes subtle specificities of the sialidase for α-2,3-sialosides, provide a basis for the structure-based design of novel small-molecule therapeutics against P. acnes infections.
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Registered trials
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