ArticleActa crystallographica. Section F, Structural biology communications2023
Structural and enzymatic characterization of the sialidase SiaPG from Porphyromonas gingivalis.
Article in Acta crystallographica. Section F, Structural biology communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 4 citations in OpenAlex.
- Stimuli-responsive, antimicrobial-loaded nanocarriers for oral biofilm control and microbiome restoration.International journal of oral science · 2026Review
- Bacterial exo-α-sialidases subvert the complement system through desialylation.bioRxiv : the preprint server for biology · 2026Article
- Functional and structural analyses reveal that a dual domain sialidase protects bacteria from complement killing through desialylation of complement factors.PLoS pathogens · 2023Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The sialidases, which catalyze the hydrolysis of sialic acid from extracellular glycoconjugates, are a group of major virulence factors in various pathogenic bacteria. In Porphyromonas gingivalis, which causes human periodontal disease, sialidase contributes to bacterial pathogenesis via promoting the formation of biofilms and capsules, reducing the ability for macrophage clearance, and providing nutrients for bacterial colonization. Here, the crystal structure of the P. gingivalis sialidase SiaPG is reported at 2.1 Å resolution, revealing an N-terminal carbohydrate-binding domain followed by a canonical C-terminal catalytic domain. Simulation of the product sialic acid in the active-site pocket together with functional analysis enables clear identification of the key residues that are required for substrate binding and catalysis. Moreover, structural comparison with other sialidases reveals distinct features of the active-site pocket which might confer substrate specificity. These findings provide the structural basis for the further design and optimization of effective inhibitors to target SiaPG to fight against P. gingivalis-derived oral diseases.
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