ArticleThe Journal of biological chemistry2011
The Aspergillus fumigatus sialidase is a 3-deoxy-D-glycero-D-galacto-2-nonulosonic acid hydrolase (KDNase): structural and mechanistic insights.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 42 citations in OpenAlex.
- A Possible Involvement of Sialidase in the Cell Response of the Antarctic FungusLife (Basel, Switzerland) · 2025Article
- Orthogonal-Group-Controlled Site-Selective I-Branching of Poly-N-acetyllactosamine Chains Reveals Unique Binding Specificities of Proteins towards I-Antigens.Angewandte Chemie (International ed. in English) · 2025Article
- A self-immolative Kdn-glycoside substrate enables high-throughput screening for inhibitors of Kdnases.Glycobiology · 2025Article
- Glucose Catabolite Repression Participates in the Regulation of Sialidase Biosynthesis by Antarctic StrainJournal of fungi (Basel, Switzerland) · 2024Article
- Structural and functional characterization of cold-active sialidase isolated from Antarctic fungusBiochemistry and biophysics reports · 2024Article
- Structure of the immunoregulatory sialidase NEU1.Science advances · 2023Article
- Structural and enzymatic characterization of the sialidase SiaPG from Porphyromonas gingivalis.Acta crystallographica. Section F, Structural biology communications · 2023Article
- Crystal structure of the Propionibacterium acnes surface sialidase, a drug target for P. acnes-associated diseases.Glycobiology · 2022Article
- Neuraminidase and SIGLEC15 modulate the host defense against pulmonary aspergillosis.Cell reports. Medicine · 2021Article
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- Identification of novel fish sialidase genes responsible for KDN-cleaving activity.Glycoconjugate journal · 2020Article
- Article
- TheFrontiers in microbiology · 2017Article
- Interface dynamics explain assembly dependency of influenza neuraminidase catalytic activity.Journal of biomolecular structure & dynamics · 2015Article
- Structural basis of sialidase in complex with geranylated flavonoids as potent natural inhibitors.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Mechanistic investigations of unsaturated glucuronyl hydrolase from Clostridium perfringens.The Journal of biological chemistry · 2014Article
- Article
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Authors and funding
10 authors at 4 institutions in 3 countries.
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Abstract
Aspergillus fumigatus is a filamentous fungus that can cause severe respiratory disease in immunocompromised individuals. A putative sialidase from A. fumigatus was recently cloned and shown to be relatively poor in cleaving N-acetylneuraminic acid (Neu5Ac) in comparison with bacterial sialidases. Here we present the first crystal structure of a fungal sialidase. When the apo structure was compared with bacterial sialidase structures, the active site of the Aspergillus enzyme suggested that Neu5Ac would be a poor substrate because of a smaller pocket that normally accommodates the acetamido group of Neu5Ac in sialidases. A sialic acid with a hydroxyl in place of an acetamido group is 2-keto-3-deoxynononic acid (KDN). We show that KDN is the preferred substrate for the A. fumigatus sialidase and that A. fumigatus can utilize KDN as a sole carbon source. A 1.45-Å resolution crystal structure of the enzyme in complex with KDN reveals KDN in the active site in a boat conformation and nearby a second binding site occupied by KDN in a chair conformation, suggesting that polyKDN may be a natural substrate. The enzyme is not inhibited by the sialidase transition state analog 2-deoxy-2,3-dehydro-N-acetylneuraminic acid (Neu5Ac2en) but is inhibited by the related 2,3-didehydro-2,3-dideoxy-D-glycero-D-galacto-nonulosonic acid that we show bound to the enzyme in a 1.84-Å resolution crystal structure. Using a fluorinated KDN substrate, we present a 1.5-Å resolution structure of a covalently bound catalytic intermediate. The A. fumigatus sialidase is therefore a KDNase with a similar catalytic mechanism to Neu5Ac exosialidases, and this study represents the first structure of a KDNase.
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