ArticleThe Journal of biological chemistry2011
Structure analysis of the Staphylococcus aureus UDP-N-acetyl-mannosamine dehydrogenase Cap5O involved in capsular polysaccharide biosynthesis.
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 13 papers.
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13 citing papers in PubMed, 30 citations in OpenAlex.
- Phenolic Compound, Antioxidant, Antibacterial, and In Silico Studies of Extracts from the Aerial Parts ofMolecules (Basel, Switzerland) · 2024Article
- Thermophilic PHP Protein Tyrosine Phosphatases (Cap8C and Wzb) from Mesophilic Bacteria.International journal of molecular sciences · 2024Article
- Article
- Evaluation of Annona muricata extract against Staphylococcus aureus isolate and in-silico activity of bioactive compounds against Capsular protein (Cap5O).BMC complementary medicine and therapies · 2022Article
- Tyrosine Kinases and Phosphatases: Enablers of theFrontiers in oral health · 2022Review
- Analysis of nucleotide diphosphate sugar dehydrogenases reveals family and group-specific relationships.FEBS open bio · 2016Article
- Characterization of a bacterial tyrosine kinase in Porphyromonas gingivalis involved in polymicrobial synergy.MicrobiologyOpen · 2014Article
- The role of bacterial protein tyrosine phosphatases in the regulation of the biosynthesis of secreted polysaccharides.Antioxidants & redox signaling · 2014Review
- The UDP-glucose dehydrogenase of Escherichia coli K-12 displays substrate inhibition by NAD that is relieved by nucleotide triphosphates.The Journal of biological chemistry · 2013Article
- Comparative analysis of the Tyr-kinases CapB1 and CapB2 fused to their cognate modulators CapA1 and CapA2 from Staphylococcus aureus.PloS one · 2013Article
- Bacterial tyrosine kinases: evolution, biological function and structural insights.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Mucosal reactive oxygen species decrease virulence by disrupting Campylobacter jejuni phosphotyrosine signaling.Cell host & microbe · 2012Article
- Tyrosine phosphorylation and bacterial virulence.International journal of oral science · 2012Review
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Authors and funding
11 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial UDP-sugar dehydrogenases are part of the biosynthesis pathway of extracellular polysaccharides. These compounds act as important virulence factors by protecting the cell from opsonophagocytosis and complement-mediated killing. In Staphylococcus aureus, the protein Cap5O catalyzes the oxidation of UDP-N-acetyl-mannosamine to UDP-N-acetyl-mannosaminuronic acid. Cap5O is crucial for the production of serotype 5 capsular polysaccharide that prevents the interaction of bacteria with both phagocytic and nonphagocytic eukaryotic cells. However, details of its catalytic mechanism remain unknown. We thus crystallized Cap5O and solved the first structure of an UDP-N-acetyl-mannosamine dehydrogenase. This study revealed that the catalytic cysteine makes a disulfide bond that has never been observed in other structurally characterized members of the NDP-sugar dehydrogenase family. Biochemical and mutagenesis experiments demonstrated that the formation of this disulfide bridge regulates the activity of Cap5O. We also identified two arginine residues essential for Cap5O activity. Previous data suggested that Cap5O is activated by tyrosine phosphorylation, so we characterized the phosphorylation site and examined the underlying regulatory mechanism.
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