ArticleProtein & cell2012
An octamer of enolase from Streptococcus suis.
Article in Protein & cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Evaluation of trained immunity as a potential strategy for a universal Streptococcus suis vaccine using immunogenic proteins in a murine model.BMC veterinary research · 2026Article
- A phage-encoded anti-CRISPR protein co-opts host enolase to prevent type III CRISPR immunity.Nature microbiology · 2025Article
- FabG moonlights as an extracellular adhesin mediates cytoadhesion of Streptococcus suis via interaction with plasminogen.BMC microbiology · 2025Article
- Identification of plasminogen-binding sites inFrontiers in cellular and infection microbiology · 2024Article
- Article
- An alternative vaccine target for bovine Anaplasmosis based on enolase, a moonlighting protein.Frontiers in veterinary science · 2023Article
- Salmonella enterica serovar Choleraesuis vector delivering a dual-antigen expression cassette provides mouse cross-protection against Streptococcus suis serotypes 2, 7, 9, and 1/2.Veterinary research · 2022Article
- Article
- Streptococcus suis serotype 2 enolase interaction with host brain microvascular endothelial cells and RPSA-induced apoptosis lead to loss of BBB integrity.Veterinary research · 2021Article
- Evidence for the Rapid and Divergent Evolution of Mycoplasmas: Structural and Phylogenetic Analysis of Enolases.Frontiers in molecular biosciences · 2021Article
- Involvement of Various Enzymes in the Physiology and Pathogenesis ofVeterinary sciences · 2020Review
- Effect of ions and inhibitors on the catalytic activity and structural stability ofJournal of biosciences · 2019Article
- Featured Species-Specific Loops Are Found in the Crystal Structure ofFrontiers in cellular and infection microbiology · 2019Article
- Article
- Crystal structure of enolase from Drosophila melanogaster.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Structural and functional analysis of an anchorless fibronectin-binding protein FBPS from Gram-positive bacterium Streptococcus suis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Two novel regulators of N-acetyl-galactosamine utilization pathway and distinct roles in bacterial infections.MicrobiologyOpen · 2015Article
- Octameric structure of Staphylococcus aureus enolase in complex with phosphoenolpyruvate.Acta crystallographica. Section D, Biological crystallography · 2015Article
- The structure of bradyzoite-specific enolase from Toxoplasma gondii reveals insights into its dual cytoplasmic and nuclear functions.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Stability of the octameric structure affects plasminogen-binding capacity of streptococcal enolase.PloS one · 2015Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enolase is a conserved cytoplasmic metalloenzyme existing universally in both eukaryotic and prokaryotic cells. The enzyme can also locate on the cell surface and bind to plasminogen, via which contributing to the mucosal surface localization of the bacterial pathogens and assisting the invasion into the host cells. The functions of the eukaryotic enzymes on the cell surface expression (including T cells, B cells, neutrophils, monocytoes, neuronal cells and epithelial cells) are not known. Streptococcus suis serotype 2 (S. suis 2, SS2) is an important zoonotic pathogen which has recently caused two large-scale outbreaks in southern China with severe streptococcal toxic shock syndrome (STSS) never seen before in human sufferers. We recently identified the SS2 enolase as an important protective antigen which could protect mice from fatal S.suis 2 infection. In this study, a 2.4-angstrom structure of the SS2 enolase is solved, revealing an octameric arrangement in the crystal. We further demonstrated that the enzyme exists exclusively as an octamer in solution via a sedimentation assay. These results indicate that the octamer is the biological unit of SS2 enolase at least in vitro and most likely in vivo as well. This is, to our knowledge, the first comprehensive characterization of the SS2 enolase octamer both structurally and biophysically, and the second octamer enolase structure in addition to that of Streptococcus pneumoniae. We also investigated the plasminogen binding property of the SS2 enzyme.
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