ArticleJournal of bacteriology1992
Molecular cloning of cDNA and analysis of protein secondary structure of Candida albicans enolase, an abundant, immunodominant glycolytic enzyme.
Article in Journal of bacteriology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 98 citations in OpenAlex.
- Heterodera schachtii enolase does not elicit canonical immune responses in Arabidopsis thaliana.Scientific reports · 2026Article
- Article
- Quantitatively detectingFrontiers in microbiology · 2023Article
- Cloning and Characterization of Immunological Properties ofJournal of immunology research · 2021Article
- Structural Insights into the Interactions of Candidal Enolase with Human Vitronectin, Fibronectin and Plasminogen.International journal of molecular sciences · 2020Article
- Potential Antifungal Targets Based on Glucose Metabolism Pathways ofFrontiers in microbiology · 2020Review
- The activity of bacterial peptidylarginine deiminase is important during formation of dual-species biofilm by periodontal pathogen Porphyromonas gingivalis and opportunistic fungus Candida albicans.Pathogens and disease · 2018Article
- Enolase of Streptococcus Suis Serotype 2 Enhances Blood-Brain Barrier Permeability by Inducing IL-8 Release.Inflammation · 2016Article
- Progress in the biological function of alpha-enolase.Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2016Review
- Development of a Lateral Flow Immunoassay for the Rapid Diagnosis of Invasive Candidiasis.Frontiers in microbiology · 2016Article
- Quantitative differential proteomics of yeast extracellular matrix: there is more to it than meets the eye.BMC microbiology · 2015Article
- Integrated inference and evaluation of host-fungi interaction networks.Frontiers in microbiology · 2015Article
- Serological response and diagnostic value of recombinant candida cell wall protein enolase, phosphoglycerate kinase, and β-glucosidase.Frontiers in microbiology · 2015Article
- Production of a Chaetomium globosum enolase monoclonal antibody.Monoclonal antibodies in immunodiagnosis and immunotherapy · 2014Article
- Extracellular enolase of Candida albicans is involved in colonization of mammalian intestinal epithelium.Frontiers in cellular and infection microbiology · 2014Article
- Heparin-binding motifs and biofilm formation by Candida albicans.The Journal of infectious diseases · 2013Article
- Candida albicans ENO1 null mutants exhibit altered drug susceptibility, hyphal formation, and virulence.Journal of microbiology (Seoul, Korea) · 2013Article
- Identification of major glucan-associated cell wall proteins of Candida albicans and their role in fluconazole resistance.Antimicrobial agents and chemotherapy · 2002Article
- CAP1, an adenylate cyclase-associated protein gene, regulates bud-hypha transitions, filamentous growth, and cyclic AMP levels and is required for virulence of Candida albicans.Journal of bacteriology · 2001Article
- Enhanced extracellular production of aspartyl proteinase, a virulence factor, by Candida albicans isolates following growth in subinhibitory concentrations of fluconazole.Antimicrobial agents and chemotherapy · 2000Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We isolated and sequenced a clone for Candida albicans enolase from a C. albicans cDNA library by using molecular genetic techniques. The 1.4-kbp cDNA encoded one long open reading frame of 440 amino acids which was 87 and 75% similar to predicted enolases of Saccharomyces cerevisiae and enolases from other organisms, respectively. The cDNA included the entire coding region and predicted a protein of molecular weight 47,178. The codon usage was highly biased and similar to that found for the highly expressed EF-1 alpha proteins of C. albicans. Northern (RNA) blot analysis showed that the enolase cDNA hybridized to an abundant C. albicans mRNA of 1.5 kb present in both yeast and hyphal growth forms. The polypeptide product of the cloned cDNA, which was purified as a recombinant protein fused to glutathione S-transferase, had enolase enzymatic activity and inhibited radioimmunoprecipitation of a single C. albicans protein of molecular weight 47,000. Analysis of the predicted C. albicans enolase showed strong conservation in regions of alpha helices, beta sheets, and beta turns, as determined by comparison with the crystal structure of apo-enolase A of S. cerevisiae. The lack of cysteine residues and a two-amino-acid insertion in the main domain differentiated C. albicans enolase from S. cerevisiae enolase. Immunofluorescence of whole C. albicans cells by using a mouse antiserum generated against the purified fusion protein showed that enolase is not located on the surface of C. albicans. Recombinant C. albicans enolase will be useful in understanding the pathogenesis and host immune response in disseminated candidiasis, since enolase is an immunodominant antigen which circulates during disseminated infections.
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