The DOI matches its Crossref record; 78 of the 78 references it cites were found in a registry or an index.
Major roles of isocitrate lyase and malate synthase in bacterial and fungal pathogenesis
Abstract
The glyoxylate cycle is an anaplerotic pathway of the tricarboxylic acid (TCA) cycle that allows growth on C 2 compounds by bypassing the CO 2-generating steps of the TCA cycle. The unique enzymes of this route are isocitrate lyase (ICL) and malate synthase (MS). ICL cleaves isocitrate to glyoxylate and succinate, and MS converts glyoxylate and acetyl-CoA to malate. The end products of the bypass can be used for gluconeogenesis and other biosynthetic processes. The glyoxylate cycle occurs in Eukarya, Bacteria and Archaea. Recent studies of ICL- and MS-deficient strains as well as proteomic and transcriptional analyses show that these enzymes are often important in human, animal and plant pathogenesis. These studies have extended our understanding of the metabolic pathways essential for the survival of pathogens inside the host and provide a more complete picture of the physiology of pathogenic micro-organisms. Hopefully, the recent knowledge generated about the role of the glyoxylate cycle in virulence can be used for the development of new vaccines, or specific inhibitors to combat bacterial and fungal diseases.
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Cites
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The glyoxylate cycle is required for fungal virulence
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Transcriptional Response of Candida albicans upon Internalization by Macrophages
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Synthesis of Cell Constituents from C2-Units by a Modified Tricarboxylic Acid Cycle
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Mechanism of Candida pathogenesis: Revisiting the vital drivers
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Beattie, S. R., Mark, K. M. K., Thammahong, A., Ries, L. N. A., Dhingra, S., Caffrey-Carr, A. K., Cheng, C., Black, C. C., Bowyer, P., Bromley, M. J., et al. (2017) · PLOS Pathogens · doi:10.1371/journal.ppat.1006340 · Cited by 103
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Metadata
- Authors
- Dunn, M. F., Ramírez-Trujillo, J. A., & Hernández-Lucas, I.
- Venue
- Microbiology
- Publisher
- Microbiology Society
- Published
- 2009-10-01
- Volume
- 155
- Issue
- 10
- Pages
- 3166-3175
- ISSN
- 1350-0872 (ISSN-L)
- 1465-2080
- OpenAlex
- W2149606963
- Cited by
- 304
- References
- 78
- FWCI
- 3.00
- Type
- journal article
- Language
- en
- Open access
- closed
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