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Updated: May 30, 2026
12:29
Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
Published on: March 11, 2022
Effector glycosyltransferases in legionella
Yury Belyi1, Thomas Jank, Klaus Aktories
1Gamaleya Research Institute Moscow, Russia.
Frontiers in Microbiology
|August 12, 2011
Summary
Legionella pneumophila uses glucosyltransferases (Lgts) to inhibit host protein synthesis, causing severe pneumonia. These Lgts modify elongation factor eEF1A, leading to cell death.
Area of Science:
- Microbiology
- Cell Biology
- Molecular Biology
Background:
- Legionella is a bacterium causing severe pneumonia by interfering with host cell functions.
- Legionella pneumophila secretes effector proteins, including glucosyltransferases (Lgts), that manipulate host cells.
Purpose of the Study:
- To review recent findings on the structure-function relationship of Lgt glucosyltransferases from L. pneumophila.
- To understand how Lgt effectors contribute to Legionella pathogenesis.
Main Methods:
- Structural and functional analysis of Lgt glucosyltransferases.
- Investigation of Lgt interaction with eukaryotic elongation factor eEF1A.
- Comparison with clostridial glucosylating toxins.
Main Results:
- Lgt1, Lgt2, and Lgt3 are L. pneumophila glucosyltransferases.
- These enzymes modify eukaryotic elongation factor eEF1A at serine-53 using UDP-glucose.
- Modification inhibits protein synthesis and causes target cell death.
Conclusions:
- Lgt glucosyltransferases are key virulence factors for L. pneumophila.
- The mechanism involves targeted modification of host protein synthesis machinery.
- Further research into Lgt structure-function relationships can inform therapeutic strategies.
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