Sidc Effector Protein
Sidc Effector Protein - Related Videos
04:41
Introduction of Bacterial Effector Proteins into Mammalian Cells by Electroporation
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2025
In this video, we demonstrate the introduction of bacterial effector proteins into mammalian cells by electroporation. The intracellular localization of the bacterial effector proteins is detected by confocal microscopy following staining with specific fluorophore-conjugated antibodies.
02:20
Monitoring Bacterial Infection and Effector Protein Delivery in Plant Cells
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2025
Source: Lee, H. et. al., Split Green Fluorescent Protein System to Visualize Effectors Delivered from Bacteria During Infection. J. Vis. Exp. (2018)This video demonstrates a method for monitoring bacterial infection and effector protein delivery in plant cells using split superfolder green fluorescent protein (sfGFP) complementation combined with confocal microscopy. The approach enables precise visualization of effector translocation into the host cell cytosol.
12:23
Analysis of Yersinia enterocolitica Effector Translocation into Host Cells Using Beta-lactamase Effector Fusions
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Cited by 5 •
2015
Effector translocation into host cells via a type III secretion system is a common virulence strategy among gram-negative bacteria. A beta-lactamase effector fusion based assay for quantitative analysis of translocation was applied. In Yersinia infected cells, conversion of a FRET reporter by the beta-lactamase is monitored using laser scanning microscopy.
08:39
Electroporation of Functional Bacterial Effectors into Mammalian Cells
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Cited by 7 •
2015
Electroporation was used to insert purified bacterial virulence effector proteins directly into living eukaryotic cells. Protein localization was monitored by confocal immunofluorescence microscopy. This method allows for studies on trafficking, function, and protein-protein interactions using active exogenous proteins, avoiding the need for heterologous expression in eukaryotic cells.
12:11
Capture Compound Mass Spectrometry - A Powerful Tool to Identify Novel c-di-GMP Effector Proteins
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Cited by 15 •
2015
The ubiquitous second messenger c-di-GMP controls growth and behavior of many bacteria. We have developed a novel Capture Compound Mass Spectrometry based technology to biochemically identify and characterize c-di-GMP binding proteins in virtually any bacterial species.
FAQs
A key event is recognition of phosphatidylinositol 4-phosphate, a host-cell membrane lipid. SidC binds this lipid on the Legionella-containing vacuole, while its SNL domain recruits vesicles originating from the endoplasmic reticulum. Together, these interactions help redirect membrane supply toward the vacuole, supporting its development into a compartment where Legionella can replicate.
The U-box domain adds a second biochemical activity: E3 ubiquitin-ligase function. SidC therefore does more than attach to a particular host membrane; it also contains a domain with ubiquitin-ligase activity. Considering both domains is important because membrane remodeling and interference with host-cell trafficking may reflect coordinated effector functions rather than a single isolated interaction.
SidC must reach the host-cell interior before its membrane-associated activities can operate. Legionella pneumophila delivers it through the Dot/Icm type IV secretion system, placing the effector where the Legionella-containing vacuole forms. This delivery step connects bacterial virulence to host-cell manipulation and distinguishes secretion-dependent action from activity outside the infected cell.
SidC provides a molecular example of how a bacterial effector can redirect normal membrane traffic rather than merely damage the host cell. Its recruitment of endoplasmic-reticulum-derived vesicles and association with the vacuole show how pathogen-driven membrane reorganization can create a replication-permissive compartment. This makes SidC useful for linking specific domains to altered cellular organization.
Studies can follow three connected features: SidC delivery by the Dot/Icm system, its binding to phosphatidylinositol 4-phosphate on the Legionella-containing vacuole, and recruitment of endoplasmic-reticulum-derived vesicles through the SNL domain. Examining these features together helps relate bacterial secretion to membrane remodeling and then to formation of a vacuole that supports intracellular replication.
SidC research helps explain how Legionella pneumophila survives inside host cells by redirecting host processes. The effector links bacterial secretion, membrane trafficking, vacuole formation, and intracellular replication in one infection-associated system. In immunology and infection research, this provides context for studying pathogen manipulation of host cells and identifying targets relevant to understanding Legionnaires’ disease.
Separating the SNL and U-box activities conceptually can clarify how distinct effector functions contribute to infection. The SNL domain is associated with recruitment of endoplasmic-reticulum-derived vesicles, whereas the U-box supplies E3 ubiquitin-ligase activity. Comparing these roles may help identify which molecular activity influences membrane remodeling, trafficking interference, or the replication-permissive vacuole.