Functional and intricate interaction network connecting Helicobacter pylori Cag type 4 secretion system surface proteins with outer membrane proteins HopQ and HopZ
Contact us if these videos are not relevant.
Contact us if these videos are not relevant.
View abstract on PubMed
Summary
This summary is machine-generated.This study reveals a network of interactions between Helicobacter pylori outer membrane proteins and CagT4SS components. These interactions are crucial for the type IV secretion system
Area Of Science
- Microbiology
- Molecular Biology
- Cell Biology
Background
- The Helicobacter pylori cag pathogenicity island (cagPAI) encodes the Cag type IV secretion system (CagT4SS), a key virulence factor.
- Recent Cryo-EM studies have advanced CagT4SS structural understanding, yet functional details remain incomplete.
Purpose Of The Study
- To investigate the hypothesis that external CagT4SS proteins assemble with non-CagT4SS proteins on the cell surface, impacting T4SS function.
- To elucidate functional protein-protein interactions involving CagT4SS extracellular proteins and outer membrane proteins.
Main Methods
- Interaction screens
- Biochemical characterization
- Functional assays
- Chromosomal tag insertions in H. pylori
Main Results
- Identified novel interactions between CagT4SS surface proteins (CagC, CagL, CagN) and outer membrane proteins (HopQ, HopZ).
- Quantified pH-dependent interactions of T4SS surface proteins with HopZ, HopQ, host factors (CEACAM, integrin), and self-interactions of HopZ/HopQ.
- Detected surface colocalization of HopQ with T4SS components and uncovered antagonistic roles of HopQ and HopZ in early epithelial cell activation.
Conclusions
- A network of interactions between H. pylori outer membrane proteins and CagT4SS surface proteins is essential for T4SS-dependent transport.
- This study provides a foundation for future research on the structure and function of the CagT4SS surface components.
Contact us if these videos are not relevant.
Contact us if these videos are not relevant.
Related Concept Videos
Gram-negative bacteria utilize sophisticated protein secretion systems to transport proteins across their double-membrane envelope into the extracellular environment or host cells. Based on their mechanism of action, these systems are classified into one-step and two-step pathways.One-Step Secretion Systems (Types I, III, IV, and VI)One-step secretion systems bypass the periplasm entirely, forming a continuous channel that spans both the inner and outer membranes:Type I Secretion System (T1SS):...
Fimbriae and pili are specialized bacterial surface structures that play pivotal roles in adhesion, genetic exchange, and motility. Composed primarily of pilin protein, these hairlike appendages are crucial for bacterial survival and pathogenicity in various environments.Fimbriae: Adhesion and PathogenicityFimbriae are fine, filamentous structures measuring 2–10 nanometers in diameter and are densely distributed on the bacterial cell surface. They facilitate bacterial adhesion to abiotic...
Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types – adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
Adherens Junctions are Dynamic
The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
Archaeal surface appendages are highly specialized structures essential for environmental adaptation, encompassing roles in adhesion, biofilm formation, and motility. Among these appendages, pili and archaella stand out for their distinct morphologies and functionalities, enabling archaea to thrive in diverse and often extreme environments.Pili: Adhesion and Biofilm FormationPili are filamentous structures assembled from pilin protein subunits, primarily contributing to adhesion and biofilm...