Related Experiment Video
Updated: Jun 23, 2025

Anti-virulent Disruption of Pathogenic Biofilms using Engineered Quorum-quenching Lactonases
Published on: January 1, 2016
Halenaquinol Blocks Staphylococcal Protein A Anchoring on Cell Wall Surface by Inhibiting Sortase A in Staphylococcus
Jaepil Lee1, Jae-Hyeong Choi2,3, Jayho Lee1
1Department of Agricultural Biotechnology, College of Agriculture and Life Sciences and Natural Products Research Institute, Seoul National University, Seoul 08826, Republic of Korea.
Marine sponge compounds, like halenaquinol, inhibit Sortase A (SrtA) activity, blocking surface protein anchoring in Staphylococcus aureus. This discovery offers potential new anti-infective strategies against bacterial virulence.
Area of Science:
- Marine Natural Products Chemistry
- Microbiology
- Biochemistry
Background:
- Sortase A (SrtA) is essential for anchoring surface proteins to the bacterial cell wall.
- Staphylococcus aureus virulence is linked to SrtA-mediated protein display.
Purpose of the Study:
- To identify inhibitors of Sortase A (SrtA) from marine natural products.
- To elucidate the mechanism of SrtA inhibition by marine pentacyclic polyketides.
Main Methods:
- Isolation and structural elucidation of compounds from marine sponge Xestospongia sp.
- Biochemical assays to determine SrtA inhibitory activity (IC50).
- Molecular biology techniques including RT-PCR, Western blot, and immunofluorescence microscopy.
Main Results:
- Six pentacyclic polyketides were isolated; halenaquinol showed potent SrtA inhibition (IC50 = 13.94 μM).
- Halenaquinol does not affect srtA or spA gene transcription.
- Halenaquinol inhibits Sortase A activity, preventing surface protein A (SpA) anchoring to the cell wall.
Conclusions:
- Halenaquinol effectively inhibits SrtA-mediated SpA cell wall anchoring in S. aureus.
- Marine-derived pentacyclic polyketides are promising candidates for anti-infective drug development targeting S. aureus virulence.
More Related Videos
10:00Targeting Biofilm Associated Staphylococcus aureus Using Resazurin Based Drug-susceptibility Assay
Published on: May 5, 2016
11:59Isolation of Lipoprotein Particles from Chicken Egg Yolk for the Study of Bacterial Pathogen Fatty Acid Incorporation into Membrane Phospholipids
Published on: May 15, 2019
Related Concept Videos
Antimicrobial Proteins
Interferons
Interferons (IFNs) are proteins produced by lymphocytes, macrophages, and fibroblasts infected with viruses. While IFNs cannot prevent viruses from entering and...
Indirect-Acting Cholinergic Agonists: Mechanism of Action
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex,...
Factors Affecting Protein-Drug Binding: Drug-Related Factors
One crucial factor in drug-protein binding is the drug's lipophilicity or its affinity for fat. More lipophilic drugs tend to have higher binding extents. For example, highly lipophilic drugs like cloxacillin exhibit substantial protein binding, with as much as 95% of the drug binding to proteins. In...