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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
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Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
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G protein-coupled receptor (GPCR) signaling plays a crucial role in cell functioning. GPCR desensitization is an equally essential process. It allows cells to respond to changing environments and regain sensitivity to new stimuli while preventing unnecessary stimulation when no longer needed. Prolonged exposure to stimuli leads to GPCR desensitization. It involves blocking the receptors from binding and activating additional G proteins. This inhibits activation of downstream effectors, thereby...
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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Altering the ligand specificity of DectiSomes.

Suresh Ambati1, Xiaorong Lin2, Zachary A Lewis2

  • 1Department of Genetics, University of Georgia, Athens, Georgia, USA.

The Journal of Biological Chemistry
|May 2, 2025
PubMed
Summary

DectiSomes, liposomes with pathogen receptors Dectin-2 and Dectin-3, bind fungal ligands. Their binding specificity changes based on labeling location, impacting immuno-liposome properties.

Keywords:
C-type lectinCandida albicansDectiSomeDectinLNPamphotericin Bantifungal drugsfluorescent proteinsfluorophoresimmuno-liposomeliposomemembranemicrofluidicsremote loadingreporters

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Area of Science:

  • Immunology
  • Biotechnology
  • Mycology

Background:

  • DectiSomes are liposomes engineered with C-type lectins (CTLs) Dectin-2 (D2) and Dectin-3 (D3, MCL) for targeted drug delivery.
  • These CTLs recognize oligoglycan ligands on pathogenic fungi, such as Candida albicans.
  • Amphotericin B (AmB)-loaded DectiSomes (D2-AmB-LLs and D3-AmB-LLs) have demonstrated efficacy against fungal infections.

Purpose of the Study:

  • To investigate the ligand-binding specificity of DectiSomes when Dectin-2 and Dectin-3 are labeled differently.
  • To explore how the location of fluorescent labels on DectiSomes affects their interaction with fungal cell wall components.
  • To understand the implications of these binding properties for the development of novel immuno-liposomes.

Main Methods:

  • DectiSomes loaded with amphotericin B were labeled internally (lumen) or externally (membrane surface) with fluorescent proteins (Venus, mCherry) or small fluorophores (FITC, Rhodamine B).
  • The binding patterns of labeled D2-AmB-LLs and D3-AmB-LLs to Candida albicans colonies were analyzed using fluorescence microscopy.
  • Dectin-2 and Dectin-3 proteins themselves were also labeled to assess their direct ligand interactions.

Main Results:

  • When labeled internally, both D2-AmB-LLs and D3-AmB-LLs bound overlapping regions of oligoglycans in C. albicans.
  • Conversely, external labeling of DectiSomes or labeling of the Dectin proteins themselves resulted in binding to distinct, non-overlapping ligand sets.
  • These findings suggest that the presentation and labeling strategy significantly influence DectiSome and Dectin ligand specificity.

Conclusions:

  • The ligand-binding specificity of DectiSomes is highly dependent on the location of labeling and the presentation of the Dectin receptors.
  • Altered binding patterns raise critical questions regarding the design and function of immuno-liposomes for targeted therapies.
  • Further research is needed to fully elucidate the complex ligand interactions of these engineered nanoparticles.