C-type Lectin Receptors
C-type Lectin Receptors - Related Videos
01:07
Types of Receptors: Internal Receptors
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2023
Many cellular signals are hydrophilic and cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind intracellular receptors that reside within the cell cytoplasm or nucleus. Many mammalian steroid hormones and nitric oxide (NO) gas use this cell signaling mechanism. Similar to membrane-bound receptors, the binding of a ligand to the intracellular receptor of causes a conformational change in the...
01:28
Types of Receptors: Cell Surface Receptors
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2023
Cell-surface receptors, also known as transmembrane receptors, are cell surface, membrane-anchored (integral) proteins that bind to external ligand molecules. This type of receptor spans the plasma membrane and performs signal transduction, converting an extracellular signal into an intracellular signal. Ligands that interact with cell-surface receptors do not have to enter the cell that they affect. Cell-surface receptors are also called cell-specific proteins or markers because they are...
09:25
Lectin-based Isolation and Culture of Mouse Embryonic Motoneurons
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Cited by 21 •
2011
An alternative way of isolating mouse embryonic motoneurons from the spinal cord is described. The method takes into account the fact that lectin can bind to the low affinity nerve growth factor receptor p75NTR. This lectin-based preplating allows a purification similar to that with a specific antibody against the p75NTR.
20:23
A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
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Cited by 13 •
2009
Lectin-conjugated POROS beads were employed for HPLC. Glycopeptide standards served as positive and negative controls. MARS-14 depleted, trypsin-digested human plasma was chromatographed and flow-through (FT) and bound fractions collected for ESI-LC-MS/MS analyses. Glycopeptides were enriched in the bound fraction as compared to FT.
08:11
Measuring Influenza Neuraminidase Inhibition Antibody Titers by Enzyme-linked Lectin Assay
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Cited by 54 •
2016
We describe the enzyme-linked lectin assay (ELLA) for measuring influenza neuraminidase (NA)-inhibition antibody titers in sera. The assay uses peanut agglutinin to quantify galactose residues that become accessible when NA removes sialic acid from fetuin-coated, 96-well plates.
FAQs
Calcium-dependent coordination helps the C-type lectin-like domain recognize particular carbohydrate structures. This interaction gives the receptor ligand specificity rather than allowing indiscriminate binding to every glycan. For bioengineering, that selectivity is important when designing glycan-based ligands or materials intended to interact with chosen immune-cell receptors and produce more controlled biological responses.
After ligand recognition, intracellular signaling motifs or adaptor proteins regulate how the receptor’s external binding event is converted into a cellular response. These signaling components can influence activation, migration, phagocytosis, and cytokine production. Engineering strategies therefore need to consider not only receptor binding, but also whether the interaction engages pathways that produce the intended immune outcome.
Ligand specificity determines which carbohydrate structures are recognized and helps distinguish one receptor interaction from another. This matters because receptor engagement can direct different cellular behaviors, including migration, phagocytosis, or cytokine production. In engineered systems, matching a glycan-based ligand to the relevant receptor can improve selectivity and reduce unintended interactions with surrounding cells or materials.
Cell-surface receptors can support direct communication between an engineered ligand and a responding cell, whereas soluble forms can contribute to interactions within the surrounding environment. This distinction affects how a bioengineered design is conceived, whether as a cell-targeting interface, a soluble recognition component, or a material that presents glycans for selective receptor engagement.
A practical design sequence begins by identifying the receptor interaction of interest, selecting a carbohydrate structure suited to its ligand specificity, and evaluating how receptor engagement could influence the desired cellular response. The ligand can then be incorporated into a delivery system, biosensor, or biomaterial. This approach connects molecular recognition with a defined bioengineering objective.
Their carbohydrate recognition can provide a targeting principle for drug-delivery systems designed to interact selectively with immune cells. A glycan-based feature may be incorporated into the delivery design to engage a compatible receptor, while the receptor’s signaling behavior helps determine the likely cellular consequence. The strategy is useful when delivery and immune modulation must be considered together.
C-type lectin receptors can serve as recognition elements in biosensors because their lectin-like domains interact with carbohydrate structures. A biosensor design can use this molecular selectivity to detect or report glycan-related interactions. The receptor’s binding properties are therefore connected to the sensor’s ability to distinguish relevant carbohydrate signals from the surrounding environment.
Immunomodulatory biomaterials can be engineered to present carbohydrate features that interact with C-type lectin receptors on or around immune cells. Such interactions may influence cell activation, migration, phagocytosis, or cytokine production through receptor-associated signaling. This provides a route for designing materials that do more than provide structural support and instead help direct a selected immune response.