Dendritic cells: functional aspects of glycosylation and lectins

Annika Erbacher1, Friederike Gieseke, Rupert Handgretinger

  • 1University Children's Hospital, Department of General Pediatrics, Hematology and Oncology, 72026 Tübingen, Germany.

Human Immunology
|February 25, 2009
PubMed

Insights

Dendritic cells (DCs) utilize carbohydrate-protein interactions, involving lectins and glycans, for antigen uptake, immune modulation, and viral infections. These interactions are critical for DC function, influencing immune responses beyond gene expression. Keywords: Dendritic cells, lectins, glycans, immune response, viral infection.

Area of Science:

  • Immunology
  • Glycobiology
  • Cell Biology

Background:

  • Dendritic cells (DCs) are key regulators of immune responses, directing them towards tolerance or inflammation.
  • While gene expression profiling identified many crucial proteins, carbohydrate-protein interactions are increasingly recognized as vital for DC functions.
  • These interactions are essential for antigen uptake, cell migration, homing, and susceptibility to viral infections.

Purpose of the Study:

  • To review the glycobiological aspects of dendritic cell (DC) biology.
  • To highlight the role of lectins and glycans in DC-mediated antigen uptake, immune modulation, and viral infections.
  • To emphasize the importance of these interactions in bridging innate and acquired immunity.

Main Methods:

  • Literature review focusing on glycobiological mechanisms in dendritic cells.
  • Analysis of the roles of specific C-type lectins (e.g., DC-SIGN, dectin-1, langerin, DEC-205) and other lectins (e.g., CD83, siglecs, galectins).
  • Examination of how DC surface glycosylation impacts immune signaling and function.

Main Results:

  • DCs employ various lectins for efficient antigen uptake and processing.
  • Altered DC surface glycosylation patterns significantly influence immune responses.
  • Lectins and glycans are critical mediators in DC interactions with antigens, pathogens, and other immune cells.

Conclusions:

  • Carbohydrate-protein interactions are fundamental to dendritic cell biology, impacting antigen handling, immune regulation, and host-pathogen interactions.
  • Understanding these glycobiological processes is crucial for deciphering DC functions at the innate-adaptive immunity interface.
  • This review underscores the significance of lectins and glycans in DC-mediated immune responses and viral infections.

Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Glycocalyx and its Functions01:14

Glycocalyx and its Functions

The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
Components of...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
T Cell Activation and Clonal Selection01:22

T Cell Activation and Clonal Selection

T cells are integral to our adaptive immune system, recognizing and effectively responding to foreign antigens. T cell activation and clonal selection are pivotal in orchestrating this immune response. This article elucidates these mechanisms, detailing the roles of cluster of differentiation (CD) markers, major histocompatibility complex (MHC) molecules, costimulatory signals, and the process of clonal selection.
Naive T cells that have not yet encountered an antigen express two primary CD...
Antigens Involved in Adaptive Immunity01:26

Antigens Involved in Adaptive Immunity

An antigen is any substance the immune system identifies as foreign and potentially harmful to the body, prompting an immune response. Antigens have two functional properties: immunogenicity and reactivity. Immunogenicity is the ability of an antigen to stimulate a specific immune response. At the same time, reactivity describes the antigen's ability to react with the cells and antibodies produced in response to it.
Complete Antigens
Complete antigens possess both immunogenicity and reactivity.