In immunology, an Fc receptor is a protein found on the surface of certain cells – including, among others, B lymphocytes, follicular dendritic cells, natural killer cells, macrophages, neutrophils, eosinophils, basophils, human platelets, and mast cells – that contribute to the protective functions of the immune system. Its name is derived from its binding specificity for a part of an antibody known as the Fc (fragment crystallizable) region. Fc receptors bind to antibodies that are attached to infected cells or invading pathogens. Their activity stimulates phagocytic or cytotoxic cells to destroy microbes, or infected cells by antibody-mediated phagocytosis or antibody-dependent cell-mediated cytotoxicity. Some viruses such as flaviviruses use Fc receptors to help them infect cells, by a mechanism known as antibody-dependent enhancement of infection.[1]
Immunoglobulin-like receptor | |
---|---|
Identifiers | |
Symbol | Fc receptor |
Membranome | 10 |
Classes
editThere are several different types of Fc receptors (abbreviated FcR), which are classified based on the type of antibody that they recognize. The Latin letter used to identify a type of antibody is converted into the corresponding Greek letter, which is placed after the 'Fc' part of the name. For example, those that bind the most common class of antibody, IgG, are called Fc-gamma receptors (Fc
Fc-gamma receptors
editAll of the Fc
The Fc-gamma receptors differ in their affinity for IgG and likewise the different IgG subclasses have unique affinities for each of the Fc gamma receptors.[6] These interactions are further tuned by the glycan (oligosaccharide) at position CH2-84.4 of IgG.[6] For example, by creating steric hindrance, fucose containing CH2-84.4 glycans reduce IgG affinity for Fc
Neonatal Fc Receptor
editAnother FcR is expressed on multiple cell types and is similar in structure to MHC class I. This receptor also binds IgG and is involved in preservation of this antibody.[7] However, since this Fc receptor is also involved in transferring IgG from a mother either via the placenta to her fetus or in milk to her suckling infant, it is called the neonatal Fc receptor (FcRn).[8][9] Recently, research suggested that this receptor plays a role in the homeostasis of IgG serum levels.
Fc-alpha receptors
editOnly one Fc receptor belongs to the Fc
Fc-epsilon receptors
editTwo types of Fc
- the high-affinity receptor Fc
ε RI is a member of the immunoglobulin superfamily (it has two Ig-like domains). Fcε RI is found on epidermal Langerhans cells, eosinophils, mast cells and basophils.[13][14] As a result of its cellular distribution, this receptor plays a major role in controlling allergic responses. Fcε RI is also expressed on antigen-presenting cells, and controls the production of important immune mediators called cytokines that promote inflammation.[15] - the low-affinity receptor Fc
ε RII (CD23) is a C-type lectin. Fcε RII has multiple functions as a membrane-bound or soluble receptor; it controls B cell growth and differentiation and blocks IgE-binding of eosinophils, monocytes, and basophils.[16]
Summary table
editReceptor name | Principal antibody ligand | Affinity for ligand | Cell distribution | Effect following binding to antibody |
Fc |
IgG1 and IgG3 | High (Kd ~ 10−9 M) | Macrophages Neutrophils Eosinophils Dendritic cells |
Phagocytosis Cell activation Activation of respiratory burst Induction of microbe killing |
Fc |
IgG | Low (Kd > 10−7 M) | Macrophages Neutrophils Eosinophils Platelets Langerhans cells |
Phagocytosis Degranulation (eosinophils) |
Fc |
IgG | Low (Kd > 10−7 M) | B Cells Mast cells |
No phagocytosis Inhibition of cell activity |
Fc |
IgG | Low (Kd > 10−7 M) | Macrophages Neutrophils Eosinophils |
Phagocytosis Inhibition of cell activity |
Fc |
IgG | Low (Kd > 10−6 M) | NK cells Macrophages (certain tissues) |
Induction of antibody-dependent cell-mediated cytotoxicity (ADCC) Induction of cytokine release by macrophages |
Fc |
IgG | Low (Kd > 10−6 M) | Eosinophils Macrophages Neutrophils Mast cells Follicular dendritic cells |
Induction of microbe killing |
Fc |
IgE | High (Kd ~ 10−10 M) | Mast cells Eosinophils Basophils Langerhans cells Monocytes |
Degranulation Phagocytosis |
Fc |
IgE | Low (Kd > 10−7 M) | B cells Eosinophils Langerhans cells |
Possible adhesion molecule IgE transport across human intestinal epithelium Positive-feedback mechanism to enhance allergic sensitization (B cells) |
Fc |
IgA | Low (Kd > 10−6 M) | Monocytes Macrophages Neutrophils Eosinophils |
Phagocytosis Induction of microbe killing |
Fc |
IgA and IgM | High for IgM, Mid for IgA | B cells Mesangial cells Macrophages |
Endocytosis Induction of microbe killing |
Fc |
IgM | (unknown) | Human Fc |
function has not been fully elucidated / diverse [19] |
FcRn | IgG | high in acidic cellular endosomes low in pH neutral extracellular environment |
Monocytes Macrophages Dendritic cells Epithelial cells Endothelial cells Hepatocytes |
Transfers IgG from a mother to fetus through the placenta Transfers IgG from a mother to infant in milk Protects IgG from degradation Transfers IgG across endothelial/epithelial layers |
Functions
editFc receptors are found on a number of cells in the immune system including phagocytes like macrophages and monocytes, granulocytes like neutrophils and eosinophils, and lymphocytes of the innate immune system (natural killer cells) or adaptive immune system (e.g., B cells).[20][21][22]
They allow these cells to bind to antibodies that are attached to the surface of microbes or microbe infected cells, helping these cells to identify and eliminate microbial pathogens. The Fc receptors bind the antibodies at their Fc region (or tail), an interaction that activates the cell that possesses the Fc receptor.[23] Activation of phagocytes is the most common function attributed to Fc receptors. For example, macrophages begin to ingest and kill an IgG-coated pathogen by phagocytosis following engagement of their Fc
Signaling mechanisms - Fc gamma receptors
editActivation
editFc gamma receptors belong to the group of non-catalytic tyrosine-phosphorylated receptors which share a similar signalling pathway involving phosphorylation of tyrosine residues.[26] The receptors generate signals within their cells through an important activation motif known as an immunoreceptor tyrosine-based activation motif (ITAM).[27] An ITAM is a specific sequence of amino acids (YXXL) occurring twice in close succession in the intracellular tail of a receptor. When phosphate groups are added to the tyrosine (Y) residue of the ITAM by membrane-anchored enzymes of the Src kinase family, a signaling cascade is generated within the cell. This phosphorylation reaction typically follows interaction of an Fc receptor with its ligand. An ITAM is present in the intracellular tail of Fc
Inhibition
editThe presence of only one YXXL motif is not sufficient to activate cells, and represents a motif (I/VXXYXXL) known as an immunoreceptor tyrosine-based inhibitory motif (ITIM). Fc
The negative signaling by Fc
Cellular activation
editOn phagocytes
editWhen IgG molecules, specific for a certain antigen or surface component, bind to the pathogen with their Fab region (fragment antigen binding region), their Fc regions point outwards, in direct reach of phagocytes. Phagocytes bind those Fc regions with their Fc receptors.[24] Many low affinity interactions are formed between receptor and antibody that work together to tightly bind the antibody-coated microbe. The low individual affinity prevents Fc receptors from binding antibodies in the absence of antigen, and therefore reduces the chance of immune cell activation in the absence of infection. This also prevents agglutination (clotting) of phagocytes by antibody when there is no antigen. After a pathogen has been bound, interactions between the Fc region of the antibody and the Fc receptors of the phagocyte results in the initiation of phagocytosis. The pathogen becomes engulfed by the phagocyte by an active process involving the binding and releasing of the Fc region/Fc receptor complex, until the cell membrane of the phagocyte completely encloses the pathogen.[32]
On NK cells
editThe Fc receptor on NK cells recognize IgG that is bound to the surface of a pathogen-infected target cell and is called CD16 or Fc
On mast cells
editIgE antibodies bind to antigens of allergens. These allergen-bound IgE molecules interact with Fc
On eosinophils
editLarge parasites like the helminth (worm) Schistosoma mansoni are too large for ingestion by phagocytes. They also have an external structure called an integument that is resistant to attack by substances released by macrophages and mast cells. However, these parasites can become coated with IgE and recognized by Fc
On T lymphocytes
editCD4+ T cells (mature Th cells) provide help to B cells that produce antibodies. Several subsets of activated effector CD4+ T cells are observed in disease pathology. Earlier studies summarized by Sanders and Lynch in 1993 suggested critical roles for FcRs in CD4+ T cell mediated immune responses and proposed the formation of a joint signaling complex among FcRs and TCR on the cell surface.[41][42][43][44] Chauhan and coworkers reported the colocalization of the labeled ICs with the CD3 complex on activated CD4+ T cell surface, which thus suggest the coexistence of FcRs together with TCR complex.[45] Both of these receptors are observed forming an apical structure on the membrane of activated CD4+ T cells, suggesting the lateral movement of these receptors.[46] Co-migration of FcRs with TCR and BCR complex is observed on the cells surface and T:B cell cytoconjugates show this coexistence at the point of contact.[47] An earlier review suggested that the expression of FcRs on CD4+ T cells is an open question.[48] This established the current paradigm that T cells do not express FcRs and these findings were never challenged and experimentally tested.[49] Chauhan and coworkers showed binding of immune complexes (ICs), the FcR ligand to activated CD4+ T cells.[49] CD16a expression is induced in the activated human naïve CD4+ T cells, which express CD25, CD69, and CD98 and ligation to ICs leads to generation of effector memory cells.[50] CD16a signaling is mediated by phosphorylation of Syk (pSyk).[50][51][52]
A study now suggests induced expression of CD32a upon activation of human CD4+ T cells, similar to CD16a.[51][53] CD32a expression on CD4+ T cells was also suggested by three independent studies from HIV-1 researchers. The expression of CD16a and CD32a in a subset of activated CD4+ T cells is now confirmed.[51][53] FcRs on the cell surface upon binding to ICs composed of nucleic acids trigger cytokine production and upregulate nucleic acid sensing pathways. FcRs are present both on the cell surface and in the cytosol. CD16a signaling upregulate the expression of nucleic acid sensing toll-like receptors and relocate them to cell surface.[50][54] CD16a is a new costimulatory signal for human CD4+ T cells, which successfully substitute the CD28 requirement during autoimmunity.[55] In an autoimmune background CD4+ T cells bypass the requirement of CD28 cosignaling to become fully activated.[55] Furthermore, the blockade of CD28 cosignaling does not inhibit the development of TFH cells, a key subset for the generation of autoantibody producing autoreactive plasma B cells.[56] A balance among costimulatory and inhibitory signals is required for immune homeostasis. Excessive costimulation and/or insufficient co-inhibition leads to the tolerance-breakdown and autoimmunity. CD16a mediated costimulation provides a positive signal in the activated CD4+ T cells and not in the quiescent cells which lack Fc
See also
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Further reading
edit- Janeway CA, Travers P, Waldport M, Shlomchik MJ (2001). "Chapter 9. The Humoral Immune Response". Immunobiology: The Immune System in Health and Disease (5th ed.). New York: Garland. ISBN 978-0-8153-3642-6.
- Abbas AK, Lichtman AH, Pillai S (2012). "Chapter 12: Effector Mechanisms of Humoral Immunity". Cellular and molecular immunology (7th ed.). Philadelphia: Elsevier/Saunders. ISBN 978-1-4377-1528-6.
- Gerber JS, Mosser DM (February 2001). "Stimulatory and inhibitory signals originating from the macrophage Fcgamma receptors". Microbes and Infection. 3 (2): 131–9. doi:10.1016/s1286-4579(00)01360-5. PMID 11251299.
- Maverakis E, Kim K, Shimoda M, Gershwin ME, Patel F, Wilken R, Raychaudhuri S, Ruhaak LR, Lebrilla CB (February 2015). "Glycans in the immune system and The Altered Glycan Theory of Autoimmunity: a critical review". Journal of Autoimmunity. 57: 1–13. doi:10.1016/j.jaut.2014.12.002. PMC 4340844. PMID 25578468.
External links
edit- Fc+Receptor at the U.S. National Library of Medicine Medical Subject Headings (MeSH)