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CD64 (biology)
CD64 (biology)
CD64 (biology)
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Fc fragment of IgG, high affinity Ia, receptor (CD64)
Identifiers
SymbolFCGR1A
NCBI gene2209
HGNC3613
OMIM146760
RefSeqNM_000566
UniProtP12314
Other data
LocusChr. 1 q21.2-21.3
Search for
StructuresSwiss-model
DomainsInterPro
Fc fragment of IgG, high affinity Ib, receptor (CD64)
Identifiers
SymbolFCGR1B
NCBI gene2210
HGNC3614
OMIM601502
RefSeqNM_001004340
UniProtQ92637
Other data
LocusChr. 1 p11.2
Search for
StructuresSwiss-model
DomainsInterPro
Fc fragment of IgG, high affinity Ic, receptor (CD64)
Identifiers
SymbolFCGR1C
NCBI gene2211
HGNC3615
OMIM601503
RefSeqXM_001133198
Other data
LocusChr. 1 q21.1

CD64 (Cluster of Differentiation 64) is a type of integral membrane glycoprotein known as an Fc receptor that binds monomeric IgG-type antibodies with high affinity.[1] It is more commonly known as Fc-gamma receptor 1 (FcγRI). After binding IgG, CD64 interacts with an accessory chain known as the common γ chain (γ chain), which possesses an ITAM motif that is necessary for triggering cellular activation.[2]

Structurally CD64 is composed of a signal peptide that allows its transport to the surface of a cell, three extracellular immunoglobulin domains of the C2-type that it uses to bind antibody, a hydrophobic transmembrane domain, and a short cytoplasmic tail.[3]

CD64 is constitutively found on only macrophages and monocytes, but treatment of polymorphonuclear leukocytes with cytokines like IFNγ and G-CSF can induce CD64 expression on these cells.[4][5]

There are three distinct (but highly similar) genes in humans for CD64 called FcγRIA (CD64A), FcγRIB (CD64B), and FcγRIC (CD64C) that are located on chromosome 1.[6] These three genes produce six different mRNA transcripts; two from CD64A, three from CD64B, and one from CD64C; by alternate splicing.[3]

References

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CD64 (biology)

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CD64, also known as FcγRI, is the sole high-affinity receptor for monomeric immunoglobulin G (IgG) among the human Fc gamma receptors, binding IgG subclasses IgG1, IgG3, and IgG4 with nanomolar affinity (K_D ≈ 10⁻⁹ to 10⁻¹⁰ M). This transmembrane glycoprotein, encoded by the FCGR1A gene on chromosome 1, consists of three extracellular immunoglobulin-like domains (D1, D2, D3), a single transmembrane region, and a short cytoplasmic tail that associates with signaling subunits for immune activation. Expressed constitutively on myeloid cells such as monocytes, macrophages, and dendritic cells, CD64 expression is inducible on neutrophils, eosinophils, mast cells, endothelial cells, and even neurons in response to proinflammatory cytokines like interferon-gamma (IFN-γ) and tumor necrosis factor-alpha (TNF-α). In physiological contexts, CD64 plays a central role in bridging humoral and cellular immunity by facilitating (ADCC), of opsonized pathogens or immune complexes, , and release of proinflammatory cytokines such as TNF-α and interleukin-6 (IL-6). Its high-affinity binding enables rapid clearance of low-abundance IgG and amplification of immune responses during infection or inflammation, but dysregulation contributes to pathological conditions including autoimmune diseases like systemic lupus erythematosus (SLE), (RA), and (ITP), where it promotes excessive inflammation via immune complex deposition. In cancer, CD64 enhances the efficacy of therapies by mediating ADCC against tumor cells, and it has been targeted in immunotoxins and bispecific antibodies for selective depletion of activated macrophages or tumor-associated immune cells. Additionally, emerging research highlights its involvement in through neuronal expression and in modulating inhibitory checkpoints like PD-1/ interactions to boost antitumor immunity.

Molecular biology

Gene organization

The genes encoding CD64, known as the FCGR1 , consist of three highly homologous members: FCGR1A, FCGR1B, and FCGR1C. FCGR1A and FCGR1C are located on the long arm of at band q21.2 (positions 149,782,671-149,791,675 for FCGR1A), while FCGR1B maps to the short arm at band p11.2-p12 (positions 120,926,979-120,935,937). These genes flank the and arose from ancient duplications, contributing to the diversity of Fc gamma receptors. Through , the FCGR1 genes produce six distinct mRNA transcripts. FCGR1A generates two transcripts that encode functional α-chains of the CD64 receptor, including the full-length isoform with all six exons. In contrast, FCGR1B yields three transcripts: one potentially full-length but non-functional due to inactivating mutations, and two others that are truncated or inhibitory owing to . FCGR1C produces a single transcript, which is pseudogene-like and lacks functionality, often missing key coding regions for membrane anchoring. Only transcripts from FCGR1A result in a stable, surface-expressed receptor capable of associating with the common γ-chain (encoded by FCER1G on 1q23), which is essential for signaling. Each FCGR1 gene spans approximately 10 kb and comprises six s that correspond to distinct protein domains. Exons 1 and 2 encode the , exons 3 through 5 code for the three extracellular immunoglobulin-like domains responsible for binding, and exon 6 encompasses the transmembrane region and cytoplasmic tail, with in this exon generating isoform variability. The genomic structure of FCGR1A was first elucidated through cloning and sequencing efforts reported in 1991, which identified the promoter region and interferon-gamma responsive elements driving inducible expression. A notable polymorphism in FCGR1A is the p.R92* (Arg92Ter) nonsense variant (rs74315310), located in exon 3, which introduces a premature stop codon in the first Ig-like domain and results in complete loss of receptor function due to mRNA decay or truncated protein. This rare allele (minor allele frequency <0.01) has been associated with impaired phagocytic activity in affected individuals.

Protein structure

CD64, also known as FcγRI or high-affinity immunoglobulin gamma Fc receptor I, is encoded by the FCGR1A gene on chromosome 1q21.2. The protein precursor consists of 374 amino acids, with the N-terminal signal peptide (residues 1–15) cleaved upon maturation to yield a 359-amino-acid α-chain. This α-chain comprises three extracellular C2-set immunoglobulin-like domains—D1 (residues 22–100), D2 (residues 104–185), and D3 (residues 196–274)—a single hydrophobic transmembrane domain (residues 293–313), and a cytoplasmic domain spanning residues 314–374 (61 amino acids) that lacks an immunoreceptor tyrosine-based activation motif (ITAM). The α-chain does not possess intrinsic signaling capability due to the absence of ITAM in its short cytoplasmic tail; instead, it associates non-covalently but stably with a disulfide-linked homodimer of the common γ-chain (encoded by FCER1G) via interactions in the transmembrane and juxtamembrane regions. This γ-chain homodimer provides the necessary ITAM motifs for downstream and anchors the complex in the plasma membrane. The three-dimensional of the extracellular domains reveals a compact, elongated well-suited for recognition. structures, such as the 3.2 Å resolution structure of the unbound FcγRI extracellular domain and the complex with IgG1 Fc, show that the D1–D2 hinge adopts an acute angle, while the D2–D3 interface forms a hydrophobic pocket involving key residues like Leu128, Phe150, and Ile200 that accommodate the IgG Fc region for high-affinity binding. Additionally, solution studies using demonstrate that the unbound receptor maintains a compact conformation in solution, facilitating monomeric IgG engagement without significant domain reorientation. CD64 is a with seven conserved N-linked sites (Asn59 in D1, Asn78 in D1, Asn152 and Asn159 in D2, Asn163 in D2, Asn195 in D3, and Asn240 in the stem region), which contribute to proper folding, structural integrity, and overall protein stability by shielding hydrophobic regions and promoting correct domain assembly. Deglycosylation leads to misfolding and reduced thermal stability, underscoring the glycans' role in maintaining the receptor's functional conformation.

Cellular expression

Constitutive expression

CD64 (FcγRI) is constitutively expressed at high levels on monocytes, macrophages—including alveolar macrophages in the lungs and Kupffer cells in the liver—and dendritic cells in both humans and mice, enabling baseline immune recognition of IgG-opsonized targets. This expression pattern supports the role of these cells in steady-state and without external stimuli. In peripheral blood and tissues, CD64 distribution is prominent among resident macrophages in the , liver, and , where it facilitates ongoing immune surveillance, while expression is lower in macrophages. Quantitative analyses indicate approximately 5,000–20,000 CD64 molecules per or under normal conditions, reflecting sufficient density for high-affinity IgG binding. Resting neutrophils, eosinophils, and lymphocytes exhibit low to absent CD64 expression in humans under steady-state conditions, distinguishing them from myeloid . Species differences are notable, with constitutive CD64 presence on neutrophils observed in some animals, such as dogs, but not in humans or mice. Although cytokines like IFN-γ can upregulate CD64 on these cells, constitutive levels remain the focus of baseline expression patterns.

Inducible expression

CD64 expression is dynamically upregulated on neutrophils and in response to proinflammatory stimuli, particularly interferon-gamma (IFN-γ) and (G-CSF). In neutrophils, which typically exhibit low basal levels of CD64, exposure to IFN-γ or G-CSF results in a rapid increase of up to 10-fold within 24-48 hours, enhancing their capacity for and during . Similarly, IFN-γ induces CD64 on , leading to approximately an 8-fold elevation in surface expression, thereby modulating their role in immune complex clearance. Induction of CD64 also occurs on non-hematopoietic cells such as endothelial cells and fibroblasts under inflammatory conditions. Inflammatory cytokines such as tumor necrosis factor-alpha (TNF-α) promote CD64 expression on endothelial cells, facilitating interactions with immune complexes at sites of vascular inflammation. On fibroblasts, including fibroblast-like mesangial cells in the kidney, IFN-γ drives CD64 upregulation, contributing to tissue remodeling in response to immune activation. CD64 expression is also inducible on mast cells and neurons in response to proinflammatory cytokines such as IFN-γ, contributing to immune modulation in tissues. At the molecular level, inducible expression of CD64 is governed by transcriptional regulation of the FCGR1A gene, which contains IFN-γ responsive elements in its promoter that recruit transcription factors such as STAT1 and IRF1 to drive rapid gene activation in response to cytokine signaling. Downregulation mechanisms counteract this induction, including receptor internalization following ligand binding, which removes CD64 from the cell surface, and suppression by anti-inflammatory cytokines like IL-10, which inhibit proinflammatory gene expression. In clinical settings, elevated CD64 levels, particularly on neutrophils, serve as an early biomarker for sepsis and bacterial infections, reflecting acute inflammatory responses.

Biological function

Ligand binding

CD64, also known as FcγRI, exhibits high-affinity binding to the Fc portion of monomeric human (IgG) subclasses IgG1, IgG3, and IgG4, with dissociation constants (K_d) in the range of 10^{-9} to 10^{-10} M, while it shows no affinity for IgG2 due to sequence variations in the IgG lower hinge region. This high affinity enables CD64 to engage free IgG monomers, distinguishing it from low-affinity Fcγ receptors that primarily interact with multivalent immune complexes. For immune complexes, CD64 binding is enhanced by effects, allowing effective capture despite the intrinsic monomeric affinity. The primary binding interface involves the Fc region's CH2 domain of IgG interacting with the D2 domain of CD64, forming a hydrophobic pocket that accommodates key IgG residues such as Leu235 in the lower hinge. The D3 domain of CD64 contributes to stabilizing the high-affinity interaction, with the overall interface spanning D1, D2, and D3 extracellular domains, though D2 forms the core contact site. Specific receptor residues, including Trp104 and Lys128 in D2, facilitate this docking through hydrogen bonding and van der Waals interactions. Ligand binding to CD64 is optimal at neutral (around 7.4), where the FG-loop in the D2 domain adopts a conformation conducive to high-affinity engagement; at acidic (below 6.0), a structural switch reduces affinity, aiding release in endosomal compartments. Unlike certain receptors, IgG binding to CD64 is calcium-independent, relying instead on protein-protein interactions without divalent cation modulation. Due to its superior monomeric affinity, CD64 outcompetes low-affinity Fcγ receptors (such as FcγRII and FcγRIII) for IgG ligands on the cell surface, particularly in scenarios involving soluble IgG or nascent immune complexes, thereby directing effector responses. In addition to IgG, CD64 binds other ligands such as (CRP), an acute-phase reactant that engages the receptor to modulate , with binding mediated through distinct sites overlapping the IgG interface. It also interacts with certain autoantibodies, facilitating their clearance or contributing to autoimmune pathology via Fc-dependent mechanisms.

Signal transduction

CD64, also known as FcγRI, lacks intrinsic signaling motifs in its cytoplasmic domain and associates noncovalently with the Fc receptor γ-chain (FcRγ), which contains immunoreceptor tyrosine-based activation motifs (ITAMs) essential for signal initiation. Cross-linking of CD64 by multimeric IgG ligands induces clustering of the receptor complex, leading to phosphorylation of the ITAM tyrosine residues by Src family kinases, such as Lyn or Hck. This phosphorylation creates docking sites for the SH2 domains of Syk kinase, which is recruited and activated to propagate downstream signals. Activated Syk triggers multiple intracellular cascades, including the (PI3K)/Akt pathway, which generates lipid second messengers like PI(3,4,5)P3 to regulate actin cytoskeleton reorganization, and the (MAPK)/extracellular signal-regulated kinase (ERK) pathway, promoting gene transcription. These pathways culminate in calcium mobilization, often through and kinase activation, facilitating transient calcium spikes that support cellular activation. Additionally, signaling induces transcription of proinflammatory cytokines, such as IL-6 and TNF-α, via ERK-dependent mechanisms in monocytes and macrophages. The functional outcomes of CD64-mediated signaling include enhanced phagocytosis of opsonized particles through Rac and Cdc42 activation for pseudopod extension, (ADCC) via targeted release of cytotoxic granules, and in effector cells like neutrophils. In macrophages, these signals drive membrane trafficking and immune effector functions, with PI3K playing a key role in formation independent of calcium fluxes. CD64 signaling integrates with Toll-like receptors (TLRs) through cross-talk, where co-engagement with IgG complexes and TLR ligands amplifies Syk-dependent proinflammatory responses, leading to synergistic production of cytokines like TNF-α and IL-6 in macrophages. This integration enhances innate immune activation without altering core cell phenotypes.

Role in disease

Autoimmune and inflammatory disorders

CD64, also known as FcγRI, plays a significant role in the pathogenesis of (RA) by promoting through the uptake of IgG-containing immune complexes (IgG-ICs) by macrophages, leading to enhanced release such as TNF-α and IL-1β. In RA synovial tissue, CD64 expression on macrophages is markedly elevated compared to healthy controls, and this upregulation correlates with disease severity and joint inflammation. In systemic lupus erythematosus (SLE), CD64 facilitates autoantibody-mediated tissue damage by enabling the binding and internalization of immune complexes, which amplifies inflammatory responses in organs like the kidneys and . Elevated CD64 expression on circulating monocytes in SLE patients parallels and correlates with renal disease activity, underscoring its contribution to disease progression. Although polymorphisms in FCGR2A and other FcγR genes have been linked to SLE susceptibility, evidence for FCGR1A variants specifically influencing risk remains limited in large meta-analyses. In (ITP), CD64 on splenic and hepatic macrophages mediates the of antibody-opsonized platelets, contributing to . Enhanced expression of CD64 on and differences in monocyte subpopulations have been observed in ITP patients, suggesting its role in disease pathogenesis and potential as a diagnostic . In (IBD), CD64 is upregulated on intestinal macrophages, distinguishing them from dendritic cells and contributing to chronic mucosal inflammation. This enhanced expression drives pro-inflammatory signaling, including activation of the pathway and , which promotes IL-1β and IL-18 production and exacerbates tissue damage in conditions like and . CD64 levels also serve as a marker of active IBD, reflecting the overall inflammatory burden in the gut. CD64 contributes to the of autoimmune neuropathies, including antibody-mediated demyelination as seen in Guillain-Barré (GBS), where FcγRI on macrophages and potentially neurons facilitates immune complex deposition and complement activation, leading to . In GBS models, activating FcγRs, including CD64, amplify antibody-dependent effector functions that promote axonal damage and demyelination. Therapeutic blockade of CD64 has shown promise in reducing in animal models of autoimmune diseases; for instance, FcγRI-deficient mice exhibit diminished severity due to impaired IgG-IC-induced production and swelling. Similarly, anti-CD64 antibodies attenuate immune complex-mediated in models of SLE and neuropathy, highlighting its potential as a target for modulating pathogenic responses without broadly impairing immunity.

Infections and immunity

CD64 plays a crucial role in host defense against bacterial infections by enhancing the phagocytosis of IgG-opsonized bacteria, such as Staphylococcus aureus, through its expression on macrophages and neutrophils. This high-affinity receptor binds IgG-opsonized pathogens, facilitating their uptake and destruction by these effector cells, which is particularly important in IFN-γ-driven immune responses that amplify macrophage activation and bacterial clearance. In viral immunity, CD64 mediates (ADCC) against virus-infected cells by engaging IgG antibodies bound to viral antigens on the cell surface, thereby recruiting monocytes and macrophages to lyse infected targets. During infection, CD64 is upregulated on neutrophils and monocytes, enhancing effector functions and contributing to the acute against , though excessive expression correlates with disease severity. For fungal and parasitic infections, CD64 binds IgG-containing immune complexes to promote eosinophil-mediated killing of pathogens, as eosinophils inducibly express this receptor to facilitate antibody-dependent degranulation and against helminths and fungi. This mechanism supports type 2 immune responses essential for clearing multicellular parasites. In the context of , elevated CD64 expression in diabetic patients—showing a 1.25-fold increase in chronic ulcerative skin compared to non-diabetic individuals—impairs tissue repair by driving excessive and prolonging activation, which hinders progression to the proliferative phase of . The high-affinity IgG binding property of CD64 is evolutionarily conserved across mammals, enabling rapid immune clearance of opsonized pathogens and underscoring its fundamental role in innate immunity from early vertebrates to humans.

Research and applications

Diagnostic utility

CD64, particularly its expression on neutrophils (nCD64), has emerged as a valuable biomarker for the early diagnosis and monitoring of sepsis, primarily due to its rapid upregulation in response to bacterial infections. Neutrophil CD64 expression increases significantly within 4–6 hours of sepsis onset, driven by proinflammatory cytokines such as interferon-gamma, allowing for timely detection via flow cytometry quantification. Meta-analyses have demonstrated high diagnostic accuracy, with pooled sensitivity around 82% and specificity of 88% for distinguishing bacterial sepsis from non-infectious systemic inflammatory response syndrome, often outperforming traditional markers like C-reactive protein (CRP) and procalcitonin. This utility was first comprehensively validated in a 2009 review, which highlighted nCD64's potential as a reliable infection marker across adult and pediatric populations. In autoimmune and inflammatory conditions, CD64 expression serves as an inflammation index, reflecting disease activity in disorders such as (RA) and systemic lupus erythematosus (SLE). In RA, elevated monocyte CD64 (mCD64) levels correlate with joint inflammation and disease flares, showing strong associations with clinical scores and traditional markers like CRP and (ESR). Similarly, in SLE, mCD64 expression on monocytes strongly correlates with the Systemic Lupus Erythematosus Disease Activity Index (SLEDAI), providing a sensitive indicator of active disease that outperforms some interferon-related biomarkers. These measurements, typically assessed by , enable non-invasive monitoring of therapeutic responses and flare prediction. In , CD64 overexpression on tumor-associated s (TAMs) facilitates diagnostic imaging to assess the . Radiolabeled anti-CD64 antibodies, such as those conjugated for (PET), have been developed to visualize activated s in inflammatory tissues, such as in , aiding in the characterization of and progression. For instance, CD64-targeted tracers highlight macrophage density, which correlates with poor in various cancers, supporting personalized diagnostic strategies. Despite these advantages, CD64's diagnostic utility is limited by its lack of specificity, as expression can elevate in non-bacterial conditions including viral infections, necessitating with other markers like for improved accuracy. Additionally, variability in baseline expression and assay standardization across flow cytometers can affect reproducibility, underscoring the need for validated cutoffs in clinical settings.

Therapeutic targeting

Therapeutic targeting of CD64 (FcγRI) has emerged as a strategy to modulate immune responses in cancer, , and by leveraging its high-affinity IgG binding to enhance or inhibit effector functions. Monoclonal antibodies (mAbs) against CD64, such as H22, have been developed to direct cytotoxic payloads to CD64-expressing cells, particularly monocytes and macrophages in tumors, promoting (ADCC) and targeted delivery of therapeutics like immunotoxins or siRNA. For instance, H22-based bispecific constructs have demonstrated efficient recruitment of effector cells to CD30-positive cells in preclinical models, highlighting its potential in . In autoimmune contexts, blocking CD64 with mAbs like clone 197 reduces immune complex-mediated ; in (ITP), it decreased platelet clearance by approximately 50% in early patient studies, suggesting utility in dampening FcγRI-driven effects. Fc engineering of therapeutic antibodies modulates CD64 engagement to optimize efficacy and safety. Enhancements in the Fc domain, such as glycoengineering or substitutions (e.g., S239D/I332E/A330L), increase binding affinity to CD64, boosting ADCC by macrophages and monocytes, which is particularly relevant for biologics like rituximab in B-cell malignancies where FcγRI polymorphisms influence response rates. Conversely, Fc-silent variants (e.g., ) minimize CD64 interaction to reduce unintended in autoimmune therapies, preventing excessive release while preserving target-specific effects. These modifications have been validated in preclinical assays showing up to 10-fold improved effector function against CD20-positive targets. Small molecule inhibitors targeting downstream components of CD64 signaling offer an alternative to direct receptor blockade, particularly in (RA). Spleen tyrosine kinase (Syk) inhibitors, such as (R788), interrupt the γ-chain-associated signaling cascade initiated by CD64 cross-linking, reducing pro-inflammatory cytokine production and joint destruction in preclinical arthritis models. Clinical data from phase II/III trials in RA patients demonstrated modest improvements in disease activity scores (e.g., DAS28 reduction by 1.0-1.3 points) with , though side effects limited broader adoption; this approach indirectly dampens CD64-mediated immune complex activation without affecting high-affinity IgG binding. No direct inhibitors of the FcR γ-chain have advanced clinically, but Syk targeting remains a validated strategy for FcγRI-related inflammation. Gene therapy approaches hold potential for addressing FCGR1A polymorphisms that impair CD64 function in immunodeficiencies, though clinical translation remains exploratory. Variants altering CD64 expression or signaling, such as those reducing affinity, have been linked to altered immune responses in conditions like , suggesting that lentiviral correction of FCGR1A in hematopoietic stem cells could restore phagocytic and ADCC capabilities; however, no trials have been reported as of 2025. As of 2025, clinical trials for anti-CD64 therapies have primarily focused on rather than or . Phase I studies of H22-based constructs (e.g., MDX-1401) in showed safety and partial responses in CD64-high tumors, but no phase II/III data for or exist; preclinical blockade in models supports future investigation. Soluble recombinant CD64 has reduced inflammation in murine , informing potential human trials. Recent preclinical studies and planned phase I/II trials explore CD64 CAR-T therapy for venetoclax-resistant AML, targeting monocytic leukemia stem cells. In 2025, an anti-CD64(scFv)-SNAP-auristatin F ADC demonstrated selective cytotoxicity against CD64-positive monocytic leukemia cells in preclinical studies.

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