Alternative titles; symbols
HGNC Approved Gene Symbol: CD55
SNOMEDCT: 1279887007;
Cytogenetic location: 1q32.2 Genomic coordinates (GRCh38): 1:207,321,678-207,360,966 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 1q32.2 | [Blood group Cromer] | 613793 | Autosomal recessive | 3 |
| Complement hyperactivation, angiopathic thrombosis, and protein-losing enteropathy | 226300 | Autosomal recessive | 3 |
The major isoform of DAF, or CD55, is a 70-kD plasma membrane protein that is widely distributed on all blood cells and on endothelial and epithelial tissues. The physiologic role of DAF is to inhibit the complement cascade at the level of the critical C3 (120700) convertase step. By this mechanism, DAF protects autologous cells and tissues from complement-mediated damage and thereby plays a role in preventing or modulating autoimmune disease and inflammation. DAF also serves as a receptor for certain strains of E. coli and certain types of enteroviruses. Variation in DAF forms the basis of the Cromer blood group system (CROM; 613793) (review by Lublin, 2005). In addition to the major membrane-bound isoform of DAF, several other minor soluble and membrane-bound DAF isoforms are produced by alternative splicing (Osuka et al., 2006)
Avoidance by host tissues of attack by autologous complement proteins is dependent in part on the activities of membrane regulatory factors. One molecule involved in this control is a 70-kD glycoprotein termed decay-accelerating factor (DAF). Interruption by DAF of the complement sequence at an early step in activation effectively halts progression of the cascade and prevents consequent cell injury. In man, a glycolipid-anchored form of DAF is expressed on the plasma membrane of all cell types that are in intimate contact with plasma complement proteins. DAF is also found on the surfaces of epithelial cells lining extracellular compartments, and variants of DAF are present in body fluids and in extracellular matrix. Medof et al. (1987) cloned cDNAs for human DAF. The deduced 376-amino acid protein contains a 29-amino acid N-terminal leader peptide, followed by 4 approximately 61-amino acid repeats of internal homology, a 70-amino acid serine- and threonine-rich segment with multiple potential O-glycosylation sites, and a C-terminal hydrophobic segment. However, the sequence lacks an initiation codon, indicating it is incomplete. Northern blot analysis of HeLa cells and myeloid leukemia cells detected transcripts of 3.1, 2.7, and 2.0 kb.
Osuka et al. (2006) noted that glycosylphosphatidylinositol (GPI)-anchored DAF (gDAF) and soluble DAF (sDAF) are generated by alternative splicing. Insertion of a unique exon (exon 10) into the sDAF cDNA causes a frameshift that results in a unique C-terminal sequence lacking the GPI-anchored portion of gDAF. By RT-PCR of a lung cDNA library, Osuka et al. (2006) cloned 5 additional minor DAF variants. Three of the variants, vDAF1, vDAF2, and vDAF3, include novel exons (exons 11, 12, and 13, respectively) compared with gDAF and, like sDAF, encode proteins lacking the GPI-anchored portion in the C terminus. Variants vDAF4 and vDAF5 include part or all of intron 7, respectively, and encode proteins that retain the GPI-anchored portion of the C terminus but have expanded central STP-rich regions. PCR analysis detected expression of the DAF variants in almost all tissues examined, with higher expression of all variants in lung, liver, and peripheral blood compared with colon and stomach. The main band was derived from gDAF. Transfection of vDAF1, vDAF2, and vDAF3 into Chinese hamster ovary cells resulted in the secretion of these isoforms into the culture medium. Each was highly O-glycosylated prior to secretion. vDAF4 was expressed as a highly O-glycosylated membrane-bound protein.
Osuka et al. (2006) determined that the CD55 gene contains 14 exons.
Lublin et al. (1987) and Lemons et al. (1987) found by study of hamster-human somatic cell hybrids with DAF cDNA clones and by in situ hybridization using the same clones that the gene is located at 1q32. Thus, DAF is closely linked to structural genes for 4 other complement proteins, C4-binding protein (C4BPA; 120830), CR1 (120620), CR2 (120650), and factor H (CFH; 134370), with which it shares 60-amino acid repeats as well as functional similarities. Their close genetic linkage suggests that this complement regulatory gene family evolved from an ancestral C3b-binding molecule.
Hourcade et al. (1992) described 9 overlapping YACs that encompassed a genomic region of 800 kb, encoding 4 RCA (regulator of complement activation) genes and 3 RCA-gene-like elements. An arrangement of CR1, MCP-like, CR1-like, and MCP (120920), in that order, strongly suggested that this region of 1q was generated by a single duplication of neighboring CR1/CR1-like and MCP/MCP-like forerunners.
CD55 is deficient in red blood cells from patients with paroxysmal nocturnal hemoglobinuria (300818). Hamann et al. (1996) found that CD55 is the cellular ligand for CD97 (601211). Erythrocytes from patients with paroxysmal nocturnal hemoglobinuria failed to adhere to cells expressing CD97.
The placenta is an immunologically privileged site. Using DNA microarrays to compare gene expression patterns, Sood et al. (2006) found that 3 regulators of complement, CD55, CD59 (107271), and MCP, are expressed at higher levels in normal placental villus sections compared with other normal human tissues. Within the placenta, CD55 and CD59 are expressed at greatest levels in amnion, followed by chorion and villus sections, whereas MCP is expressed at higher levels only in villus sections. These inhibitors of complement are expressed on syncytiotrophoblasts, the specialized placental cells lining the villi that are in direct contact with maternal blood. The amnion compared with chorion is remarkably nonimmunogenic, and the immune properties of the amnion are intriguing because it is not in direct contact with maternal cells. Sood et al. (2006) suggested that the amnion may secrete the complement inhibitors themselves or in the form of protected exosomes into the amniotic fluid or the neighboring maternofetal junction.
Capasso et al. (2006) showed that stimulation of CD4 (186940) cells through engagement of CD55, either with monoclonal antibodies or with CD97, together with anti-CD3, led to enhanced T-cell proliferation, cytokine production, and expression of activation markers. This activation did not affect CD55-mediated complement inhibition and suggested a novel role for CD55.
Using differential display PCR, Brandt et al. (2005) identified a CD55 splice variant that was overexpressed in a breast cancer cell line displaying increased transendothelial invasiveness. In situ hybridization of tissue microarrays and RT-PCR analysis showed the splice variant was expressed in a proportion of invasive breast cancer tissues but not in normal mammary tissue. Western blot analysis detected the dominant full-length protein at an apparent molecular mass of 70 kD and the isoform at about 45 kD. The isoform was detected in cytoplasm and secreted into the culture medium.
Group B coxsackieviruses (CVBs) must cross the epithelium to initiate infection. Coxsackievirus and adenovirus receptor (CAR, or CXADR; 602621), which mediates attachment and infection by all CVBs, is a component of the tight junction (TJ) and is inaccessible to virus approaching from the apical surface. Using Caco2 human colorectal carcinoma cells, Coyne and Bergelson (2006) showed that CVB attachment to DAF on the apical cell surface activated ABL (189980), triggering RAC1 (602048)-dependent actin rearrangements that permitted virus movement to the TJ. Within the TJ, interaction with CAR promoted conformational changes in the virus capsid that were essential for virus entry and release of viral RNA. Interaction with DAF also activated FYN (137025), which was required for phosphorylation of caveolin-1 (CAV1; 601047) and transport of the virus into the cell within caveolar vesicles. Coyne and Bergelson (2006) concluded that CVBs exploit DAF-mediated signaling pathways to surmount the epithelial barrier.
During infection with Plasmodium falciparum, the cause of severe malaria (see 611162), parasites invade and replicate within erythrocytes. Using RNA interference-based knockdown of gene expression in CD34 (142230)-positive hematopoietic progenitor cells, induction of ex vivo erythropoiesis, and infection of terminally differentiated erythroblasts with P. falciparum, Egan et al. (2015) identified CD55 as a critical factor for parasite invasion. CD44 (107269) also appeared to play a role in invasion. Mature erythrocytes from individuals with the Inab phenotype (i.e., CD55 deficiency) of the Cromer blood group system, as well as CD55-knockdown cells, were refractory to invasion, but not to initial attachment, by laboratory and clinical P. falciparum strains. In contrast, the zoonotic P. knowlesi parasite invaded CD55-null and wildtype erythrocytes similarly, suggesting the existence of a P. falciparum-specific ligand for CD55. Egan et al. (2015) proposed that CD55 is an attractive target for malaria therapeutics and suggested that hematopoietic stem cell-based forward screens may be valuable in identifying host determinants of malaria pathogenesis.
Cromer Blood Group System: Inab Phenotype
The Cromer Inab phenotype (see 613793), or Cromer null, in which red blood cells lack all Cromer system antigens and have a deficiency of DAF, is very rare. In the Japanese man in whom the Inab phenotype was first detected (Daniels et al., 1982), Lublin et al. (1994) demonstrated a nonsense mutation in the DAF gene (W53X; 125240.0001). The mutation truncated DAF near the N terminus, explaining the complete absence of surface DAF in the red cells of the individual. The patient also had protein-losing enteropathy (see 226300) and an ileocecal tumor; after he underwent hemicolectomy, the protein-losing enteropathy was reported to have resolved.
In a 28-year-old Japanese woman (HA) with the Cromer Inab phenotype, Wang et al. (1998) identified homozygosity for a mutation in the CD55 gene (125240.0002) causing activation of a cryptic splice site and generation of a premature stop codon. The proband had no history of intestinal disease.
In a 30-year-old Japanese woman with the Inab phenotype, Daniels et al. (1998) identified homozygosity for the W53X mutation in the DAF gene. The proband was also reported to have a capillary angioma of the small intestine.
Cromer Blood Group System: Dr(a-) Phenotype
In 3 unrelated patients with the Dr(a-) Cromer blood phenotype, Lublin et al. (1991) identified homozygosity for a missense mutation in the DAF gene (S165L; 125240.0003).
In a Russian woman (KZ) with the Dr(a-) phenotype, Lublin et al. (1994) identified the S165L mutation in the DAF gene. Analysis of cDNA yielded 2 products: a full-length 291-bp sequence with the S165L change, and a more abundant 247-bp product. The authors showed that the single nucleotide transition results in 2 changes: an amino acid substitution that is the basis for the antigenic variation, and an alternative splicing event that underlies the decreased expression of DAF in the Dr(a-) phenotype.
In a Japanese female blood donor (Kim) with the Dr(a-) phenotype, Daniels et al. (1998) identified homozygosity for the S165L substitution in the DAF gene.
Complement Hyperactivity, Angiopathic Thrombosis, and Protein-Losing Enteropathy
In 11 patients with complement hyperactivity, angiopathic thrombosis, and protein-losing enteropathy (CHAPLE; 226300) from 8 consanguineous families of Turkish, Moroccan, or Syrian origin, Ozen et al. (2017) identified homozygosity for mutations in the CD55 gene (see, e.g., 125240.0004-125240.0007) that segregated with disease and were not found in controls or in the ExAC database.
In a large consanguineous Muslim-Arab family with protein-losing enteropathy and hypercoagulability, Kurolap et al. (2017) identified homozygosity for a 1-bp deletion in the CD55 gene (125240.0008) that segregated fully with disease.
Egan et al. (2015) identified 2 CD55 polymorphisms that were significantly enriched in persons with ancestral or current exposure to malaria: CROM3 (arg52 to leu) in African Americans in southwestern USA and in the Yoruba ethnic group in Nigeria, and CROM1 (ala227 to pro) in the Luhya ethnic group in Kenya.
Lin et al. (2002) demonstrated enhanced susceptibility to experimental autoimmune myasthenia gravis (254200) in mice lacking Daf. Following anti-AChR Ab injection, Daf1 -/- mice (devoid of neuromuscular DAF protein) showed dramatically greater muscle weakness than their Daf1 +/+ littermates. Reversal of the weakness by edrophonium was consistent with a myasthenic disorder. Immunohistochemistry revealed greatly augmented C3b deposition localized at postsynaptic junctions, and radioimmunoassays showed more profound reductions in AChR levels. Electron microscopy demonstrated markedly greater junctional damage in the Daf1 -/- mice compared with the Daf1 +/+ littermates.
Liu et al. (2005) found that Daf -/- mice had significantly enhanced T-cell responses after immunization. This phenotype was characterized by hypersecretion of Ifng (147570) and Il2 (147680), as well as downregulation of Il10 (124092) upon restimulation of lymphocytes in vitro. Daf1 -/- mice also displayed exacerbated disease progression and pathology in the T cell-dependent experimental autoimmune encephalomyelitis (EAE) model. Both T-cell responses and EAE disease severity could be attenuated by neutralization of the complement system. Liu et al. (2005) concluded that there is a critical link between the complement system and T-cell immunity and proposed that DAF may have a role in organ transplantation and vaccine development.
In a 27-year-old Japanese man (Inab) with absence of all Cromer system antigens on red blood cells (CROM; 613793), originally reported by Daniels et al. (1982), Lublin et al. (1994) identified a homozygous c.314G-A transition in exon 2 of the DAF gene, resulting in a trp53-to-ter (W53X) substitution. The truncation near the amino terminus explained the complete absence of surface DAF in the subject. The patient also had protein-losing enteropathy (see 226300) and an ileocecal tumor; after he underwent hemicolectomy, the protein-losing enteropathy was reported to have resolved.
In a 30-year-old Japanese woman (Osad family) with the Inab phenotype, Daniels et al. (1998) identified homozygosity for the W53X mutation in the DAF gene. Her unaffected parents were heterozygous for the mutation; DNA from her unaffected children was not tested. The proband was also reported to have a capillary angioma of the small intestine.
Ozen et al. (2017) stated that this mutation is a c.261G-A transition in the CD55 gene, resulting in a trp87-to-ter (W83X) substitution.
In a 28-year-old Japanese woman (HA), Wang et al. (1998) demonstrated that the Cromer Inab phenotype (CROM; 613793) was due to homozygosity for a 1579C-A transversion at the position 24 bp upstream of the 3-prime end of exon 2 of the CD55 gene. This substitution caused the activation of a novel cryptic splice site and resulted in the production of mRNA with a 26-bp deletion. The deletion introduced a frameshift and created a stop codon immediately downstream of the deletion. Translation of mRNA would be terminated at the first amino acid residue of the second short consensus repeat (SCR2) domain (exon 3) of DAF. The functional domains of DAF's complement regulatory activity and the C-terminal signal domains for glycosylphosphatidylinositol (GPI) anchoring were predicted to be lacking in the subject. The proband had no history of intestinal disease.
In 3 unrelated patients with the Dr(a-) Cromer blood phenotype (CROM; 613793), including the original Dr(a-) proband (MD) described by Levene et al. (1984), Lublin et al. (1991) identified homozygosity for a c.649C-T transition in exon 5 of the DAF gene, resulting in a ser165-to-leu (S165L) substitution. Western blot analysis of Dr(a-) erythrocytes demonstrated markedly reduced expression of DAF. Radioimmunoassay confirmed markedly reduced reactivity to antibodies to DAF, whereas the Dr(a-) erythrocytes showed normal reactivity to the 3 other GPI-anchored membrane proteins, acetylcholinesterase (100740), CD59 (107271), and CD58 (153420). Lublin et al. (1991) designated the Dr(a-) variant allele of DAF 'Dr(b).'
In a Russian woman (KZ) with the Dr(a-) phenotype, originally studied by Reid et al. (1991), Lublin et al. (1994) identified the S165L mutation in the DAF gene. Analysis of cDNA yielded 2 products: a full-length 291-bp sequence with the S165L change, and a more abundant 247-bp product, corresponding to a 44-bp deletion previously detected by Reid et al. (1991). Lublin et al. (1994) showed that the S165L variant creates a cryptic branch point in the Dr(a-) allele that leads to use of a downstream cryptic acceptor splice site, shifting the reading frame and resulting in a premature stop codon that abrogates membrane anchoring. The authors concluded that the c.649C-T transition results in 2 changes: an amino acid substitution that is the basis for the antigenic variation, and an alternative splicing event that underlies the decreased expression of DAF in the Dr(a-) phenotype. Radioimmunoassay of patient Dr(a-) erythrocytes showed approximately 40% of normal DAF levels, and immunoblot analysis suggested somewhat lower levels.
In a Japanese female blood donor (Kim) with the Dr(a-) phenotype, Daniels et al. (1998) identified homozygosity for the S165L substitution in the DAF gene.
In 4 affected individuals from 3 consanguineous Turkish families (families 2, 3, and 5) with complement hyperactivation, angiopathic thrombosis, and protein-losing enteropathy (CHAPLE; 226300), Ozen et al. (2017) identified homozygosity for a 1-bp deletion (c.109delG) in exon 2 of the CD55 gene, causing a frameshift predicted to result in a premature termination codon (Gly37AlafsTer24). In 1 of the families, an affected sister had died at age 4.5 years with ascites, pleural effusion, and pulmonary infection. The mutation segregated with disease in each of the families and was not found in the ExAC database. Flow cytometry histograms of patient CD4+ T lymphocytes showed no CD55 cell surface expression.
In an 8-year-old Turkish girl (family 1) and a 4-year-old Syrian girl (family 7) with complement hyperactivation, angiopathic thrombosis, and protein-losing enteropathy (CHAPLE; 226300), Ozen et al. (2017) identified homozygosity for a 2-bp deletion/4-bp insertion (c.149_150delAAinsCCTT) in exon 2 of the CD55 gene, causing a frameshift predicted to result in a premature termination codon (Glu50AlafsTer12). The mutation segregated with disease in both families and was not found in the ExAC database. Flow cytometry histograms of patient CD4+ T lymphocytes showed no CD55 cell surface expression.
In 3 affected sibs from a consanguineous family (family 4) with complement hyperactivation, angiopathic thrombosis, and protein-losing enteropathy (CHAPLE; 226300), Ozen et al. (2017) identified homozygosity for a c.800G-C transversion in exon 8 of the CD55 gene, resulting in a cys267-to-ser (C267S) substitution within the fourth short consensus repeat (SCR4) domain. The mutation segregated with disease in the family and was not found in the ExAC database. Flow cytometry histograms of patient CD4+ T lymphocytes showed no CD55 cell surface expression.
In a Turkish boy with complement hyperactivation, angiopathic thrombosis, and protein-losing enteropathy (CHAPLE; 226300), who died of pulmonary embolism at age 15 years, Ozen et al. (2017) identified homozygosity for a splice site mutation (c.287-1G-A) in intron 2 of the CD55 gene, predicted to cause alternative splicing. Flow cytometry histograms of patient CD4+ T lymphocytes showed some residual CD55 cell surface expression.
In 5 affected individuals from a large consanguineous Muslim-Arab family with complement hyperactivation, angiopathic thrombosis, and protein-losing enteropathy (CHAPLE; 226300), 1 of whom died at 4 years of age from disease-related complications, Kurolap et al. (2017) identified homozygosity for a 1-bp deletion at nucleotide 43 (c.43del, NM_001114752.1), causing a frameshift predicted to result in a premature termination codon (Leu15SerfsTer46). The mutation segregated fully with disease in the family. Flow cytometric and hemagglutination studies revealed markedly decreased binding of CD55 antigens on patient erythrocytes and granulocytes compared to controls.
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