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At least 19 recordsLinked to original sources
PubMed1992

Complete determination of disulfide bonds localized within the short consensus repeat units of decay accelerating factor (CD55 antigen).

Decay accelerating factor (DAF) has 4 SCR (short consensus repeat) units. Each SCR unit consists of approx. 60 amino acids characterized by having four conserved cysteine residues and several other highly conserved residues which include proline, tryptophan, tyrosine/phenylalanine and glycine. To determine the disulfide-bonding pattern, we used the urine form of DAF. After thermolysin and trypsin digestion, we isolated seven disulfide-linked peptides by HPLC purification. Because all of the cysteine residues are disulfide-bonded, DAF should contain eight disulfide bonds. After subtilisin and trypsin digestion, we isolated the eighth disulfide-bonded peptides by HPLC purification. From sequence analyses of these peptides, we could identify all disulfide bonds in the 4 SCR units of DAF as being between the first and the third and between the second and the fourth half-cystines within each SCR unit.

Amino Acid Sequence↗
PubMed2006

A neoadjuvant/adjuvant randomized trial of colorectal cancer patients vaccinated with an anti-idiotypic antibody, 105AD7, mimicking CD55.

PURPOSE: To assess the tolerability and effectiveness of 105AD7 vaccination in colorectal cancer patients. 105AD7 is a human anti-idiotypic antibody mimicking CD55, a glycoprotein, which is more than expressed on colorectal cancer cells and protects them from attack by complement. EXPERIMENTAL DESIGN: Colorectal cancer patients (n = 67) eligible for primary surgery were randomized to receive the anti-idiotypic antibody 105AD7+/-Bacillus Calmette-Guerin/alum or to no treatment (control group). The immunizations were given i.d./i.m. before surgery and continued for a period of 2 years. The patients were monitored in enzyme-linked immunospot (ELISPOT; gamma-IFN), proliferation assay, and Luminex cytokine assays. RESULTS: No serious adverse events were recorded. Of the 32 investigated immunized patients, 14 (44%) were considered to be responders in the ELISPOT assay. Induced proliferative responses were noted in 17 of 40 (43%) monitored patients. There was no correlation between the ELISPOT and proliferation assays. Luminex analyses revealed tumor necrosis factor-alpha and granulocyte macrophage colony-stimulating factor responses not only to the vaccine but also toward the native antigen CD55 in 9 of 13 (69%) patients. CONCLUSIONS: Immune responses to vaccination were induced in a majority of monitored patients measured by ELISPOT and proliferation assay. The lack of correlation between the ELISPOT and proliferation assays may reflect the fact that the two methods measure different T-cell responses and highlights the importance of multiple readouts in evaluating a potential cancer vaccine. Responses to both the anti-idiotype and the CD55 antigen were measurable, adding support to the use of CD55 as a target in cancer treatment.

Adjuvants, Immunologic↗
PubMed1993

[Rapid diagnosis of paroxysmal nocturnal hemoglobinuria by gel test agglutination].

Murine monoclonal antibodies (MoAbs) directed against DAF (Decay Accelerating Factor, CD55 antigen) and MIRL (Membrane Inhibitor of Reactive Lysis, CD59 antigen) were used to identify the affected red cells (CD55-/CD59-) of PNH patients. MoAbs NaM16-4D3 (CD55, IgG2a) and NaM77-1E5 (CD59, IgG3) weakly agglutinate red cells and represent powerful tools to quantitate normal (PNHI) and abnormal (PNHII and PNHIII) cells from PNH patients by indirect flow cytometry. MoAbs NaM125-7H10 (CD55) and NaM123-6G12 (CD59), both IgM, were selected for their agglutinating properties and used for the separation of PNHI from PNHII and PNHIII red cells by the gel test technology. From analysis of artificial mixtures of DAF+ and DAF- cells, a direct relationship was established between fluorescent cells detected by flow cytometry, and erythrocytes agglutinated in microtyping cards. The method was further confirmed by analysis of ten blood samples from PHN patients and represent an alternative to classical hemolysis tests. On the basis of our experience we propose the following for the diagnosis of PNH: 1) agglutination test with NaCl microtyping cards using IgM CD55 and CD59; 2) flow cytometry analysis for accurate quantitation of CD55-/CD59- red cells.

Agglutination Tests↗
PubMed2000

Flow cytometric analysis of glycosylphosphatidyl-inositol-anchored proteins to assess paroxysmal nocturnal hemoglobinuria clone size.

Paroxysmal nocturnal hemoglobinuria (PNH) is characterized by total or partial deficiency of membrane proteins anchored to the cell surface through a glycosylphosphatidyl-inositol (GPI) moiety. The relationship between the size of the PNH clone, determined by the expression of GPI-anchored proteins (AP; CD14, CD48, CD55, CD59, and CD66b) on erythrocytes, lymphocytes, monocytes, and granulocytes using forward and side scatter analysis, and severity of the disease was evaluated in 19 PNH patients. CD55 antigen expression did not delineate abnormal erythrocytes as well as did anti-CD59. The proportion of monocytes deficient in CD55, CD59, CD48, and CD14 (48-97%) and of granulocytes deficient in CD55, CD59, and CD66b (60-99%) was greater than the proportion of erythrocytes deficient in CD59 (24-95%) and the proportion of lymphocytes deficient in CD55 and CD59 (30-98%). There were no significant correlations among reticulocyte, leukocyte, and platelet counts and GPI-AP-deficient immunophenotypes in red and white blood cells. However, high coefficients of determination were seen between hemoglobin levels and granulocytes deficient in CD59 (r(2) = 0.76), CD55 (r(2) = 0.74), and CD66b (r(2) = 0.74) antigens and between hemoglobin and monocytes deficient in CD55 (r(2) = 0.73), CD59 (r(2) = 0.80), and CD14 (r(2) = 0.75) antigens. These results are interpreted as indicating that the size of PNH clone is better assessed by immunophenotypic analysis of monocytes and granulocytes rather than of lymphocytes and erythrocytes.

Adult↗
PubMed2000

105Ad7 cancer vaccine stimulates anti-tumour helper and cytotoxic T-cell responses in colorectal cancer patients but repeated immunisations are required to maintain these responses.

105AD7 is a human anti-idiotypic antibody that recognises the binding site of the anti-tumour antibody 791T/36 and can thereby mimic the CD55 antigen. The molecular basis of 105AD7 mimicry has been identified with 3 CDR regions of 105AD7 showing similarity to 3 regions of CD55. These regions have been analysed for potential T-cell epitopes, and sequences that are predicted to bind to HLA/A1, 3,24 and to HLA/DR1,3,7 have been identified within the CDRH3 region of 105AD7. These epitopes should be stimulating CD8 and CD4 responses, respectively. This prediction was tested on 12 colorectal cancer patients receiving 105AD7 therapy. There was good concordance in 10 of 11 patients between accumulation of CD8RO cells or tumour killing and expression of HLA/A1,3,24. The only patient who failed to respond had a non-permissive class II haplotype and failed to show a helper response. Again 10 of 11 patients showing accumulation of CD4RO cells, in vitro blastogenesis responses, enhanced IL-2 or enhanced NK activity expressed one or more of the HLA/DR1,3,7 haplotypes. Although there was a consistent accumulation of CD45RO cells following 14 of 18 immunisations, only one patient showed a sustained memory response. Our results suggest that 105AD7 can stimulate CD4 and CD8 responses in patients with the appropriate haplotype. However, it may be necessary to continue to immunise, since few patients produce a sustained memory response.

Antibodies, Anti-Idiotypic↗
PubMed1997

Flow cytometry and immunoblotting analysis of monoclonal antibodies directed to complement regulatory proteins.

A series of 18 monoclonal antibodies directed to complement regulatory proteins were investigated by flow cytometry and immunoblotting. Seventeen antibodies are directed against a phosphatidyl inositol-linked glycoprotein since they show a dual population of erythrocytes from a paroxysmal nocturnal haemoglobinuria (PNH) patient. From this group, 6 antibodies revealed a 65-70 kDa band on immunoblots allowing their identification as anti-DAF (Decay Accelerating Factor; CD55 antigen), and 11 bound to a 20 kDa molecule corresponding to MIRL (Membrane Inhibitor of Reactive lysis, CD59 antigen). One antibody revealed an homogeneous population from the PNH patient and bound to a 200 kDa band on immunoblot that might corresponds to the CR1 (Complement Receptor type 1; CD35).

Antibodies, Monoclonal↗
PubMed2005

Functional idiotopes: tumor antigen-directed expression of CD8+ T-cell epitopes nested in unique NH2-terminal VH sequence of antiidiotypic antibodies?

Antiidiotypic antibodies have been and are being used for cancer immunotherapy based on the rationale that Ab2 carrying an "internal image" of the corresponding tumor antigen can induce tumor antigen-specific antibodies (i.e., Ab3 and inhibit tumor growth). Recent evidence indicates that Ab2 also induces cellular responses by CD4+ and CD8+ T cells. This finding has raised the question of where the short peptides, which express CD8+ T-cell-defined epitopes, are located and their relationship with the tumor antigen. We found that two of the four known Ab2 associated with tumor antigen, with known amino acid sequence, express unique NH2-terminal V(H) sequences which precede the framework regions. Both the unique and the shared NH2-terminal V(H) sequences are nested MHC class I antigen-binding peptides. These peptides were highly homologous with peptides from corresponding tumor antigen (carcinoembryonic antigen, CD55, and human high molecular weight melanoma-associated antigen) but differed from the tumor antigen peptides by the presence of the side chain known to mediate stronger forces of interaction with other atoms. The presence of candidate CTL epitopes in NH2-terminal V(H) of Ab2 homologous with tumor antigen may be important for the development of novel immunotherapeutic strategies for cancer.

Amino Acid Sequence↗
PubMed1999

Expression of chimeric monomer and dimer proteins on the plasma membrane of mammalian cells.

Targeting of proteins to the plasma membrane of cells may be useful for vaccine development, tissue engineering, genetic research, bioseparations, and disease treatment. The ability of different transmembrane domains (TM) to direct a reporter protein (human alpha-feto protein, AFP) to the surface of mammalian cells was examined. High surface expression was achieved with chimeric proteins composed of AFP and the TM and cytosolic tail of murine B7-1 (AFP-B7) as well as with AFP containing a GPI-anchor from decay-accelerating factor (AFP-DAF). Lower surface expression of AFP was observed when the TM of human platelet-derived growth factor receptor or the human asialoglycoprotein receptor H1 subunit were employed. Introduction of the hinge-CH2-CH3 region of human IgG (gamma1 domain) between AFP and TM allowed efficient formation of disulfide-linked dimers. Surface expression of AFP-gamma1-B7 dimers was impaired compared to AFP-B7 whereas AFP-gamma1-DAF dimers were efficiently targeted to the surface. Accumulation of chimeric proteins on the cell surface did not correlate with the level of protein expression. This study demonstrates that high levels of monomeric and dimeric proteins can be targeted to the cell membrane of mammalian cells by proper selection of TM.

Animals↗
PubMed1997

The plasma membrane polarity of human biliary epithelial cells: in situ immunohistochemical analysis and functional implications.

BACKGROUND/AIMS: In transporting epithelia, like the biliary epithelium, most plasma membrane proteins present a polarized distribution, essential for the maintenance of the structural and functional properties of the epithelium. We therefore analyzed the expression of polarized plasma membrane proteins by human biliary epithelial cells in order to compare them with other transporting epithelial cells and to search for differences in plasma membrane protein expression between their different anatomical subsets. METHODS: We designed an in situ immunohistochemical study of the various anatomical compartments of the human biliary tract in order to assess the pattern of expression of selected polarized plasma membrane proteins, including integrin receptors, ectopeptidases, membrane transporters and GPI-linked proteins. RESULTS: All biliary epithelial cells expressed the same repertoire of integrins, except for integrin chain alpha5, restricted to the intra-hepatic compartments. All biliary epithelial cells expressed the following apical ectopeptidases: aminopeptidase-N, neutral-endopeptidase, dipeptidyl-peptidase IV. All biliary epithelial cells expressed the membrane transporter Na+ K+-ATPase, restricted to the basolateral domain, and the apical transporters CFTR and MDR-1. The apical AE2 anion exchanger was restricted to the small intra-hepatic bile ducts and the gallbladder. The GPI-linked protein protectin was basolateral in the intrahepatic bile ducts and apical in the gallbladder. CONCLUSIONS: The structural organization of the plasma membrane of biliary epithelial cells is very similar to that of other simple epithelia and exhibits a limited degree of heterogeneity.

ATP Binding Cassette Transporter, Subfamily B, Mem↗
PubMed1991

Phosphatidylinositol-glycan linked proteins of the erythrocyte membrane.

The human erythrocyte bears a number of proteins anchored to the outer membrane surface via a phosphatidylinositol-glycan linkage. This class of proteins includes several complement regulatory proteins (including decay-accelerating factor, CD59 antigen (protectin), and C8 binding protein) as well as several enzymes and at least one protein important in cell-cell interaction. In addition, a number of blood group antigens have been identified to reside on proteins with phosphatidylinositol anchors. One blood group (Cromer) resides on DAF. Study of variants in this blood group system has led to interesting information about the function and expression of this protein. Several other blood groups, such as JMH and Holley/Gregory, appear to reside on as yet unidentified phosphatidylinositol-linked proteins. In paroxysmal nocturnal haemoglobinuria, a variable proportion of red cells fail to express or express weakly all phosphatidylinositol-linked proteins. The origin of this deficiency is now being worked out. In addition, individuals with inherited deficiency of DAF or CD59 (protectin) have been identified. Only the latter deficiency leads to a PNH-like syndrome.

Antigens↗
PubMed1999

Complement sensitivity of erythrocytes in a patient with inherited complete deficiency of CD59 or with the Inab phenotype.

We investigated the complement sensitivity of erythrocytes from three patients, one with inherited complete deficiency of CD59, one with the Inab phenotype, and one with paroxysmal nocturnal haemoglobinuria (PNH). The complement lysis sensitivity units on the erythrocytes were 11.7, 4.6, and 47.6 for inherited CD59 deficiency, Inab phenotype, and PNH, respectively. Two-colour flow cytometric analysis showed that the erythrocytes from the three patients consisted of a single population negative for CD59, negative for decay accelerating factor (DAF), and negative for both proteins, respectively. In addition, only the Inab phenotype patient had no haemolysis in vivo. These facts suggest that CD59 deficiency plays a more important role than DAF deficiency in complement-mediated haemolysis in vitro and in vivo, and that deficiency of both proteins, but not CD59 or DAF alone, causes complement sensitivity corresponding to that of PNH III erythrocytes in vitro.

Adult↗
PubMed2000

Molecular basis of Cromer blood group antigens.

BACKGROUND: The Cromer blood group system consists of 10 antigens located on decay-accelerating factor (DAF). Previous molecular genetic analysis has determined the basis for four of these antigens. The present study was undertaken to identify the mutations that determine the remaining antigens. STUDY DESIGN AND METHOD: Existing or new data were used to localize each Cromer system antigen to a specific short consensus repeat (SCR) domain of DAF. The exon encoding that SCR domain was amplified by using the polymerase chain reaction (PCR) on genomic DNA obtained from individuals of that Cromer phenotype, and the DNA product was subjected to DNA sequence analysis. RESULTS: The Tc(a)/Tc(c) polymorphism is due to an R18P amino acid substitution in SCR1 of DAF. The Es(a+)/Es(a-) polymorphism is due to an I46N mutation in SCR1 of DAF. The WES(b)/WES(a) polymorphism is due to an L48R mutation in SCR1 of DAF. The UMC+/UMC- polymorphism is due to a T216M substitution in SCR4 of DAF. CONCLUSIONS: With information from previous reports and the findings of this study, the molecular genetic basis of all known alleles of the Cromer blood group system has been elucidated. Single amino acid substitutions are responsible for 9 of the 10 antigens (all except the multiple-epitope antigen IFC).

Base Sequence↗
PubMed2003

GUTI: a new antigen in the Cromer blood group system.

BACKGROUND: The Cromer blood group system consists of seven high-incidence and three low-incidence antigens carried on decay-accelerating factor (DAF). This report describes the identification and characterization of a new Cromer high-incidence antigen, named GUTI. STUDY DESIGN AND METHODS: RT-PCR and sequence analysis were performed on cDNA prepared from a Chilean donor whose serum contained the alloantibody (anti-GUTI). Based on the observed point mutation, a PCR-RFLP assay using MaeII was developed. To map the epitope, DAF-deletion mutants were tested by immunoblotting with anti-GUTI. RESULTS: Sequence analysis revealed a substitution of 719G>A in DAF in the proband. The proband's parents and two daughters were heterozygotes for 719G>A, one sister whose RBCs typed GUTI- was homozygous for 719A, and one sister had the wild-type DAF (719G). Seven additional heterozygote samples were identified among 214 Chileans. No heterozygotes were found in 197 New York donors. Analysis using DAF-deletion mutants showed the antigenic determinant to be within short consensus repeat (SCR) 4. CONCLUSION: This study describes a novel high- incidence antigen (GUTI) in the Cromer blood group system characterized by the amino acid arginine at position 206 in SCR4 of DAF. The GUTI-negative proband has a substitution mutation that predicts for histidine at this position.

Adult↗
PubMed1988

Identification of human erythrocyte blood group antigens on decay-accelerating factor (DAF) and an erythrocyte phenotype negative for DAF.

Decay accelerating factor (DAF) is a glycoprotein present on the surfaces of many types ofcells in contact with plasma, including erythrocytes, leukocytes, and platelets (reviewed in reference 1). A small amount of DAF is also present in serum. Numerous investigators have demonstrated that DAF inhibits the action of C3 convertases on cell surfaces, and its absence has been shown to be at least partially responsible for the abnormal sensitivity to lysis by complement exhibited by erythrocytes of patients with the acquired stem cell disorder paroxysmal nocturnal hemoglobinuria (PNH) (2). Hereditary absence of DAF has not been previously described. Tc(a) and Cr(a) are high-frequency human erythrocyte antigens . These antigens are part of a family of blood group antigens, designated Cromer related, which are all absent from the null phenotype cell IFC(-) , or Inab (3). Recently, Spring and colleagues (4) have identified two monoclonal antibodies which bound to high frequency red cell antigens absent from the Inab phenotype. They also demonstrated that these antibodies, as well as several human antisera to Cromer-related antigens, bound to a 70-kD glycoprotein when used to stain immunoblots of human erythrocyte membrane proteins . Because the wide tissue distribution of mAb reactivity, along with some of the biochemical characterization and immunoblotting data, was similar to that of DAF, we investigated whether the Cromer-related antigens Cr(a) and Tc(a) resided on the DAF molecule.

Blood Group Antigens↗
PubMed1994

Purified GPI-anchored CD4DAF as a receptor for HIV-mediated gene transfer.

CD4 is the major cellular receptor for the human immunodeficiency virus (HIV). A hybrid gene encoding the extracellular domains of CD4, linked to the sequence encoding the membrane attachment region of the glycosylphosphatidylinositol (GPI)-anchored protein decay accelerating factor (DAF) was stably transfected into HeLa cells. The resultant cell line (T4HD) expressed GPI-anchored CD4DAF at high levels and was susceptible to gene transfer with a recombinant HIV vector. In an effort to expand the spectrum of cells susceptible to HIV gene transfer, CD4DAF was released from the surface of the T4HD cell line by detergent lysis, purified by immunoaffinity chromatography, and reincorporated into native HeLa cells. Incorporation occurred via the GPI anchor as evidenced by cleavage with phosphatidylinositol-specific phospholipase C. More than 95% of the CD4DAF-treated HeLa cells were CD4-positive by flow cytometry, and kinetic analysis demonstrated that over 75% of the fusion protein remained anchored to the cell membrane after 90 min at 37 degrees C. The purified protein retained its ability to bind the envelope protein of HIV. When incorporated, it bound fluorescein isothiocyanate (FITC)-conjugated gp120, and in its soluble form blocked transduction of CD4-positive cells incubated with an HIV-derived vector containing the Neo gene. In contrast to the T4HD cells, exposure of CD4DAF-treated cells to the Neo HIV vector yielded only transient neomycin-resistant colonies. These results suggest that endogenous synthesis of the CD4 molecule may be necessary for successful HIV genomic integration.

Antigens, CD↗