A5077035016- Glycosylation and Glycoproteins Research
- Blood groups and transfusion
- Monoclonal and Polyclonal Antibodies Research
- Erythrocyte Function and Pathophysiology
- Complement system in diseases
- Carbohydrate Chemistry and Synthesis
- Chemokine receptors and signaling
- T-cell and B-cell Immunology
- Protein purification and stability
- Biochemical and Molecular Research
- Diabetes and associated disorders
- HIV Research and Treatment
- Blood disorders and treatments
- Chronic Lymphocytic Leukemia Research
- Immunotoxicology and immune responses
- Malaria Research and Control
- Psoriasis: Treatment and Pathogenesis
- Invertebrate Immune Response Mechanisms
- Insect Resistance and Genetics
- Metabolism and Genetic Disorders
- Animal Diversity and Health Studies
- Neurobiology and Insect Physiology Research
- Peanut Plant Research Studies
- Cytomegalovirus and herpesvirus research
- Microbial infections and disease research
Polish Academy of Sciences
2002-2020
Ludwik Hirszfeld Institute of Immunology and Experimental Therapy
2003-2020
Opole University of Technology
2009-2019
Lund University
2008
Universidade Estadual de Campinas (UNICAMP)
2008
Immucor (United States)
2008
National Institutes of Health
1985-2008
New York Blood Center
2008
CASI Pharmaceuticals (United States)
1998
University of Louisville
1993-1994
A 175-kilodalton erythrocyte binding protein, EBA-175, of the parasite Plasmodium falciparum mediates invasion erythrocytes. The receptor for EBA-175 is dependent on sialic acid. domain that binds erythrocytes was identified as region II with use truncated portions expressed COS cells. Region II, which contains a cysteine-rich motif, and native bind specifically to glycophorin A, but not B, membrane. Erythrocyte recognition requires both acid peptide backbone A. identification ligand domains...
The human erythrocyte chemokine receptor has recently been shown to be identical the Duffy blood group antigen and is expressed in multiple organs, including kidney. Here we have examined molecular properties of renal isoform. Immunoblot analysis kidney detergent lysates, with a monoclonal antibody (Fy6) antigen, revealed that isoform had mass 43-45 kD, which could distinguished from observed erythroid cells (38-47 kD). Chemical cross-linking membranes 125I-melanoma growth stimulatory...
The major glycopeptides purified from the tryptic digests of M and N blood-group glycoproteins were degraded with cyanogen bromide into two fragments. chemical composition serological activities fragments obtained determined. results show that determinants are located on smaller N-terminal fragments, containing 8 amino acid residues only alkali-labile oligosaccharide chains. Two different in M-specific N-specific glycopeptide. All inhibited Vicia graminea anti-N lectin, but fragment...
Rare polyagglutinable NOR erythrocytes contain three unique globoside (Gb4Cer) derivatives, NOR1, NORint, and NOR2, in which Gal(α1–4), GalNAc(β1–3)Gal(α1–4), Gal(α1–4)GalNAc(β1–3)Gal(α1–4), respectively, are linked to the terminal GalNAc residue of Gb4Cer. NOR1 both terminate with a Gal(α1–4)GalNAc- sequence, react anti-NOR antibodies commonly present human sera. While searching for an enzyme responsible biosynthesis Gal(α1–4)GalNAc, we identified mutation A4GALT gene encoding Gb3/CD77...
Summary. The Duffy antigen/receptor for chemokines (DARC), a seven‐transmembrane glycoprotein carrying the (Fy) blood group, acts as widely expressed promiscuous chemokine receptor. In structure–function study, we analysed binding of and anti‐Fy monoclonal antibodies (mAbs) to K562 cells expressing 39 mutant forms DARC with alanine substitutions spread out on four extracellular domains (ECDs). Using synthetic peptides, defined previously Fy6 epitope (22‐FEDVW‐26), characterized Fy linear...
The mouse hybridoma monoclonal antibody BIII.136 of the IgG2a class is specific for human erythrocyte band‐3 protein. It was shown by means immunoblotting and immunoprecipitation assays that recognized an epitope located in cytoplasmic pole molecule within approximately 20 kDa from N‐terminal end. fragments protein, migrating SDS/polyacrylamide gel electrophoresis 60‐kDa, 40‐kDa 20‐kDa regions, were detected with untreated red‐cell membranes as products autolysis A correlation found between...
Incubation of polyacrylamide gels after electrophoresis glycoproteins with Vicia graminea lectin, labeled radioactive iodine, showed that the lectin was bound strongly to blood‐group N and S s human sialoglycoproteins, weakly major sialoglycoprotein horse red cell membranes, not M sialoglycoprotein. Inhibition binding NN erythrocytes by untreated modified erythrocyte their structurally defined glycopeptide fragments studied. The glycopeptides were desialylation, ‐acetylation, Edman...
Summary The epitope recognized by a new anti‐Fy6 monoclonal antibody (MoAb) (clone name: NaM185‐2C3) was characterized using peptides synthesized on pins (Epitope scanning kit). clone obtained from splenocytes of mice immunized with CHO cells expressing the recombinant Duffy glycoprotein. NaM185‐2C3 linear epitope, essential portion which pentapeptide Phe‐Glu‐Asp‐Val‐Trp comprising amino acid residues 22–26 main (336 aa) isoform antigen. All except Asp, were for antibody‐binding, because...
Summary Four new anti‐Duffy murine monoclonal antibodies (MAbs): two anti‐Fy6 (MIMA‐107 and MIMA‐108), one anti‐Fy a (MIMA‐19) anti‐Fy3 (MIMA‐29) were characterized. Identification of epitopes by means synthetic peptides (Pepscan) showed that the reacted most strongly with containing sequence 19 QLDFEDV 25 Duffy glycoprotein, less LDFEDV (MIMA‐107) or LDF only (MIMA‐108). The recognized epitope 38 DGDYGA 43 Gly 42 residue, which defines Fy blood group antigen. MIMA‐29 is first reactive...
ABSTRACT A biotinylated peptide covering a sequence of 21 amino acids (aa) from the erythrocyte binding antigen (EBA-175) Plasmodium falciparum bound to human glycophorin A, an receptor for merozoites, as demonstrated by enzyme-linked immunosorbent assay (ELISA) and erythrocytes flow cytometry analysis. The peptide, EBA(aa1076–96), also desialylated B when tested ELISA. blocked parasite multiplication in vitro. was further delineated 12-aa sequence, EBA(aa1085–96), testing range truncated...
The Miltenberger (Mi) subsystem, which originally consisted of four phenotypes, now has 11 phenotypes. antigens this subsystem belong to the MNS blood group system. Mia antigen been reported be present on red cells with several namely: Mi.I, Mi.II, Mi.III, Mi.IV, Mi.VI and Mi.X. However, existence as a separate entity in question difficult prove polyclonal reagents. We report first monoclonal anti-Mia (GAMA210), whose epitope is TNDKHKRD or QTNDMHKR, thereby confirm antigen.
Purified and desialized blood‐group‐M glycoprotein from human O erythrocytes precipitated with a lectin isolated Euonymus europaeus seeds. The precipitation was inhibited completely by lacto‐N‐fucopentaose I lactose. H2 N‐terminal tryptic fragment of M (MT), containing most carbohydrate all fucose [Lisowska Jeanloz (1973) Carbohydr. Res. 29 , 181 ‐ 191], did not precipitate the but inhibit precipitation. Reduced alkali‐labile oligosaccharides glycopeptide alkali‐stable oligosaccha‐ride were...
BACKGROUND: The blood group antigens S and s are defined by amino acids Met or Thr at position 29, respectively, on glycophorin B (GPB). Commercial anti‐s reagents expensive to produce because of the scarcity human serum. Our aim was develop hybridoma cell lines that secrete reagent‐grade monoclonal antibodies (MoAbs) supplement supply reagents. STUDY DESIGN AND METHODS: Mice were immunized with GPB peptide sequence TKSTISSQTNGE T GQLVHRF. Hybridomas produced fusing mouse splenocytes myeloma...
A warm auto‐antibody with specificity in the Pr blood group system was demonstrated serum and red cell eluate of a patient purine nucleoside phosphorylase (NP) deficiency. The antibody reacted all cells tested except En(a‐) which lack glycophorin A, major erythrocyte sialoglycoprotein. However, anti‐Ena ruled out by absorption cells. similar serologic characteristics to Pra antibodies, that those previously described were inactive protease‐ treated cells, while this case, reactivity...