Fine Characterization of a Series of New Monoclonal Antibodies Directed against Glycophorin A

Rasamoelisolo, M.; Czerwiński, Marcin; Bruneau, V.; Lisowska, Elwira; Blanchard, Dominique

doi:10.1159/000461989

Cited by 9 publications

(7 citation statements)

References 31 publications

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“…However, in the epitope 2C3 a distinct increase of the antibody‐binding was observed by replacement of Asp 24 by Glu, which are both acidic. This feature seems to be characteristic for recognition by anti‐Fy6 antibodies, because such strong enhancement of antibody‐binding by amino acid replacement was found in two Fy6 epitopes, and was not observed in other epitopes characterized by replacement analysis (Wasniowska et al ., 1992; Rasamoelisolo et al, 1997; Jaskiewicz et al ., 1999).…”

Section: Discussionmentioning

confidence: 99%

Structural characterization of the epitope recognized by the new anti‐Fy6 monoclonal antibody NaM185‐2C3

Waśniowska

Petit-LeRoux

Tournamille

et al. 2002

Transfusion Medicine

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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). The clone was obtained from splenocytes of mice immunized with CHO cells expressing the recombinant Duffy glycoprotein. NaM185-2C3 recognized a linear epitope, the essential portion of which was pentapeptide Phe-Glu-Asp-Val-Trp comprising amino acid residues 22-26 of the main (336aa) isoform of the Duffy antigen. All the amino acid residues of the epitope, except Asp, were essential for the antibody-binding, because they could not be replaced by any or most other amino acid residues. The Asp residue could be replaced by most other amino acid residues and its replacement by some amino acid residues gave a distinct increase in the antibody-binding. The MoAb NaM185-2C3, similarly as other anti-Fy6 antibodies, inhibits interleukin (IL)-8-binding to the Duffy antigen. A part of the results was presented at ISBT meeting (Blanchard et al., 1998, Vox Sanguinis, 74, S1, Abstract no. 71).

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Section: Discussionmentioning

confidence: 99%

Structural characterization of the epitope recognized by the new anti‐Fy6 monoclonal antibody NaM185‐2C3

Waśniowska

Petit-LeRoux

Tournamille

et al. 2002

Transfusion Medicine

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“…Moreover, treating sheep erythrocytes with trypsin did not improve their trace agglutination by anti‐ C. braakii O37 serum (data not shown). These results implied that glycophorin A, which can be cleaved by trypsin (Rasamoelisole et al , 1997), masked the epitope recognized by anti‐ C. braakii O37 antibodies and, when removed by trypsin, the epitope became more available to these antibodies.…”

Section: Resultsmentioning

confidence: 97%

Antibodies againstCitrobacter braakiiO37 cells recognize theN-glycan of the band 3 glycoprotein of human erythrocyte membrane

Ebaid

Duk

Gamian

2008

FEMS Immunology &Amp; Medical Microbiology

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The phenomenon of molecular mimicry was found previously for Citrobacter braakii O37, which shared epitopes with human and horse erythrocytes. The aim of this study was to elucidate the basis of the serological cross-reactivity between anti-C. braakii O37 serum and human erythrocytes. The experiments involved analyzing the epitope on the human erythrocyte membrane, that could be recognized by affinity-purified antibodies. The results indicated a specific glycoprotein fraction in immunoblotting, namely band 3, which interacted with the antibodies purified on lipopolysaccharide from C. braakii O37 LPS (LPS O37) and its core affinity columns. Treating the erythrocytes with trypsin, which cleaves glycophorin A, improved the agglutination because band 3 became more available for antibody binding. Isolated band 3 immobilized on an affinity plate could be used to purify antibodies from the anti-C. braakii O37 serum. These antibodies showed a specific reactivity to LPS O37, but not to the related lipopolysaccharide from Salmonella Toucra O48. Furthermore, the inhibition of agglutination with lactose, the diminished interaction of the specific antibodies purified on LPS O37 with endo-beta-galactosidase-treated band 3, and the reactivity of these antibodies to the 40-kDa fragment of band 3 but not to its trypsin-elaborated 60-kDa fragment, all indicated that the epitope is located on the N-glycan of band 3.

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“…Human MoAbs anti‐D (RH1), ‐C (RH2), ‐E (RH3), ‐c (RH4), ‐e (RH5) and ‐Kell (K1) were also purchased from BioAtlantic. The antiglycophorin A (clone NaM26‐3F4) produced in our Institute ( Rasamoelisolo et al ., 1997 ) was used as positive control for RBCs. Anti‐Fy a (FY1) human polyclonal antibody was prepared in our laboratory from the serum of an immunized patient (H.E.R., titre in indirect antiglobulin test: 128).…”

Section: Methodsmentioning

confidence: 99%

Flow cytometric monitoring of red blood cell chimerism after bone marrow transplantation

David

Bernard

Navenot

et al. 1999

Transfusion Medicine

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Chimerism after bone marrow transplantation (BMT) was investigated by flow cytometry analysis of red blood cells (RBCs) and of reticulocytes using a series of selected monoclonal or polyclonal antibodies directed against ABO, Rhesus, Kell, Duffy or MNSs antigens. The method allows the routine detection of less than 0.1% of positive cells in artificial mixed field populations. Blood samples from 135 patients undergoing BMT were investigated around days 15, 30, 45, 60, 90, 180, and then every 6 months after transplantation. Characteristic patterns showing expression of donor red blood cell antigens (expansion markers) and concomitant decrease of recipient specific antigens (depletion markers) within days 16-20 were observed for 125 successfully engrafted patients. Distinct patterns were obtained in 10 patients. A delay in engraftment was evidenced in four patients by the absence of chimerism during the first 6 months without any sign of relapse. Re-appearance of recipient RBCs and reticulocytes was observed in five patients; it was consistent with relapse that was later confirmed by clinical, haematological and cytogenetic studies. Finally, a stable and partial chimerism with 20% of RBCs expressing a marker from the recipient was observed in one patient without any sign of relapse. The reported investigation demonstrated that flow cytometry of RBCs and reticulocytes represents a powerful method to efficiently monitor bone marrow transplanted patients on a long-term basis.

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Fine Characterization of a Series of New Monoclonal Antibodies Directed against Glycophorin A

Cited by 9 publications

References 31 publications

Structural characterization of the epitope recognized by the new anti‐Fy6 monoclonal antibody NaM185‐2C3

Structural characterization of the epitope recognized by the new anti‐Fy6 monoclonal antibody NaM185‐2C3

Antibodies againstCitrobacter braakiiO37 cells recognize theN-glycan of the band 3 glycoprotein of human erythrocyte membrane

Flow cytometric monitoring of red blood cell chimerism after bone marrow transplantation

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