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Dennis R Burton - One of the best experts on this subject based on the ideXlab platform.

  • anti acetylcholine receptor fab fragments isolated from thymus derived phage display libraries from myasthenia gravis patients reflect predominant specificities in serum and block the action of pathogenic serum antibodies
    Immunology Letters, 1997
    Co-Authors: Yvo M F Graus, Marc H De Baets, Peter J C Van Breda Vriesman, Dennis R Burton
    Abstract:

    Abstract Myasthenia gravis (MG) is a prototype antibody-mediated autoimmune disease in which antibodies against nicotinic acetylcholine receptors (AChR) induce loss of functional receptors at the neuromuscular junction. Germinal centers present in MG hyperplastic thymus contain activated B-cells spontaneously producing anti-human AChR (huAChR) Ab in vitro. In order to access the anti-huAChR repertoire phage display Fab libraries of thymic lymphocytes were constructed from two MG patients. A total of four Fabs highly specific for huAChR were isolated that bind to determinants in or near the main immunogenic region (MIR). These anti-huAChR Fabs showed evidence of significant somatic mutations supporting the notion that the anti-huAChR Ab response in MG patients is driven by antigen. A total of two Fabs were able to inhibit up to 90% of donor serum anti-huAChR antibodies. Competition with serum anti-huAChR Ab was also observed in unrelated MG patients and indicate that anti-huAChR Fabs bind to epitopes on huAChR recognized by the majority of MG patients. In vitro antigenic modulation studies demonstrated that anti-huAChR Fabs were able to induce AChR loss when cross-linked by an anti-Fab antibody but not as monovalent Fab. Moreover, anti-huAChR Fabs were able to protect against AChR loss by antigenic modulation induced by MG serum antibodies suggesting a potential therapeutic role for these recombinant Fabs in patients with a myasthenic crisis.

  • human anti nicotinic acetylcholine receptor recombinant fab fragments isolated from thymus derived phage display libraries from myasthenia gravis patients reflect predominant specificities in serum and block the action of pathogenic serum antibodies
    Journal of Immunology, 1997
    Co-Authors: Yvo M F Graus, Peter J C Van Breda Vriesman, M De Baets, Paul W H I Parren, Sonia Berrihaknin, John H J Wokke, Dennis R Burton
    Abstract:

    Myasthenia gravis (MG) is a prototype Ab-mediated autoimmune disease in which Abs against nicotinic acetylcholine receptors (AChR) induce loss of functional receptors at the neuromuscular junction. Germinal centers present in MG hyperplastic thymus contain activated B cells spontaneously producing anti-human AChR (anti-huAChR) Ab in vitro. To access the anti-huAChR repertoire, phage display Fab libraries of thymic lymphocytes were constructed from two MG patients. Four Fabs highly specific for huAChR were isolated that bind to determinants in or near the main immunogenic region. These anti-huAChR Fabs showed evidence of significant somatic mutations, supporting the idea that the anti-huAChR Ab response in MG patients is driven by Ag. Two Fabs were able to inhibit up to 90% of donor serum anti-huAChR Abs. Competition with serum anti-huAChR Ab was also observed in unrelated MG patients and indicate that anti-huAChR Fabs bind to epitopes on huAChR recognized by the majority of MG patients. In vitro antigenic modulation studies demonstrated that anti-huAChR Fabs were able to induce AChR loss when cross-linked by an anti-Fab Ab but not as monovalent Fab. Moreover, anti-huAChR Fabs were able to protect against AChR loss by antigenic modulation induced by MG serum Abs, suggesting a potential therapeutic role for these recombinant Fabs in patients with a myasthenic crisis.

  • human antibody responses to hiv type 1 glycoprotein 41 cloned in phage display libraries suggest three major epitopes are recognized and give evidence for conserved antibody motifs in antigen binding
    AIDS Research and Human Retroviruses, 1996
    Co-Authors: James M Binley, Joseph Sodroski, Paul W H I Parren, Henrik J Ditzel, Carlos F Barbas, Nancy J Sullivan, Dennis R Burton
    Abstract:

    ABSTRACT A large panel of human Fab fragments against the gp41 subunit of the HIV-1 envelope glycoprotein was isolated by panning six phage-displayed antibody libraries against recombinant gp41. The libraries were prepared from HIV-1-seropositive donors. Twenty-three Fabs recognizing conformation-dependent determinants on gp41 were isolated. Further selection of libraries against (1) gp41 ligated with Fabs from the initial selection and against (2) a recombinant gp41-containing gp140 protein yielded five additional Fabs. Competition of members of the Fab panel with one another and with previously described antibodies revealed a series of overlapping specificities that were conveniently grouped into three major epitope clusters. The majority of Fabs recognized epitopes involving residues 649–668 (previously known as the cluster II region), numbered using the Los Alamos LAI sequence. A second set of Fabs reacted with an epitope involving residues 584–609 (known as the cluster I region). Another set of Fabs ...

Yvo M F Graus - One of the best experts on this subject based on the ideXlab platform.

  • anti acetylcholine receptor fab fragments isolated from thymus derived phage display libraries from myasthenia gravis patients reflect predominant specificities in serum and block the action of pathogenic serum antibodies
    Immunology Letters, 1997
    Co-Authors: Yvo M F Graus, Marc H De Baets, Peter J C Van Breda Vriesman, Dennis R Burton
    Abstract:

    Abstract Myasthenia gravis (MG) is a prototype antibody-mediated autoimmune disease in which antibodies against nicotinic acetylcholine receptors (AChR) induce loss of functional receptors at the neuromuscular junction. Germinal centers present in MG hyperplastic thymus contain activated B-cells spontaneously producing anti-human AChR (huAChR) Ab in vitro. In order to access the anti-huAChR repertoire phage display Fab libraries of thymic lymphocytes were constructed from two MG patients. A total of four Fabs highly specific for huAChR were isolated that bind to determinants in or near the main immunogenic region (MIR). These anti-huAChR Fabs showed evidence of significant somatic mutations supporting the notion that the anti-huAChR Ab response in MG patients is driven by antigen. A total of two Fabs were able to inhibit up to 90% of donor serum anti-huAChR antibodies. Competition with serum anti-huAChR Ab was also observed in unrelated MG patients and indicate that anti-huAChR Fabs bind to epitopes on huAChR recognized by the majority of MG patients. In vitro antigenic modulation studies demonstrated that anti-huAChR Fabs were able to induce AChR loss when cross-linked by an anti-Fab antibody but not as monovalent Fab. Moreover, anti-huAChR Fabs were able to protect against AChR loss by antigenic modulation induced by MG serum antibodies suggesting a potential therapeutic role for these recombinant Fabs in patients with a myasthenic crisis.

  • human anti nicotinic acetylcholine receptor recombinant fab fragments isolated from thymus derived phage display libraries from myasthenia gravis patients reflect predominant specificities in serum and block the action of pathogenic serum antibodies
    Journal of Immunology, 1997
    Co-Authors: Yvo M F Graus, Peter J C Van Breda Vriesman, M De Baets, Paul W H I Parren, Sonia Berrihaknin, John H J Wokke, Dennis R Burton
    Abstract:

    Myasthenia gravis (MG) is a prototype Ab-mediated autoimmune disease in which Abs against nicotinic acetylcholine receptors (AChR) induce loss of functional receptors at the neuromuscular junction. Germinal centers present in MG hyperplastic thymus contain activated B cells spontaneously producing anti-human AChR (anti-huAChR) Ab in vitro. To access the anti-huAChR repertoire, phage display Fab libraries of thymic lymphocytes were constructed from two MG patients. Four Fabs highly specific for huAChR were isolated that bind to determinants in or near the main immunogenic region. These anti-huAChR Fabs showed evidence of significant somatic mutations, supporting the idea that the anti-huAChR Ab response in MG patients is driven by Ag. Two Fabs were able to inhibit up to 90% of donor serum anti-huAChR Abs. Competition with serum anti-huAChR Ab was also observed in unrelated MG patients and indicate that anti-huAChR Fabs bind to epitopes on huAChR recognized by the majority of MG patients. In vitro antigenic modulation studies demonstrated that anti-huAChR Fabs were able to induce AChR loss when cross-linked by an anti-Fab Ab but not as monovalent Fab. Moreover, anti-huAChR Fabs were able to protect against AChR loss by antigenic modulation induced by MG serum Abs, suggesting a potential therapeutic role for these recombinant Fabs in patients with a myasthenic crisis.

Emmanuel Delamarche - One of the best experts on this subject based on the ideXlab platform.

  • a bead based immunogold silver staining assay on capillary driven microfluidics
    Biomedical Microdevices, 2018
    Co-Authors: Ngoc Minh Pham, Sebastian Rusch, Yuksel Temiz, Robert D Lovchik, Hanspeter Beck, Walter Karlen, Emmanuel Delamarche
    Abstract:

    Point-of-care (POC) diagnostics are critically needed for the detection of infectious diseases, particularly in remote settings where accurate and appropriate diagnosis can save lives. However, it is difficult to implement immunoassays, and specifically immunoassays relying on signal amplification using silver staining, into POC diagnostic devices. Effective immobilization of antibodies in such devices is another challenge. Here, we present strategies for immobilizing capture antibodies (cAbs) in capillary-driven microfluidic chips and implementing a gold-catalyzed silver staining reaction. We illustrate these strategies using a species/anti-species immunoassay and the capillary assembly of fluorescent microbeads functionalized with cAbs in “bead lanes”, which are engraved in microfluidic chips. The microfluidic chips are fabricated in silicon (Si) and sealed with a dry film resist. Rabbit IgG antibodies in samples are captured on the beads and bound by detection antibodies (dAbs) conjugated to gold nanoparticles. The gold nanoparticles catalyze the formation of a metallic film of silver, which attenuates fluorescence from the beads in an analyte-concentration dependent manner. The performance of these immunoassays was found comparable to that of assays performed in 96 well microtiter plates using “classical” enzyme-linked immunosorbent assay (ELISA). The proof-of-concept method developed here can detect 24.6 ng mL−1 of rabbit IgG antibodies in PBS within 20 min, in comparison to 17.1 ng mL−1 of the same antibodies using a ~140-min-long ELISA protocol. Furthermore, the concept presented here is flexible and necessitate volumes of samples and reagents in the range of just a few microliters.

  • Toward one-step point-of-care immunodiagnostics using capillary-driven microfluidics and PDMS substrates
    Lab on a Chip, 2009
    Co-Authors: Luc Gervais, Emmanuel Delamarche
    Abstract:

    Point-of-care diagnostics will strongly benefit from miniaturization based on microfluidics because microfluidics integrate functions that can together preserve valuable samples and reagents, increase sensitivity of a test, and accelerate mass transport limited reactions. But a main challenge is to incorporate reagents into microfluidics and to make microfluidics simple to use. Here, we integrate microfluidic functional elements, some of which were developed earlier, and reagents such as detection antibodies (dAbs), capture antibodies (cAbs) and analyte molecules for making one-step immunoassays: the integrated device only requires the addition of sample to trigger a cascade of events powered by capillary forces for effecting a sandwich immunoassay that is read using a fluorescence microscope. The microfluidic elements comprise a sample collector, delay valves, flow resistors, a deposition zone for dAbs, a reaction chamber sealed with a polydimethylsiloxane (PDMS) substrate, and a capillary pump and vents. Parameters for depositing 3.6 nL of a solution of dAb on the chip using an inkjet are optimized and the PDMS substrate is patterned with analytes, which provide a positive control, and cAbs. Various storage conditions of the patterned PDMS are investigated for up to 6 months revealing that storage with a desiccant preserved at least 51% of the activity of the cAbs. C-reactive protein (CRP), a general inflammation and cardiac marker, is detected using this one-step chip using only 5 µL of human serum by measuring fluorescent signals from 30 × 100 µm2 areas of the PDMS substrate in the wet reaction chamber. The one-step chip can detect CRP at a concentration of 10 ng mL−1 in less than 3 min and below 1 ng mL−1 within 14 min. The work presented here may spur the adoption of fluorescence immunoassays using capillary driven microfluidics and PDMS substrates for point-of-care diagnostics.

Peter J C Van Breda Vriesman - One of the best experts on this subject based on the ideXlab platform.

  • anti acetylcholine receptor fab fragments isolated from thymus derived phage display libraries from myasthenia gravis patients reflect predominant specificities in serum and block the action of pathogenic serum antibodies
    Immunology Letters, 1997
    Co-Authors: Yvo M F Graus, Marc H De Baets, Peter J C Van Breda Vriesman, Dennis R Burton
    Abstract:

    Abstract Myasthenia gravis (MG) is a prototype antibody-mediated autoimmune disease in which antibodies against nicotinic acetylcholine receptors (AChR) induce loss of functional receptors at the neuromuscular junction. Germinal centers present in MG hyperplastic thymus contain activated B-cells spontaneously producing anti-human AChR (huAChR) Ab in vitro. In order to access the anti-huAChR repertoire phage display Fab libraries of thymic lymphocytes were constructed from two MG patients. A total of four Fabs highly specific for huAChR were isolated that bind to determinants in or near the main immunogenic region (MIR). These anti-huAChR Fabs showed evidence of significant somatic mutations supporting the notion that the anti-huAChR Ab response in MG patients is driven by antigen. A total of two Fabs were able to inhibit up to 90% of donor serum anti-huAChR antibodies. Competition with serum anti-huAChR Ab was also observed in unrelated MG patients and indicate that anti-huAChR Fabs bind to epitopes on huAChR recognized by the majority of MG patients. In vitro antigenic modulation studies demonstrated that anti-huAChR Fabs were able to induce AChR loss when cross-linked by an anti-Fab antibody but not as monovalent Fab. Moreover, anti-huAChR Fabs were able to protect against AChR loss by antigenic modulation induced by MG serum antibodies suggesting a potential therapeutic role for these recombinant Fabs in patients with a myasthenic crisis.

  • human anti nicotinic acetylcholine receptor recombinant fab fragments isolated from thymus derived phage display libraries from myasthenia gravis patients reflect predominant specificities in serum and block the action of pathogenic serum antibodies
    Journal of Immunology, 1997
    Co-Authors: Yvo M F Graus, Peter J C Van Breda Vriesman, M De Baets, Paul W H I Parren, Sonia Berrihaknin, John H J Wokke, Dennis R Burton
    Abstract:

    Myasthenia gravis (MG) is a prototype Ab-mediated autoimmune disease in which Abs against nicotinic acetylcholine receptors (AChR) induce loss of functional receptors at the neuromuscular junction. Germinal centers present in MG hyperplastic thymus contain activated B cells spontaneously producing anti-human AChR (anti-huAChR) Ab in vitro. To access the anti-huAChR repertoire, phage display Fab libraries of thymic lymphocytes were constructed from two MG patients. Four Fabs highly specific for huAChR were isolated that bind to determinants in or near the main immunogenic region. These anti-huAChR Fabs showed evidence of significant somatic mutations, supporting the idea that the anti-huAChR Ab response in MG patients is driven by Ag. Two Fabs were able to inhibit up to 90% of donor serum anti-huAChR Abs. Competition with serum anti-huAChR Ab was also observed in unrelated MG patients and indicate that anti-huAChR Fabs bind to epitopes on huAChR recognized by the majority of MG patients. In vitro antigenic modulation studies demonstrated that anti-huAChR Fabs were able to induce AChR loss when cross-linked by an anti-Fab Ab but not as monovalent Fab. Moreover, anti-huAChR Fabs were able to protect against AChR loss by antigenic modulation induced by MG serum Abs, suggesting a potential therapeutic role for these recombinant Fabs in patients with a myasthenic crisis.

Paul W H I Parren - One of the best experts on this subject based on the ideXlab platform.

  • human anti nicotinic acetylcholine receptor recombinant fab fragments isolated from thymus derived phage display libraries from myasthenia gravis patients reflect predominant specificities in serum and block the action of pathogenic serum antibodies
    Journal of Immunology, 1997
    Co-Authors: Yvo M F Graus, Peter J C Van Breda Vriesman, M De Baets, Paul W H I Parren, Sonia Berrihaknin, John H J Wokke, Dennis R Burton
    Abstract:

    Myasthenia gravis (MG) is a prototype Ab-mediated autoimmune disease in which Abs against nicotinic acetylcholine receptors (AChR) induce loss of functional receptors at the neuromuscular junction. Germinal centers present in MG hyperplastic thymus contain activated B cells spontaneously producing anti-human AChR (anti-huAChR) Ab in vitro. To access the anti-huAChR repertoire, phage display Fab libraries of thymic lymphocytes were constructed from two MG patients. Four Fabs highly specific for huAChR were isolated that bind to determinants in or near the main immunogenic region. These anti-huAChR Fabs showed evidence of significant somatic mutations, supporting the idea that the anti-huAChR Ab response in MG patients is driven by Ag. Two Fabs were able to inhibit up to 90% of donor serum anti-huAChR Abs. Competition with serum anti-huAChR Ab was also observed in unrelated MG patients and indicate that anti-huAChR Fabs bind to epitopes on huAChR recognized by the majority of MG patients. In vitro antigenic modulation studies demonstrated that anti-huAChR Fabs were able to induce AChR loss when cross-linked by an anti-Fab Ab but not as monovalent Fab. Moreover, anti-huAChR Fabs were able to protect against AChR loss by antigenic modulation induced by MG serum Abs, suggesting a potential therapeutic role for these recombinant Fabs in patients with a myasthenic crisis.

  • human antibody responses to hiv type 1 glycoprotein 41 cloned in phage display libraries suggest three major epitopes are recognized and give evidence for conserved antibody motifs in antigen binding
    AIDS Research and Human Retroviruses, 1996
    Co-Authors: James M Binley, Joseph Sodroski, Paul W H I Parren, Henrik J Ditzel, Carlos F Barbas, Nancy J Sullivan, Dennis R Burton
    Abstract:

    ABSTRACT A large panel of human Fab fragments against the gp41 subunit of the HIV-1 envelope glycoprotein was isolated by panning six phage-displayed antibody libraries against recombinant gp41. The libraries were prepared from HIV-1-seropositive donors. Twenty-three Fabs recognizing conformation-dependent determinants on gp41 were isolated. Further selection of libraries against (1) gp41 ligated with Fabs from the initial selection and against (2) a recombinant gp41-containing gp140 protein yielded five additional Fabs. Competition of members of the Fab panel with one another and with previously described antibodies revealed a series of overlapping specificities that were conveniently grouped into three major epitope clusters. The majority of Fabs recognized epitopes involving residues 649–668 (previously known as the cluster II region), numbered using the Los Alamos LAI sequence. A second set of Fabs reacted with an epitope involving residues 584–609 (known as the cluster I region). Another set of Fabs ...