The Experts below are selected from a list of 120 Experts worldwide ranked by ideXlab platform

Qurban Hussain - One of the best experts on this subject based on the ideXlab platform.

  • Monospecific Antibody against Bordetella pertussis Adenylate Cyclase protects from Pertussis
    Journal of Microbiology and Infectious Diseases, 2012
    Co-Authors: Yasmeen Faiz Kazi, Qurban Hussain
    Abstract:

    Objectives: Acellular pertussis vaccines has been largely accepted world-wide however, there are reports about limited Antibody response against these vaccines suggesting that multiple antigens should be included in acellular vaccines to attain full protection. The aim of present study was to evaluate the role of Bordetella pertussis adenylate cyclase as a protective antigen. Materials and methods: Highly mono-specific Antibody against adenylate cyclase (AC) was raised in rabbits using nitrocellulose bound adenylate cyclase and the specificity was assessed by immuoblotting. B.pertussis 18-323, was incubated with the mono-specific serum and without serum as a control. Mice were challenged intra-nasally and patho physiolgical responses were recorded. Results: The production of B.pertussis adenylate cyclase Monospecific Antibody that successfully recognized on im munoblot and gave protection against fatality (p< 0.01) and lung consolidation (p

  • Monospecific Antibody against bordetella pertussis adenylate cyclase protects from pertussis
    Journal of Microbiology and Infectious Diseases, 2012
    Co-Authors: Yasmeen Faiz Kazi, Qurban Hussain
    Abstract:

    Objectives: Acellular pertussis vaccines has been largely accepted world-wide however, there are reports about limited Antibody response against these vaccines suggesting that multiple antigens should be included in acellular vaccines to attain full protection. The aim of present study was to evaluate the role of Bordetella pertussis adenylate cyclase as a protective antigen. Materials and methods: Highly mono-specific Antibody against adenylate cyclase (AC) was raised in rabbits using nitrocellulose bound adenylate cyclase and the specificity was assessed by immuoblotting. B.pertussis 18-323, was incubated with the mono-specific serum and without serum as a control. Mice were challenged intra-nasally and patho physiolgical responses were recorded. Results: The production of B.pertussis adenylate cyclase Monospecific Antibody that successfully recognized on im munoblot and gave protection against fatality (p< 0.01) and lung consolidation (p <0.01). Mouse weight gain showed significant difference (p< 0.05). Conclusion: These preliminary results highlight the role of the B.pertussis adenylate cyclase as a potential pertussis vaccine candidate. B.pertussis AC exhibited significant protection against pertussis in murine model. J Microbiol Infect Dis 2012; 2(2): 36-43

Takeshi Imamura - One of the best experts on this subject based on the ideXlab platform.

  • direct immobilization of gold binding Antibody fragments for immunosensor applications
    Analytical Chemistry, 2010
    Co-Authors: Takahisa Ibii, Hidenori Shiotsuka, Masaru Kaieda, Mitsuo Umetsu, Hideki Watanabe, Izumi Kumagai, Satoru Hatakeyama, Takeshi Imamura
    Abstract:

    A novel method that enables Antibody fragments to be immobilized on a sensor substrate with a high binding capability using molecular recognition has been developed. Using genetic engineering, we fabricated bispecific recombinant Antibody fragments, which consist of two kinds of Antibody fragments: a gold Antibody fragment and a target molecule Antibody fragment. Surface plasmon resonance (SPR) analysis indicated that these gold-binding bispecific Antibody fragments bind directly to the gold substrate with high affinity (KD ∼ 10−9 M). About 70% of the bispecific Antibody fragments immobilized on the gold substrate retained their target protein-binding efficiency. The Sips isotherm was used to assess the heterogeneity in Antibody affinity for the bispecific Antibody fragments. The results showed that the immobilized bispecific Antibody fragments exhibited an increased homogeneity of affinity (KD) to target molecules when compared with Monospecific Antibody fragments immobilized by conventional methods. The...

  • Direct immobilization of gold-binding Antibody fragments for immunosensor applications
    Analytical Chemistry, 2010
    Co-Authors: Takahisa Ibii, Shuichiro Hatakeyama, Hidenori Shiotsuka, Masaru Kaieda, Mitsuo Umetsu, Hideki Watanabe, Izumi Kumagai, Takeshi Imamura
    Abstract:

    A novel method that enables Antibody fragments to be immobilized on a sensor substrate with a high binding capability using molecular recognition has been developed. Using genetic engineering, we fabricated bispecific recombinant Antibody fragments, which consist of two kinds of Antibody fragments: a gold Antibody fragment and a target molecule Antibody fragment. Surface plasmon resonance (SPR) analysis indicated that these gold-binding bispecific Antibody fragments bind directly to the gold substrate with high affinity (K(D) approximately 10(-9) M). About 70% of the bispecific Antibody fragments immobilized on the gold substrate retained their target protein-binding efficiency. The Sips isotherm was used to assess the heterogeneity in Antibody affinity for the bispecific Antibody fragments. The results showed that the immobilized bispecific Antibody fragments exhibited an increased homogeneity of affinity (K(D)) to target molecules when compared with Monospecific Antibody fragments immobilized by conventional methods. The use of bispecific Antibody fragments to directly immobilize Antibody fragments on a solid-phase substrate offers a useful platform for immunosensor applications.

David J Salant - One of the best experts on this subject based on the ideXlab platform.

  • m type phospholipase a2 receptor as target antigen in idiopathic membranous nephropathy
    The New England Journal of Medicine, 2009
    Co-Authors: Laurence H Beck, Ramon G B Bonegio, David M Beck, Timothy D Cummins, David W Powell, Jon B Klein, Gérard Lambeau, David J Salant
    Abstract:

    BACKGROUND Idiopathic membranous nephropathy, a common form of the nephrotic syndrome, is an Antibody-mediated autoimmune glomerular disease. Serologic diagnosis has been elusive because the target antigen is unknown. METHODS We performed Western blotting of protein extracts from normal human glomeruli with serum samples from patients with idiopathic or secondary membranous nephropathy or other proteinuric or autoimmune diseases and from normal controls. We used mass spectrometry to analyze the reactive protein bands and confirmed the identity and location of the target antigen with a Monospecific Antibody. RESULTS Serum samples from 26 of 37 patients (70%) with idiopathic but not secondary membranous nephropathy specifically identified a 185-kD glycoprotein in nonreduced glomerular extract. Mass spectrometry of the reactive protein band detected the M-type phospholipase A 2 receptor (PLA 2 R). Reactive serum specimens recognized recombinant PLA 2 R and bound the same 185-kD glomerular protein as did the Monospecific anti-PLA 2 R Antibody. Anti-PLA 2 R autoantibodies in serum samples from patients with membranous nephropathy were mainly IgG4, the predominant immunoglobulin subclass in glomerular deposits. PLA 2 R was expressed in podocytes in normal human glomeruli and colocalized with IgG4 in immune deposits in glomeruli of patients with membranous nephropathy. IgG eluted from such deposits in patients with idiopathic membranous nephropathy, but not in those with lupus membranous or IgA nephropathy, recognized PLA 2 R. CONCLUSIONS A majority of patients with idiopathic membranous nephropathy have antibodies against a conformation-dependent epitope in PLA 2 R. PLA 2 R is present in normal podocytes and in immune deposits in patients with idiopathic membranous nephropathy, indicating that PLA 2 R is a major antigen in this disease.

  • M-Type Phospholipase A2 Receptor as Target Antigen in Idiopathic Membranous Nephropathy
    2009
    Co-Authors: Laurence H Beck, Ramon G B Bonegio, David M Beck, Timothy D Cummins, David W Powell, Jon B Klein, Gérard Lambeau, David J Salant
    Abstract:

    Background Idiopathic membranous nephropathy, a common form of the nephrotic syndrome, is an Antibody-mediated autoimmune glomerular disease. Serologic diagnosis has been elusive because the target antigen is unknown. Methods We performed Western blotting of protein extracts from normal human glomeruli with serum samples from patients with idiopathic or secondary membranous nephropathy or other proteinuric or autoimmune diseases and from normal controls. We used mass spectrometry to analyze the reactive protein bands and confirmed the identity and location of the target antigen with a Monospecific Antibody. Results Serum samples from 26 of 37 patients (70%) with idiopathic but not secondary membranous nephropathy specifically identified a 185-kD glycoprotein in nonreduced glomerular extract. Mass spectrometry of the reactive protein band detected the M-type phospholipase A2 receptor (PLA2R). Reactive serum specimens recognized recombinant PLA2R and bound the same 185-kD glomerular protein as did the Monospecific anti-PLA2R Antibody. Anti-PLA2R autoantibodies in serum samples from patients with membranous nephropathy were mainly IgG4, the predominant immunoglobulin subclass in glomerular deposits. PLA2R was expressed in podocytes in normal human glomeruli and colocalized with IgG4 in immune deposits in glomeruli of patients with membranous nephropathy. IgG eluted from such deposits in patients with idiopathic membranous nephropathy, but not in those with lupus membranous or IgA nephropathy, recognized PLA2R. Conclusions A majority of patients with idiopathic membranous nephropathy have antibodies against a conformation-dependent epitope in PLA2R. PLA2R is present in normal podocytes and in immune deposits in patients with idiopathic membranous nephropathy, indicating that PLA2R is a major antigen in this disease.

Yasmeen Faiz Kazi - One of the best experts on this subject based on the ideXlab platform.

  • Monospecific Antibody against Bordetella pertussis Adenylate Cyclase protects from Pertussis
    Journal of Microbiology and Infectious Diseases, 2012
    Co-Authors: Yasmeen Faiz Kazi, Qurban Hussain
    Abstract:

    Objectives: Acellular pertussis vaccines has been largely accepted world-wide however, there are reports about limited Antibody response against these vaccines suggesting that multiple antigens should be included in acellular vaccines to attain full protection. The aim of present study was to evaluate the role of Bordetella pertussis adenylate cyclase as a protective antigen. Materials and methods: Highly mono-specific Antibody against adenylate cyclase (AC) was raised in rabbits using nitrocellulose bound adenylate cyclase and the specificity was assessed by immuoblotting. B.pertussis 18-323, was incubated with the mono-specific serum and without serum as a control. Mice were challenged intra-nasally and patho physiolgical responses were recorded. Results: The production of B.pertussis adenylate cyclase Monospecific Antibody that successfully recognized on im munoblot and gave protection against fatality (p< 0.01) and lung consolidation (p

  • Monospecific Antibody against bordetella pertussis adenylate cyclase protects from pertussis
    Journal of Microbiology and Infectious Diseases, 2012
    Co-Authors: Yasmeen Faiz Kazi, Qurban Hussain
    Abstract:

    Objectives: Acellular pertussis vaccines has been largely accepted world-wide however, there are reports about limited Antibody response against these vaccines suggesting that multiple antigens should be included in acellular vaccines to attain full protection. The aim of present study was to evaluate the role of Bordetella pertussis adenylate cyclase as a protective antigen. Materials and methods: Highly mono-specific Antibody against adenylate cyclase (AC) was raised in rabbits using nitrocellulose bound adenylate cyclase and the specificity was assessed by immuoblotting. B.pertussis 18-323, was incubated with the mono-specific serum and without serum as a control. Mice were challenged intra-nasally and patho physiolgical responses were recorded. Results: The production of B.pertussis adenylate cyclase Monospecific Antibody that successfully recognized on im munoblot and gave protection against fatality (p< 0.01) and lung consolidation (p <0.01). Mouse weight gain showed significant difference (p< 0.05). Conclusion: These preliminary results highlight the role of the B.pertussis adenylate cyclase as a potential pertussis vaccine candidate. B.pertussis AC exhibited significant protection against pertussis in murine model. J Microbiol Infect Dis 2012; 2(2): 36-43

Andrew S Warren - One of the best experts on this subject based on the ideXlab platform.

  • enthalpy entropy compensation in the transition of a Monospecific Antibody towards antigen binding promiscuity
    Molecular Immunology, 2007
    Co-Authors: Jonghoon Kang, Andrew S Warren
    Abstract:

    Abstract In a recent article published in Molecular Immunology (Dimitrov, J.D., Lacroix-Desmazes, S., Kaveri, S.V., Vassilev, T.L., 2007. Transition towards antigen-binding promiscuity of a Monospecific Antibody. Mol. Immunol. 44, 1854–1863.), the authors perform kinetic and thermodynamic analyses using a surface plasmon resonance-based technique to explain polyspecificity of antibodies in terms of molecular mechanisms. They found that after the Antibody was exposed to urea, a protein destabilizing agent, it had the same affinity as the native state and that the two forms of the Antibody use two distinct thermodynamic pathways for binding to the same antigen. In this letter, we report our analysis of these results in terms of equilibrium thermodynamics to show that the specificity transition of the Antibody exhibits enthalpy–entropy compensation.

  • Enthalpy–entropy compensation in the transition of a Monospecific Antibody towards antigen-binding promiscuity
    Molecular Immunology, 2007
    Co-Authors: Jonghoon Kang, Andrew S Warren
    Abstract:

    Abstract In a recent article published in Molecular Immunology (Dimitrov, J.D., Lacroix-Desmazes, S., Kaveri, S.V., Vassilev, T.L., 2007. Transition towards antigen-binding promiscuity of a Monospecific Antibody. Mol. Immunol. 44, 1854–1863.), the authors perform kinetic and thermodynamic analyses using a surface plasmon resonance-based technique to explain polyspecificity of antibodies in terms of molecular mechanisms. They found that after the Antibody was exposed to urea, a protein destabilizing agent, it had the same affinity as the native state and that the two forms of the Antibody use two distinct thermodynamic pathways for binding to the same antigen. In this letter, we report our analysis of these results in terms of equilibrium thermodynamics to show that the specificity transition of the Antibody exhibits enthalpy–entropy compensation.