Mutagenesis of immunoglobulin-like domains from the extracellular human interferon-γ receptor α chain and their recognition by neutralizing antibodies monitored by surface plasmon resonance technology

Ruegg, N.; Williams, Gwyneth; Birch, Ashley; Schlatter, Daniel; Huber, Walter

doi:10.1016/0022-1759(95)00037-b

Cited by 4 publications

(4 citation statements)

References 18 publications

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“…However, the 295del12 mutant (lacking residues 85-88) was detected by A6, suggesting that the lack of residue 85 was compensated for by the loss of the three neighboring residues. The epitope recognized by γR38 was found to overlap that recognized by A6, accounting for their similar recognition of the mutant 295del12 (19,36,38,39,41,42). Interestingly, the C77Y mutant was not recognized by γR38, even on monocytes, suggesting that Cys 63 and the Cys 63-71 disulfide bridge are essential for the folding of the γR38 epitope.…”

mentioning

confidence: 93%

“…The epitopes recognized by the other mAb's (GIR94, GIR208, 21/31.1, 177.1, and IRγ2) have not yet been mapped. The epitope recognized by A6 has been investigated extensively in recent years by sitedirected mutagenesis and crystallography (37)(38)(39)(40)(41)(42). A6 recognizes a conformational epitope stabilized by Cys 63 (38).…”

mentioning

confidence: 99%

“…The C77Y mutant is recognized on monocytes but not on EBV-B cells by A6, suggesting that Cys 63 and the Cys 63-71 disulfide bridge are important but not essential in the folding of the A6 epitope. A short segment (residues 14-111) in the first domain is well recognized by A6 (39), and several residues, including Trp 85, have been found to be critical for A6 binding (41). However, the 295del12 mutant (lacking residues 85-88) was detected by A6, suggesting that the lack of residue 85 was compensated for by the loss of the three neighboring residues.…”

mentioning

confidence: 99%

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In a novel form of IFN-γ receptor 1 deficiency, cell surface receptors fail to bind IFN-γ

Jouanguy¹,

Dupuis²,

Pallier³

et al. 2000

J. Clin. Invest.

150

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confidence: 93%

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confidence: 99%

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confidence: 99%

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In a novel form of IFN-γ receptor 1 deficiency, cell surface receptors fail to bind IFN-γ

Jouanguy¹,

Dupuis²,

Pallier³

et al. 2000

J. Clin. Invest.

150

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“…The SPR-ellipsometry based optical techniques achieve high sensitivity for the case when large phase change appears on the thin film surfaces. SPR and electrochemical technology have been utilized to analyze the interferon-gamma (IFN-γ) binding reactions with antibodies or other cytokine interaction [5][6][7][8]. + These two authors contributed equally to this work.…”

Section: Introductionmentioning

confidence: 99%

Integrating SPR-ellipsometry and electrochemical measurements for performance evaluation of label-free thiophene-based biosensor

et al. 2014

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The surface plasmon resonance reflectance changes measured with a circularly polarized ellipsometry and an electrochemical impedance spectroscopy were identified to be able to characterize the critical roles of biomolecules for vastly different biological functions and processes. Throughout the course of this study, interferon-gamma (IFN-γ) was chosen as the biomarker to test and to verify the performance of this newly developed system for Tuberculosis detection. The interactions of IFN-γ with immobilized anti-IFN-γ antibody at various concentrations were interrogated both optically and electrochemically. A semi-conductive linker bis-thiophene was thiolated to ensure the cross-linked monoclonal human IFN-γ antibody got self-assembled onto the gold thin film and form a label-free biosensor. The functional features of the bis-thiophene coated-gold film were characterized by cyclic voltammetry and impedance spectroscopy methods. The association of IFN-γ to the bis-thiophene bridging units via antibody-antigen interactions provided the basis for ultrasensitive detection of IFN-γ by tracking the conformation changes in surface-bound protein molecules. The phase shift can be attributed to the average thickness and the real-time index of refraction of the protein layer in different protein layer. Experimental results obtained by impedance spectroscopy and by phase-interrogation SPR showed linear dynamic range. Our experimental results verified that an increase in the concentration of the IFN-γ usually accompanied by phase increase in SPR and an impedance decrease in EIS. These results indicated that our newly developed integrated biosensing system can potentially provide new insight into various conjugate phenomena and interfacial processes for observing molecular conformation changes.

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Variable region cDNA sequences and characterization of murine anti-human interferon γ receptor monoclonal antibodies that inhibit receptor binding by interferon γ

Bridges

Birch

Williams

et al. 1995

Molecular Immunology

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Mutagenesis of immunoglobulin-like domains from the extracellular human interferon-γ receptor α chain and their recognition by neutralizing antibodies monitored by surface plasmon resonance technology

Cited by 4 publications

References 18 publications

In a novel form of IFN-γ receptor 1 deficiency, cell surface receptors fail to bind IFN-γ

In a novel form of IFN-γ receptor 1 deficiency, cell surface receptors fail to bind IFN-γ

Integrating SPR-ellipsometry and electrochemical measurements for performance evaluation of label-free thiophene-based biosensor

Variable region cDNA sequences and characterization of murine anti-human interferon γ receptor monoclonal antibodies that inhibit receptor binding by interferon γ

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