Monoclonal anti‐biotin antibodies simulate avidin m the recognition of biotin

Bağcı, Hasan; Kohen, Förtüne; Kuscuoglu, Unsal; Bayer, Edward A.; Wilchek, Meir

doi:10.1016/0014-5793(93)81108-c

Cited by 47 publications

(39 citation statements)

References 18 publications

(9 reference statements)

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“…Recombinant chimeric IgG2 and IgG3 antibodies (against biotin) were produced essentially as described before (21) by cloning synthetic constructs coding for the variable domains (22, 23) and IgG2, IgG3, and κ constant domains (obtained from GeneArt; Invitrogen) into a pcDNA3.1 expression vector (Invitrogen). Other monoclonal IgG1, IgG2, and IgG4 antibodies used were adalimumab (Humira, Abbott), panitumumab (Vectibix, Amgen), and natalizumab (Tysabri, Biogen Idec, Inc.).…”

Section: Methodsmentioning

confidence: 99%

Dynamics of Inter-heavy Chain Interactions in Human Immunoglobulin G (IgG) Subclasses Studied by Kinetic Fab Arm Exchange

Rispens

Davies

Heer

et al. 2014

Journal of Biological Chemistry

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Background: Fab arm exchange requires weak interactions between CH3 domains, such as in human IgG4.Results: CH3-CH3 interactions differ >1,000,000-fold between human subclasses and allotypes due to variations Lys/Asn-392, Val/Met-397, and Lys/Arg-409.Conclusion: For IgG2 and IgG3, but not IgG1, hinge disulfide bonds are essential to prevent half-molecule dissociation.Significance: Subclass/allotype variation in the CH3 domain can alter antibody stability and functionality.

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Section: Methodsmentioning

confidence: 99%

Dynamics of Inter-heavy Chain Interactions in Human Immunoglobulin G (IgG) Subclasses Studied by Kinetic Fab Arm Exchange

Rispens

Davies

Heer

et al. 2014

Journal of Biological Chemistry

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“…Recombinant chimeric IgG1, IgG2, IgG3, and IgG4 antibodies, all specific for biotin, were produced as described previously by cloning synthetic constructs coding for the variable domains and IgG1, IgG2, IgG3, and IgG4 and κ constant domains (GeneArt; Invitrogen) into a pcDNA3.1 expression vector (Invitrogen). Recombinant chimeric IgG1 and IgG4 antibodies (against cat antigen Fel d1 and birch pollen antigen Bet v1) and mutants (IgG1‐C H 3[IgG4], IgG1‐R355Q, IgG1‐K409R, IgG1‐Q419E, IgG1‐P445L) used for pinpointing specific anti‐IgG4–negative RF reactivity were produced as described previously .…”

Section: Methodsmentioning

confidence: 99%

IgG Subclass Specificity Discriminates Restricted IgM Rheumatoid Factor Responses From More Mature Anti–Citrullinated Protein Antibody–Associated or Isotype‐Switched IgA Responses

Falkenburg

Schaardenburg

Heer

et al. 2015

Arthritis & Rheumatology

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Objective To investigate the presence and patterns of specific IgG subclass recognition by IgM rheumatoid factor (IgM‐RF) and IgA‐RF with a newly developed enzyme‐linked immunosorbent assay (ELISA), which can discriminate between polyspecific and restricted RF responses. Methods Polyspecific and restricted RF responses were determined with our ELISA, which uses individually coated recombinant IgG subclasses instead of polyclonal IgG as target antibodies. Fine specificity was determined using target antibodies with single amino acid mutations in the Fc region. Results In a screening panel of 93 sera that were previously found to be IgM‐RF positive in a conventional RF assay, we were able to discriminate between sera with polyspecific IgM‐RF responses (i.e., RF responses directed against all 4 IgG subclasses) and those with restricted IgM‐RF responses, with low or absent relative reactivity against IgG2, IgG3, or IgG4. We found the largest variation for anti‐IgG3 reactivity. Samples without detectable anti‐IgG4 reactivity formed an independent group from the other restricted RF responses and the polyspecific RF responses. The specificity of these anti‐IgG4–negative sera could be pinpointed to single amino acid differences between IgG1 and IgG4. Polyspecific RF responses more often showed signs of RF response maturation, with more isotype switching to IgA‐RF, as compared to restricted RF responses. In a cohort of IgM‐RF+ and/or anti–citrullinated protein antibody (ACPA)–positive arthralgia patients, we found restricted RF responses in 35% (49 of 140) of RF+/ACPA– patients, while RF+/ACPA+ patients, who have a much higher risk of developing rheumatoid arthritis, virtually always (123 of 128 [96%]) showed a polyspecific RF response. Conclusion IgG subclass–specific RF distinguishes between immature restricted RF responses and potentially more pathogenic, ACPA‐associated polyspecific responses.

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“…1B. 38 There are 83 lysine groups per IgG, available for covalent immobilization onto activated NHS ester termini of SAMs.…”

Section: Resultsmentioning

confidence: 99%

“…The typical dimensions of IgG are approximately 4.0 nm × 8.5 nm × 14.5 nm. 38 There are 83 lysine groups per IgG.…”

Section: Methodsmentioning

confidence: 99%

Characterization of protein immobilization on nanoporous gold using atomic force microscopy and scanning electron microscopy

et al. 2011

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Nanoporous gold (NPG), made by dealloying low carat gold alloys, is a relatively new nanomaterial finding application in catalysis, sensing, and as a support for biomolecules. NPG has attracted considerable interest due to its open bicontinuous structure, high surface-to-volume ratio, tunable porosity, chemical stability and biocompatibility. NPG also has the attractive feature of being able to be modified by self-assembled monolayers. Here we use scanning electron microscopy (SEM) and atomic force microscopy (AFM) to characterize a highly efficient approach for protein immobilization on NPG using N-hydroxysuccinimide (NHS) ester functionalized self-assembled monolayers on NPG with pore sizes in the range of tens of nanometres. Comparison of coupling under static versus flow conditions suggests that BSA (Bovine Serum Albumin) and IgG (Immunoglobulin G) can only be immobilized onto the interior surfaces of free standing NPG monoliths with good coverage under flow conditions. AFM is used to examine protein coverage on both the exterior and interior of protein modified NPG. Access to the interior surface of NPG for AFM imaging is achieved using a special procedure for cleaving NPG. AFM is also used to examine BSA immobilized on rough gold surfaces as a comparative study. In principle, the general approach described should be applicable to many enzymes, proteins and protein complexes since both pore sizes and functional groups present on the NPG surfaces are controllable.

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Monoclonal anti‐biotin antibodies simulate avidin m the recognition of biotin

Cited by 47 publications

References 18 publications

Dynamics of Inter-heavy Chain Interactions in Human Immunoglobulin G (IgG) Subclasses Studied by Kinetic Fab Arm Exchange

Dynamics of Inter-heavy Chain Interactions in Human Immunoglobulin G (IgG) Subclasses Studied by Kinetic Fab Arm Exchange

IgG Subclass Specificity Discriminates Restricted IgM Rheumatoid Factor Responses From More Mature Anti–Citrullinated Protein Antibody–Associated or Isotype‐Switched IgA Responses

Characterization of protein immobilization on nanoporous gold using atomic force microscopy and scanning electron microscopy

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