Instrumental biosensors: new perspectives for the analysis of biomolecular interactions

Nice, E.C.; Catimel, Bruno

doi:10.1002/(sici)1521-1878(199904)21:4<339::aid-bies11>3.0.co;2-c

Cited by 170 publications

(95 citation statements)

References 79 publications

(123 reference statements)

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“…The R max value for the two sites together was 218 RU. Using 180 and 150 g/liter, respectively, for the refractive index increment for protein and carbohydrate (25), the expected value for R max can be calculated for 1:1 and 2:1 stoichiometry of smCHIR-AB1 binding to IgY. A value of 168 kDa (26) was used for the molecular weight of IgY, and 13.5 kDa was the molecular weight calculated for smCHIR-AB1.…”

Section: Resultsmentioning

confidence: 99%

A Monomeric Chicken IgY Receptor Binds IgY with 2:1 Stoichiometry

Taylor

Beavil

Sutton

et al. 2009

Journal of Biological Chemistry

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Fc receptors link the specificity of the adaptive immune system with the effector mechanisms of innate immune cells. In birds and reptiles, IgY is the principal serum antibody, and both mammalian IgG and IgE have evolved from an IgY-like ancestor, so studies of IgY offer insights into their origins (1). The historical contribution of chicken immunology to a wider understanding of the subject has been considerable (2), and recently several chicken IgY-Fc receptors have been identified. In this paper, the chicken antibody, IgY, is shown to bind to a chicken leukocyte receptor, CHIR-AB1, 4 in a different manner from that of its mammalian orthologues, IgG and IgE, to their respective Fc receptors. Phagocytosis, mediated in mammals by IgG, and passive cutaneous anaphylaxis, mediated by both IgG and IgE in mammals, have been observed in chickens (3, 4), presumably both effected by IgY. In vitro, IgY binds to monocyte cell lines (5, 6), and an IgY receptor (CHIR-AB1) has been identified that is able to mediate the influx of calcium into cells (5).The genes for the mammalian high affinity IgE receptor, and several IgG receptors, are located in the classical Fc receptor cluster, whereas in chickens, this cluster is represented by a single gene, the product of which has been expressed and found not to bind IgY (7). Intriguingly, the first IgY leukocyte receptor, CHIR-AB1, was found to be a member of the chicken leukocyte receptor cluster (LRC) (5), adjacent to over 100 genes with high intersequence homology (8). This finding, together with phylogenetic analysis of the orthologous Fc receptor gene clusters (7, 9), implies that during the evolution of the IgY-like ancestor of both IgG and IgE, antibody-Fc binding function migrated from proteins expressed in the LRC to those in the classical Fc receptor cluster. The human LRC is the site of Fc␣RI, the leukocyte receptor for IgA (an antibody involved in mucosal immunity), the fetal IgG receptor (FcRn, involved in adult IgG homeostasis), and also a number of natural killer cell receptors including the HLA-G ligand, KIR2DL4 (10). A further leukocyte receptor for chicken IgY, also related to LRC receptors, was identified recently, on chromosome 20 (11), and remains to be characterized.Typically, the stoichiometry of the receptor-antibody complex differs for receptors located in the classical Fc receptor cluster and the LRC. Crystal structures of IgG complexes with Fc␥RIII and of IgE with Fc⑀RI show 1:1 receptor:antibody stoichiometry, with the receptor binding across both heavy chains in the lower hinge (12). In contrast, the crystal structure of Fc␣RI complexed with IgA shows 2:1 stoichiometry (13)

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Section: Resultsmentioning

confidence: 99%

A Monomeric Chicken IgY Receptor Binds IgY with 2:1 Stoichiometry

Taylor

Beavil

Sutton

et al. 2009

Journal of Biological Chemistry

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“…Acid-soluble human collagen type I (from human placenta, C7774, Sigma, UK) was immobilized (500-2000 RU) on a CM5 biosensor chip using amine coupling. Immobilized triplehelical peptides composed of GCO(GPO) 10 GCOG-NH 2 ((GPO) 10 , also known as collagen-related peptide or CRP) and GCP(GPP) 10 GCPG-NH 2 ((GPP) 10 ) [22] were immobilized ($2000 RU) using a cysteine coupling kit, according to the manufacturer's instructions [47].…”

Section: Construction Expression and Purification Of Soluble Recombimentioning

confidence: 99%

New assay to detect low‐affinity interactions and characterization of leukocyte receptors for collagen including leukocyte‐associated Ig‐like receptor‐1 (LAIR‐1)

Jiang

Barclay

2009

Eur J Immunol

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Leukocyte activity is controlled by numerous interactions between membrane receptors and ligands on the cell surface. These interactions are of low affinity making detection difficult. We developed a sensitive assay that could readily detect extremely weak interactions such as that between CD200 and the activating receptor CD200RLa (K d 4500 lM) at the protein level. We used the new technology to screen for interactions of inhibitory receptors for collagens. We confirmed that both human and mouse leukocyte-associated Ig-like receptor-1, and in addition the related inhibitory leukocyte Ig-like receptor subfamily B member 4 (CD85K, Gp49B), bound collagen specifically, whereas other cell surface proteins gave no binding. The monomeric affinities of the interactions were then determined to allow comparison with other leukocyte interactions and indicate conditions when these interactions might lead to inhibitory signals.Key words: Collagen . Inhibitory receptor . Leukocyte-associated Ig-like receptor-1 (LAIR-1) . Surface interaction and immunoregulation IntroductionLeukocyte activity is controlled by the interactions of its surface proteins with both soluble factors such as cytokines and chemokines, and ligands on other cells. Thus identification of ligands is essential in understanding the role of the receptors in regulation. However, the interactions of cell surface proteins with other cell surfaces tend to be of very low affinity when determined using isolated recombinant proteins corresponding to the extracellular regions of the proteins. For instance, typical affinities for such interactions are around 2 mM (CTLA4/CD80 K d 5 2 mM, SIRPa/CD47 K d 5 2 mM, CD2/CD58 K d 5 10 mM, CD200/CD200R K d 5 2 mM) [1-6] with fast off rates usually giving half-lives of the order of 1 s. (discussed in [7]). These proteins, of various valencies, could be adapted and applied to screen for cells expressing receptors by flow cytometry and protein microarray [5,8,9]. With the ease of producing panels of recombinant proteins a powerful way of identifying new interactions is by screening at the protein level as illustrated by Eaton and co-workers using libraries of Fc fusion proteins [10].In the present study we developed a highly sensitive beadbinding assay capable of detecting exceptionally weak interactions using immobilized proteins and surface plasmon resonance (SPR). This is the combination of a conventional binding assay using SPR with the screening reagent -multivalent nanoparticles -taking advantage of the avidity of both reactants. Using the new assay we were able to examine the weak interaction between collagen and leukocyte membrane proteins. The recent identification of a motif in collagen as a ligand for the inhibitory leukocyte-associated Ig-like receptor-1 (LAIR-1) is intriguing as it Collagens are the most abundant proteins in the body with major roles in the extracellular matrix of mammalian cells, either as network-forming or fibrillar molecules. They are intimately involved in cell adhesion, migration and different...

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“…To determine the relative affinities of unprocessed VEGF-D (VEGF-D-FULL-N-FLAG) and the VHD of VEGF-D (VEGF-D⌬N⌬C-FLAG) for VEGFR-2 and VEGFR-3, we analyzed the relative binding kinetics for these interactions by biosensor analysis using surface plasmon resonance detection (31) (Fig. 5B).…”

Section: The Fully Processed Form Of Vegf-d Is Predominantly a Non-comentioning

confidence: 99%

Biosynthesis of Vascular Endothelial Growth Factor-D Involves Proteolytic Processing Which Generates Non-covalent Homodimers

Stacker¹,

Stenvers²,

Caesar³

et al. 1999

Journal of Biological Chemistry

299

380

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Instrumental biosensors: new perspectives for the analysis of biomolecular interactions

Cited by 170 publications

References 79 publications

A Monomeric Chicken IgY Receptor Binds IgY with 2:1 Stoichiometry

A Monomeric Chicken IgY Receptor Binds IgY with 2:1 Stoichiometry

New assay to detect low‐affinity interactions and characterization of leukocyte receptors for collagen including leukocyte‐associated Ig‐like receptor‐1 (LAIR‐1)

Biosynthesis of Vascular Endothelial Growth Factor-D Involves Proteolytic Processing Which Generates Non-covalent Homodimers

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