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Results for “Cell-binding assay”

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PubMed2025

A Quantitative Real-Time PCR Assay for Measuring Poxvirus Replication and Cell Binding.

Quantitative real-time PCR (qPCR) is a fast and reliable method to quantify viral genomes as a surrogate to titering on monolayers of cells for measuring virus replication. Whether it be for determining the number of virions released, the total number of genomes produced during infection, or the number of virions bound to a cell, qPCR assays can be adapted to quickly enumerate total viral genomes in a broad range of experiments comparing virus replication under different conditions. In addition, qPCR offers several advantages compared to plaque assays including time, linearity over 9 logs, and scalability from tens-to-hundreds of samples, depending on the qPCR machine. Here we describe a qPCR assay for quantifying vaccinia virus' dsDNA genome that can be used to determine the total number of virions produced. Furthermore, we describe a straightforward protocol for a cell-binding assay that is sensitive enough to use with small concentrations of inoculating virions. This protocol is suitable for measuring the cell-binding ability of mutations that affect virus production and infectivity.

Virus Replication↗
PubMed1977

A solid-phase radioimmunoassay for Epstein-Barr virus-associated membrane antigen prepared from B95-8 cell culture supernatants.

Epstein-Barr virus(EBV)-associated membrane antigen (MA) was concentrated from B95-8 cell culture media by precipitation with polyethylene glycol followed by chromatography on Bio-Gel A-50m. In a RAJI cell-binding assay, MA-positive material could only be found in the void volume of the column. After ultracentrifugation all antigenic activity appeared in the pellet, which suggested that MA was present in aggregates, presumably fragments of cellular membranes and/or virus envelopes. The MA-containing preparation was photopolymerized in polyacrylamide gel. The homogenized gel was used in a solidphase radioimmunoassay with 125l-labeled IgG from an Anti-MA positive reference serum and an anti-MA negative control serum. The specificity of the reaction was confirmed in blocking tests with anti-EBV positive and negative sera. A good correlation was found between the results obtained in the radioimmunoassay and the results obtained in direct immunofluorescence tests for the detection of MA. The existence of at least two subspecificities of the MA complex could be confirmed by this radioimmunoassay.

Antibody Specificity↗
PubMed1979

Interaction between thyroid-stimulating immunoglobulins and thyrotropin receptors in fat cell membranes.

In the TSH radioreceptor assay to study the interaction between Graves' immunoglobulins (Ig) and TSH receptors in guinea pig fat cell membranes, Graves' Ig were found to inhibit [125I]TSH binding to fat cell membranes in a dose-dependent manner. Scatchard analysis of [125I]TSH displacement curves by Graves' Ig indicated a single population of the binding sites in fat cell membranes, in contrast to two populations of TSH-binding sites in the membranes. Displacement of [125I]TSH bound to fat cell membranes by both Graves' Ig and unlabeled TSH were time and temperature dependent, with similar dissociation curves, suggesting a specific binding of Graves' Ig to the membrane sites related to the TSH receptor in the fat cells. Such Ig are referred to as fat cell-binding Ig, to be distinguished from the thyroid-stimulating Ig (TSI) detected by TSH radioreceptor assay using human thyroid membranes. Both fat cell-binding Ig and TSI were detected in the sera of a great majority of untreated patients with Graves' disease. A significant correlation was found between both values (r = 0.80; n = 19; P less than 0.001). According to these results, TSI might represent an autoantibody to the membranes associated with the TSH receptor of the target tissues without a strict organ specificity.

Adipose Tissue↗