Some reactions of influenza viruses adsorbed to polystyrene for enzyme immunoassay

Al‐Kaissi, Elham; Mostratos, Ann

doi:10.1016/0166-0934(82)90060-x

Cited by 6 publications

(5 citation statements)

References 3 publications

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“…ASCs in spleen after primary i.v. immunization(1,000 HAU of A/Jap). Values represent mean results from triplicate assays performed on suspensions of pooled cells from 3 to 4 mice.…”

mentioning

confidence: 99%

Influenza virus-specific antibody-secreting cells in the murine lung during primary influenza virus infection

Jones¹,

Ada²

1986

J Virol

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An enzyme-linked immunosorbent plaque assay is described which can reliably enumerate influenza virus-specific antibody-secreting cells and exhibits specificity similar to that of the indirect enzyme-linked immunosorbent assay. The assay was used to characterize the development of specific antibody-secreting cells, principally within lung tissue, during primary murine influenza virus infection after intranasal inoculation. Cells secreting influenza virus-specific immunoglobulin M (IgM), IgG, and IgA were detected in greatest numbers in lung tissue, and the data presented indicated that the cells may have originated from specific B-cell precursors in lung tissue which are demonstratable in vitro. At 11 months after infection, cells secreting IgG and IgA were still present in lung tissue. Influenza virus-specific antibody-secreting cells were also detected in spleen tissue and blood. Antibody-secreting cells appeared earlier in spleen than in lung tissue and declined more rapidly in spleen tissue.

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“…ASCs in spleen after primary i.v. immunization(1,000 HAU of A/Jap). Values represent mean results from triplicate assays performed on suspensions of pooled cells from 3 to 4 mice.…”

mentioning

confidence: 99%

Influenza virus-specific antibody-secreting cells in the murine lung during primary influenza virus infection

Jones¹,

Ada²

1986

J Virol

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“…With such a large array of proteins in live virus particles why are our sdAb specific to a single internal antigen that is not even the most frequent component? Direct adsorption of proteins to polystyrene surfaces used for panning can cause large amounts of protein denaturation [71] and adsorption of virus has been shown to release the contents of influenza A [72] and we would not be surprised if a portion of Ebola virus particles underwent virolysis, thereby exposing internal antigens. Since the washing procedures also used 0.1% Tween-20 we may also have further disrupted the particles during panning and perhaps stripped away loosely attached nucleocapsid proteins leaving a string of NP attached to the genome.…”

Section: Resultsmentioning

confidence: 99%

Ebolavirus Nucleoprotein C-Termini Potently Attract Single Domain Antibodies Enabling Monoclonal Affinity Reagent Sandwich Assay (MARSA) Formulation

Sherwood

Hayhurst

2013

PLoS ONE

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BackgroundAntigen detection assays can play an important part in environmental surveillance and diagnostics for emerging threats. We are interested in accelerating assay formulation; targeting the agents themselves to bypass requirements for a priori genome information or surrogates. Previously, using in vitro affinity reagent selection on Marburg virus we rapidly established monoclonal affinity reagent sandwich assay (MARSA) where one recombinant antibody clone was both captor and tracer for polyvalent nucleoprotein (NP). Hypothesizing that the closely related Ebolavirus genus may share the same Achilles' heel, we redirected the scheme to see whether similar assays could be delivered and began to explore their mechanism.Methods and FindingsIn parallel we selected panels of llama single domain antibodies (sdAb) from a semi-synthetic library against Zaire, Sudan, Ivory Coast, and Reston Ebola viruses. Each could perform as both captor and tracer in the same antigen sandwich capture assay thereby forming MARSAs. All sdAb were specific for NP and those tested required the C-terminal domain for recognition. Several clones were cross-reactive, indicating epitope conservation across the Ebolavirus genus. Analysis of two immune shark sdAb revealed they also targeted the C-terminal domain, and could be similarly employed, yet were less sensitive than a comparable llama sdAb despite stemming from immune selections.ConclusionsThe C-terminal domain of Ebolavirus NP is a strong attractant for antibodies and enables sensitive sandwich immunoassays to be rapidly generated using a single antibody clone. The polyvalent nature of nucleocapsid borne NP and display of the C-terminal region likely serves as a bountiful affinity sink during selections, and a highly avid target for subsequent immunoassay capture. Combined with the high degree of amino acid conservation through 37 years and across wide geographies, this domain makes an ideal handle for monoclonal affinity reagent driven antigen sandwich assays for the Ebolavirus genus.

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“…Due to the unlike charges between viruses and glass surfaces, there is a possibility of adsorption of virus to the inside surfaces of the glass (Gerba 1984). Conversely, viruses adsorb weakly to organic surfaces such as polypropylene and polystyrene (Murray 1980;Al-Kaissi and Mostratos 1982).…”

Section: Thermal Stability Methods In Vitromentioning

confidence: 98%

Comparison of Methods for Evaluating the Thermal Stability of Human Enteric Viruses

Arthur

Gibson

2014

Food Environ Virol

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Human enteric viruses have been identified as one of the predominant causative agents of food-borne illnesses in developed countries, and it is estimated that human norovirus accounts for a majority of these illnesses each year. Not all of these viruses can be cultured and hence relatively little is known about their pathogenesis and physicochemical properties. To overcome this, researchers have utilized different virus surrogates for the study of non-cultivable human enteric viruses. In this review, we discuss various methods utilized for the evaluation of the thermal stability of human enteric viruses, compare the results of these methods, and examine how researchers may move toward a single standard approach (i.e., temperatures, virus concentrations, volume/weight of matrices, etc.) for determining thermal inactivation profiles of human enteric viruses and their surrogates. Based on our review, we found that temperature, time of exposure, type of matrix, analysis type, type of heat application, and the concentration and volume of virus used in the experiments were highly variable across virus surrogates even for the same surrogates. Because of these differences-along with the inherent limitations of using surrogate viruses-comparison of these methods and how the results may be extrapolated to human enteric viruses is quite challenging. As a result, we discuss how researchers may move toward a single standard approach for determining thermal inactivation profiles of human enteric viruses and their surrogates.

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Some reactions of influenza viruses adsorbed to polystyrene for enzyme immunoassay

Cited by 6 publications

References 3 publications

Influenza virus-specific antibody-secreting cells in the murine lung during primary influenza virus infection

Influenza virus-specific antibody-secreting cells in the murine lung during primary influenza virus infection

Ebolavirus Nucleoprotein C-Termini Potently Attract Single Domain Antibodies Enabling Monoclonal Affinity Reagent Sandwich Assay (MARSA) Formulation

Comparison of Methods for Evaluating the Thermal Stability of Human Enteric Viruses

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