Detection of Specific Antibodies against Tembusu Virus in Ducks by Use of an E Protein-Based Enzyme-Linked Immunosorbent Assay
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We developed an enzyme-linked immunosorbent assay (ELISA) using eukaryotically expressed E protein as the antigen (termed E-ELISA) to detect antibodies to tembusu virus (TMUV) in ducks. The E-ELISA did not react with antisera to other known pathogens, indicating the E protein is specific for recognizing anti-TMUV antibodies. Compared to the serum neutralization test, the specificity and sensitivity of the E-ELISA was 93.2 and 97.8%, respectively. Therefore, this E-ELISA is a sensitive and rapid method for detecting antibodies against TMUV in ducks.The antiserum against mouse growth hormone (MGH) was produced by immunizing monkeys and some basic immunological properties of the antiserum were studied.The antiserum formed single precipitin lines in agar gel double diffusion plate against both MGH preparation and the crude extract of mouse anterior pituitaries, but reacted with neither normal mouse serum nor the crude extracts of several viscera of mouse. Immunoelectrophoresis of the antiserum with MGH preparation showed a single precipitin arc at the corresponding site of MGH. The precipitin lines between MGH preparation and monkey antiserum and rabbit antiserum to MGH produced previously by us fused completely. Furthermore, the biological activity of MGH was significantly inhibited by the antiserum. All the results have demonstrated that the antiserum obtained in the present experiment contains the antibody specific only to MGH.The cross-reaction test of the antiserum indicates that MGH shares immunologically reactive site identical to that contained in growth hormones of rats, rabbits, goats and cows.
Precipitin
Immunoelectrophoresis
Agar gel
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Extracts from tobacco tissue cultures infected with tobacco mosaic virus grown in medium containing antiserum to the virus had only one‐half to one‐sixteenth as much virus as extracts from tissues grown in medium without the antiserum. When tissues grown with antiserum were thoroughly washed before they were extracted, the extracts contained as much virus as extracts of tissues grown without antiserum. The antiserum did not affect virus multiplication, but antibodies in the tissues may have precipitated virus either in the cells or when the tissues were macerated.
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The neutralization of a constant dose of Semliki Forest virus by various doses of different antisera was studied. The presence of complement (1/200, v/v) in the neutralization mixture inhibited the neutralization by high concentration of antiserum and somewhat potentiated neutralization by low serum concentration. Because the experiments were biased towards a measure of irreversible neutralization, the inhibition observed in the presence of complement appeared to be an inhibition of irreversible neutralization. This inhibition was interpreted as a dissociation of a complement binding virus–antibody complex. The antibodies involved appeared to be virus-specific.
Semliki Forest virus
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The anti-human soluble program death-1(sPD-1) antiserum was prepared by immunizing mice with the purified recombinant sPD-1.Immunoblotting analysis showed that this antiserum had specific reaction with sPD-1,and had some cross-reactivity with bacterial proteins.This cross-reactivity was significantly decreased after treating the antiserum with whole bacterial lysates.PD-1 expressed by activated Jurkat T cells was enriched by affinity chromatography,and assayed by commercial antibody and the antiserum respectively.Only the antiserum identified the natural PD-1,its apparent molecular weight is about 49 000.
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The controlling characteristics of neutralization system in HPO process hexanolactam installation are presented. The reforming status of neutralization system and the methods for increasing the efficiency of neutralization and separation are described. [
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Abstract The majority of infections with SARS-CoV-2 are asymptomatic or mild without the necessity of hospitalization. It is of importance to reveal if these patients develop an antibody response against SARS-CoV-2 and to define which antibodies confer virus neutralization. We conducted a comprehensive serological survey of 49 patients with a mild course of disease and quantified neutralizing antibody responses against a clinical SARS-CoV-2 isolate employing human cells as targets. Four patients (8%), even though symptomatic, did not develop antibodies against SARS-CoV-2 and two other patients (4%) were only positive in one of the six serological assays employed. For the remainder, antibody response against the S-protein correlated with serum neutralization whereas antibodies against the nucleocapsid were poor predictors of virus neutralization. Regarding neutralization, only six patients (12%) could be classified as highly neutralizers. Furthermore, sera from several individuals with fairly high antibody levels had only poor neutralizing activity. In addition, employing a novel serological Western blot system to characterize antibody responses against seasonal coronaviruses, we found that antibodies against the seasonal coronavirus 229E might contribute to SARS-CoV-2 neutralization. Altogether, we show that there is a wide breadth of antibody responses against SARS-CoV-2 in patients that differentially correlate with virus neutralization. This highlights the difficulty to define reliable surrogate markers for immunity against SARS-CoV-2.
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Examination was made of changes in the properties of N-Lauroyl-L-glutamate (LGA) with neutralization. Foaming power was maximum at neutralization of 1.6, and emulsification capacity decreased with neutralization. 13C-NMR indicated α-carboxylic acid of LGA to be neutralized predominantly, and γ-carboxylic acid to be so in proportion to neutralization at 1.6. Fluorescence probe application showed micropolarity and aggregation number of micelles to increase rapidly at neutralization of 1.6. α-carboxylic acid of LGA would thus appear to contribute to interactions between LGA molecules.
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AbstractPurified IgG M-components of all subclasses and antisera raised against different populations of IgG or IgG Fc-fragments were used in an investigation of the influence of the antiserum and of the antigenic composition of the IgG population on the immunochemical quantitation of human IgG. Both the type of antiserum and the antigenic properties of the M-components were found to markedly influence the quantitation. Antisera against IgG Fc-fragments gave much better accuracy and reproducibility from antiserum to antiserum and from M-component to M-component than other antisera. The best antiserum (a rabbit antiserum against polyclonal IgG absorbed with Fab-fragments) gave values which were not influenced by the subclass of the M-component. IgGl(λ) M-components were found to give slightly higher values than IgGl(x) M-components with all antisera used.Key Words: Antiserumimmunochemicalimmunodiffusionimmunoglobulinquantitation
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A rabbit antiserum raised against highly purified, papain‐solubilized H‐2 d antigens contained two sets of non‐crossreacting antibodies directed against each one of the two H‐2 antigen sub‐units. The antiserum recognized only 12,000 and 47,000 dalton polypeptide chains when spleno‐cyte membrane glycoproteins were analysed. Among the molecules precipitated with the rabbit antiserum all H‐2K and D antigens were present. In addition to regular H‐2K and D antigens minor amounts of material with the typical H‐2 antigen subunit structure, but lacking alloantigenic determinants, were precipitated by the antiserum. These ‘non‐H‐2 antigens’ were produced in relatively greater amounts by T‐cells than by B‐cells. Both sets of antibodies in the rabbit antiserum reacted with the TL antigens demonstrating that there is an immunological crossreactivity between the classical alloantigenic H‐2 antigen chain and the alloantigenic TL antigen chain. The F9 cell line, believed to represent cells at the morula stage, display H‐2 antigen‐like structures as revealed by the rabbit antiserum.
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