Effect of Different Aβ Aggregates as Antigen on the Measure of Naturally Occurring Autoantibodies against Amyloid-β40/42 in IVIG

2020 ◽  
Vol 16 (14) ◽  
pp. 1290-1299
Author(s):  
Haijun Cao ◽  
Xi Du ◽  
Renyong Zeng ◽  
Zhaoji Lv ◽  
Shengliang Ye ◽  
...  
Keyword(s):  
Statistical Analysis ◽  
Western Blot ◽  
Intravenous Immunoglobulin ◽  
Immunosorbent Assay ◽  
Amyloid Β ◽  
Enzyme Linked Immunosorbent Assay ◽  
Nonspecific Binding ◽  
Naturally Occurring ◽  
High Level ◽  
The Impact

Background: The specific Intravenous Immunoglobulin (IVIG) for Alzheimer’s Disease (AD) is developing, which contains a high level of naturally occurring autoantibodies against amyloid-β (nAbs-Aβ), and the measure of nAbs-Aβ content is greatly essential. Though Enzyme-Linked Immunosorbent Assay (ELISA) has been widely used in detecting the nAbs-Aβ content, the impact of Aβ aggregates species chosen as antigen in ELISA on this measure has not been evaluated. Objective: To clarify the influence of different Aβ40/42 aggregates as antigen during ELISA on the content of nAbs-Aβ40/42 measured in IVIG. Method: Preparation of various Aβ40/42 aggregates was performed by different aggregation solutions and various lengths of time, and analyzed by western blot. Different Aβ40/42 aggregates as antigen were adopted to measure the nAbs-Aβ40/42 content in IVIG by ELISA, and the control was carried out to reduce interference of nonspecific binding. The Bonferroni and Dunnett’s T3 were used for statistical analysis. Results: The duration for the formation of Aβ40/42 aggregates had more effect on detecting nAbs-Aβ40/42 content in IVIG than the aggregation solution. Higher content of nAbs-Aβ40/42 in the same IVIG was displayed when measured with Aβ40/42 aggregates at day 3, instead of at day 0.5 and day 7.0. The nAbs- Aβ40/42 contents in the same IVIG measured with Aβ40/42 aggregates prepared in different solutions were obviously different, but there was no significant regularity among them. Conclusion: The nAbs-Aβ40/42 content in the same IVIG is significantly different when measured with Aβ40/42 aggregated under different conditions. The nAbs-Aβ40/42 content in IVIG by antigen-dependent measures, like ELISA, is uncertain.

scholarly journals Interlaboratory Evaluation of Two Enzyme-Linked Immunosorbent Assay Kits for the Determination of Crustacean Protein in Processed Foods

2008 ◽  
Vol 91 (1) ◽  
pp. 123-129 ◽  
Author(s):  
Shinobu Sakai ◽  
Rieko Matsuda ◽  
Reiko Adachi ◽  
Hiroshi Akiyama ◽  
Tamio Maitani ◽  
...  
Keyword(s):  
Standard Deviation ◽  
Relative Standard Deviation ◽  
Immunosorbent Assay ◽  
Soluble Protein ◽  
Enzyme Linked Immunosorbent Assay ◽  
Processed Foods ◽  
Relative Standard ◽  
High Level

Abstract The labeling of foods containing material derived from crustaceans such as shrimp and crab is to become mandatory in Japan because of increases in the number of allergy patients. To ensure proper labeling, 2 novel sandwich enzyme-linked immunosorbent assay (ELISA) kits for the determination of crustacean protein in processed foods, the N kit (Nissui Pharmaceutical Co., Ltd, Ibaraki, Japan) and the M kit (Maruha Nichiro Holdings, Inc., Ibaraki, Japan), have been developed. Five types of model processed foods containing 10 and/or 11.9 g/g crustacean soluble protein were prepared for interlaboratory evaluation of the performance of these kits. The N kit displayed a relatively high level of reproducibility relative standard deviation (interlaboratory precision; 4.08.4 RSDR) and sufficient recovery (6586) for all the model processed foods. The M kit displayed sufficient reproducibility (17.620.5 RSDR) and a reasonably high level of recovery (82103). The repeatability relative standard deviation (RSDr) values regarding the detection of crustacean proteins in the 5 model foods were mostly <5.1 RSDr for the N kit and 9.9 RSDr for the M kit. In conclusion, the results of this interlaboratory evaluation suggest that both these ELISA kits would be very useful for detecting crustacean protein in processed foods.

Denatured virion protein 1 of equine rhinitis B virus 1 contains authentic B-cell epitopes recognised in an enzyme-linked immunosorbent assay—Short communication

2008 ◽  
Vol 56 (2) ◽  
pp. 265-270 ◽  
Author(s):  
Gernot Kriegshäuser ◽  
Anne Cullinane ◽  
Ernst Kuechler ◽  
Timothy Skern
Keyword(s):  
Immunosorbent Assay ◽  
Metal Chelate ◽  
Horse Serum ◽  
Laboratory Diagnosis ◽  
Enzyme Linked Immunosorbent Assay ◽  
Upper Respiratory Tract ◽  
Virion Protein ◽  
Current Standard ◽  
B Virus ◽  
High Level

Equine rhinitis B virus 1 (ERBV1), genus Erbovirus, family Picornaviridae , is a pathogen of horses which causes clinical and subclinical infection of the upper respiratory tract in horses. The virus is widespread in European horse populations and the current standard method for the detection of antibody against ERBV1 is by virus neutralisation (VN). VN tests, however, are labour-intensive and time-consuming, require tissue culture facilities, and generally do not provide same-day results. In this study, a protocol for the high-level expression and purification of recombinant virion protein 1 (rVP1) was established using metal-chelate affinity chromatography under denaturing condition. When used as a coating antigen in a prototype enzyme-linked immunosorbent assay (ELISA), denatured rVP1 was recognised by ERBV1 antibody present in horse serum. This finding suggests that denatured rVP1 is a promising candidate for the development of an ELISA to be used in the routine laboratory diagnosis of ERBV1 infection in horses.

scholarly journals Le diagnostic des encéphalopathies spongiformes chez les ruminants

2004 ◽  
Vol 17 (HS) ◽  
pp. 79-85
Author(s):  
F. LANTIER ◽  
D. MARC ◽  
P. SARRADIN ◽  
P. BERTHON ◽  
R. MERCEY ◽  
...  
Keyword(s):  
Western Blot ◽  
Immunosorbent Assay ◽  
Proteinase K ◽  
Enzyme Linked Immunosorbent Assay ◽  
Post Mortem ◽  
Système Nerveux Central ◽  
Système Nerveux

Le diagnostic des Encéphalopathies Spongiformes Transmissibles (EST) des ruminants est aujourd’hui basé sur la mise en évidence de l’isoforme pathologique, résistante à la protéinase K, de la protéine PrP, la PrPres. La PrPres peut être mise en évidence in situ, à l’aide de techniques immunohistochimiques ou, bien après extraction et traitement à la protéinase K, par des techniques immunochimiques (western blot, Enzyme Linked ImmunoSorbent Assay). Si le diagnostic de routine des encéphalopathies spongiformes animales a fait de gros progrès ces dernières années, il demeure un diagnostic post-mortem qui n’est applicable qu’aux tissus nerveux d’animaux suffisamment âgés pour permettre la formation de dépôts de PrPres dans le système nerveux central. La biopsie d’amygdales offre une possibilité de diagnostic ante-mortem chez les seuls animaux dont le tissu lymphoïde présente une accumulation de PrPres, les ovins génétiquement sensibles et la chèvre. Deux voies de développement des tests sont poursuivies actuellement : d’une part la mise au point d’un diagnostic sanguin précoce basé sur la détection de PrPres ou d’un autre marqueur spécifique de l’incubation d’une EST, et d’autre part des tests permettant de distinguer entre elles les souches de prion, notamment la souche Encéphalopathie Spongiforme Bovine (ESB). Ces évolutions constitueraient un progrès considérable pour notre compréhension des modes de transmission des EST et pour l’efficacité de la prophylaxie sanitaire.

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