Immunity to tapeworms: intraspecific cross-protective interactions betweenHymenolepis citelli, H. diminutaandH. microstomain mice

SUMMARYInteractions between tapeworm species in a single host offer intriguing opportunities for immunological studies that attempt to identify the mechanism(s) underlying protection against cestode infections. Mice that are immunized againstHymenolepis citelliinfections were shown to be refractory to subsequentH. diminutachallenge infections. The reciprocity of the response was also demonstrated, although the protection recorded forH. diminutawhen mice are sensitized withH. citelliis weaker than that observed when mice are primed withH. diminutaagainstH. citellichallenge.H. citelliwas also shown to be expelled simultaneously during the rejection phase ofH. diminutain concurrent infections, indicating the susceptibility of the former tapeworm to the rejection mechanism initiated by the latter.H. microstomaimmunized mice were shown to be strongly protected against heterologousH. citellichallenge. However, mice primed againstH. citelliwere not as strongly protected againstH. microstomachallenge infections: a statistically significant protection was obtained only after a 12-cysticercoidH. citelliprimary infection, although a 6-cyst infection did stunt the growth ofH. microstomachallenge worms. It is presently suggested that the cross-protective responses observed in the study betweenH. citelli, H. diminutaandH. microstomamay have emanated from a specific immunological cross-reactivity due to the sharing of similar immunogens.

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An isoform of the Ole e 7 allergen assembled by proteomics could explain the cross-reactivity with pollen and food nsLTPs

10.26226/morressier.5acc8ad2d462b8028d89a829 ◽

2018 ◽

Author(s):

Carmen Oeo

Keyword(s):

Cross Reactivity ◽

The Cross

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Cross-reactivity of rapid immunochemical methods for mycotoxins detection towards metabolites and masked mycotoxins: the current state of knowledge

World Mycotoxin Journal ◽

10.3920/wmj2014.1701 ◽

2014 ◽

Vol 7 (4) ◽

pp. 449-464 ◽

Cited By ~ 14

Author(s):

M. Zachariasova ◽

P. Cuhra ◽

J. Hajslova

Keyword(s):

Rapid Test ◽

Cross Reactivity ◽

Rapid Screening ◽

Proficiency Tests ◽

Assigned Value ◽

Screening Practice ◽

Current State ◽

Immunochemical Methods ◽

The Cross ◽

Lateral Flow Test

The cross-reactivity of antibodies employed within immunochemistry-based analytical methods may lead to overestimation of the results. Under certain conditions, specifically when controlling mycotoxin maximum limits serious problems can be encountered. Not only the structurally related mycotoxins, such as their masked (conjugated) forms, but also the unidentified matrix components are responsible for concentration overestimation of respective target analytes. The cross-reactivity phenomenon may also pose a risk of miss-interpretation of the proficiency tests results, when the assigned value becomes influenced by over-estimated results reported by users of immunochemical tests. In this paper, the current state of the knowledge on trueness problems associated with the rapid screening immunochemical methods have been reviewed. Special attention is focused on discussion of cross-reactivity in the ELISA tests, because this rapid test dominates the routine screening practice. However, the cross-reactions reported in lateral flow test strips, fluorescence polarisation immunoassay, or immunosensors have also been addressed.

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Ceftaroline Desensitization Procedure in a Pregnant Patient With Multiple Drug Allergies

Open Forum Infectious Diseases ◽

10.1093/ofid/ofv027 ◽

2015 ◽

Vol 2 (1) ◽

Cited By ~ 3

Author(s):

James L. Kuhlen ◽

Kimberly G. Blumenthal ◽

Caroline L. Sokol ◽

Diana S. Balekian ◽

Ana A. Weil ◽

...

Keyword(s):

Cystic Fibrosis ◽

Staphylococcus Aureus ◽

Methicillin Resistant Staphylococcus Aureus ◽

Skin Testing ◽

Pregnant Patient ◽

Cross Reactivity ◽

Multiple Drug ◽

Methicillin Resistant ◽

The Cross ◽

Staphylococcus Aureus Pneumonia

Abstract Validated skin testing is lacking for many drugs, including ceftaroline. The cross-reactivity between ceftaroline and other β-lactam antibiotics is unknown. We report a case of a pregnant patient with cystic fibrosis and multiple drug allergies who required ceftaroline for methicillin-resistant Staphylococcus aureus pneumonia and underwent an uncomplicated empiric desensitization procedure.

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Allergy to cephalosporin antibiotics in children

Srpski arhiv za celokupno lekarstvo ◽

10.2298/sarh0304127a ◽

2003 ◽

Vol 131 (3-4) ◽

pp. 127-130 ◽

Cited By ~ 1

Author(s):

Marina Atanaskovic-Markovic ◽

Branimir Nestorovic

Keyword(s):

Allergic Reaction ◽

Cross Reactivity ◽

Skin Tests ◽

Allergic Reactions ◽

First Line ◽

Positive Skin ◽

Cephalosporin Antibiotics ◽

The Cross ◽

Single Blind ◽

Common Infections

A particular problem is the safety of administering cephalosporins to penicillin-allergic children, because cephalosporin allergenic determinants have not been properly identified. Cephalosporin antibiotics are widely used to treat common infections and are often the first-line prophylaxis before many types of surgery. So the arm of this study is to determine the frequency of allergic reactions of anaphylactic type to cephalosporins and their cross-reactivity with penicillins. At University Children?s Hospital in Belgrade a group of 1,170 children with suspected anaphylactic allergic reaction to penicillins and/or cephalosporins were tested for the last eight years. Skin tests were performed with standard concentration of penicillins and cephalosporins. In children where skin tests were negative single-blind placebo-controlled challenges were performed. In case of positive skin tests further examinations were interrupted and the children were considered allergic to that drug. The frequency of anaphylactic allergic reactions to cephalosporins is 0.2 % to 17 %, and depends on cephalosporins generation. The cross-reactivity between cephalosporins and penicillins is 0.1 % to 14.5 %, and among cephalosporins is 0 % to 11.7 %.

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Cross-Reactivity between IgE-Binding Proteins from Anisakis Simplex and Dermatophagoides Pteronyssinus

International Journal of Immunopathology and Pharmacology ◽

10.1177/039463200501800408 ◽

2005 ◽

Vol 18 (4) ◽

pp. 671-675 ◽

Cited By ~ 25

Author(s):

R. Bernardini ◽

G. Mistrello ◽

E. Novembre ◽

D. Roncarolo ◽

S. Zanotta ◽

...

Keyword(s):

Molecular Weight ◽

Binding Proteins ◽

Specific Ige ◽

Dermatophagoides Pteronyssinus ◽

Cross Reactivity ◽

Anisakis Simplex ◽

Cross Reaction ◽

Ige Binding ◽

Sds Page ◽

The Cross

An association was found between Anisakis simplex (As) and Dermatophagoides pteronyssinus (Dp) sensitization. One recent study shows a cross-reactivity between As and Dp and tropomyosin (tr) is suspected as being one of the proteins responsible of this cross-reaction. The aim of our study was: 1) to confirm the cross-reactivity between Dp and As; 2) to determine the importance of tr in this cross reaction. SDS-PAGE analysis of Dp and As (metabolic and somatic) extracts was carried out. Then an IgE immunoblotting test using serum from a patient who had specific IgE only to Dp and As and immunoblotting inhibition experiments using Dp extract and tr as inhibitors were performed. We found that patient's serum reacted: 1) against larval As antigens with a molecular weight (mw) of 25 kilodalton (kD) and a mw > 100 kD, 2) against various metabolic As antigens with a mw > 100 kD, a mw ranging approximately from 35 to 50 kD, and a mw around 20 kD, and 3) against Dp proteins with mw between 35 and 55 kD. Preincubation of patient's serum with Dp extract caused the disappearance of reactivity against antigens with a mw > 100 kD in both larval and metabolic As extracts and against proteins with mw ranging approximately from 35 to 50 kD in the metabolic As extract. Preincubation of patient's serum with As extract caused the disappearance of reactivity against antigens with mw between 35 and 55 kD in the Dp extract. Pre-incubation of patient's serum with tr did not induce any change in the immunoblotting profile. The results show that 1) cross-reactive components between Dp and As are some proteins with a mw ranging approximately from 35 to 50 kD and with a mw > 100 kD, and 2) tr is not involved in cross-reactivity between As and Dp.

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A Rapid and International Applicable Diagnostic Device for Cobra (Genus Naja) Snakebites

Toxins ◽

10.3390/toxins12090572 ◽

2020 ◽

Vol 12 (9) ◽

pp. 572

Author(s):

Jing-Hua Lin ◽

Wang-Chou Sung ◽

Jiunn-Wang Liao ◽

Dong-Zong Hung

Keyword(s):

Detection Limits ◽

Rapid Test ◽

Cross Reactivity ◽

Enzyme Linked Immunosorbent Assay ◽

Immunochromatographic Test ◽

Tissue Destruction ◽

Diagnostic Device ◽

Life Threatening ◽

The Cross ◽

Geographical Characteristics

Cobra snakes (genus Naja) are some of the most dangerous snake species in Asia and Africa, as their bites cause severe life-threatening respiratory failure and local tissue destruction, especially in the case of late diagnosis. The differential diagnosis of snakebite envenomation still mainly relies upon symptomatology, the patient’s description, and the experience of physicians. We have designed a rapid test, immunochromatographic test of cobra (ICT-Cobra), which obtained fair results in improving the diagnosis and treatment of Naja (N.) atra snakebites in Taiwan. In this study, we further investigated the feasibility of applying the kit for the detection of other cobra venoms based on the potential interspecies similarity. We firstly demonstrated the cross-reactivity between eight venoms of medically important cobra species and the rabbit anti-N. atra IgG that was used in ICT-Cobra by Western blotting and sandwich enzyme-linked immunosorbent assay. Then, ICT-Cobra was used to detect various concentrations of the eight venoms to elucidate its performance. Noticeable correlations between the cross-reactivity of venoms from genus Naja snakes and existing geographical characteristics were found. ICT-Cobra could detect venoms from other Asian cobras with variable detection limits comparable to those observed for N. atra, but the kit was less successful in the detection of venom from African cobras. The similar but slightly different venom components and the interaction between venom and rabbit anti-N. atra IgG led to variations in the detection limits. The transcontinental usage of ICT-Cobra might be possible due to the cross-reactivity of antibodies and similarities among the larger-sized proteins. This study showed that the close immunological relationships in the genus Naja could be used to develop a venom detection kit for the diagnosis of cobra envenomation in both Asian and African regions. Additional clinical studies and technical adjustments are still needed to improve the efficacy and broadening the application of ICT-Cobra in the future.

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Cannabinol (CBN) Cross-Reacts with Two Urine Immunoassays Designed to Detect Tetrahydrocannabinol (THC) Metabolite

The Journal of Applied Laboratory Medicine ◽

10.1093/jalm/jfaa020 ◽

2020 ◽

Vol 5 (3) ◽

pp. 569-574

Author(s):

Grace M Kroner ◽

Kamisha L Johnson-Davis ◽

Kelly Doyle ◽

Gwendolyn A McMillin

Keyword(s):

Mass Spectrometry ◽

Structural Similarity ◽

Cross Reactivity ◽

Additive Effect ◽

Urine Samples ◽

Spectrometry Method ◽

Confirmatory Testing ◽

Mass Spectrometry Method ◽

Initial Testing ◽

The Cross

Abstract Background The psychoactive component of cannabis, tetrahydrocannabinol (THC), is one of many cannabinoids present in the plant. Since cannabinoids have extensive structural similarity, it is important to be aware of potential cross-reactivity with immunoassays designed to detect THC metabolite. This is especially important as cannabinoid products are increasingly marketed as legal supplements. The objective of this study was to assess the cross-reactivity of 2 commercial immunoassays designed to detect THC metabolite with 4 cannabinoids: cannabidiol, cannabinol, cannabichromene, and cannabigerol. Methods Deidentified residual patient urine samples that tested negative for THC metabolite on initial testing were pooled and fortified with the above compounds to detect cross-reactivity. We next tested a range of CBN concentrations to determine what concentration of CBN was required to trigger a positive immunoassay result. Finally, we tested whether CBN has an additive effect with THC in the immunoassay by adding CBN to 21 samples weakly positive for THC by a mass spectrometry method but negative by the EMIT II Plus immunoassay. Results Both the EMIT II Plus assay and the Microgenics MultiGent assay demonstrated cross-reactivity with CBN. For the EMIT II Plus assay, about 5-fold more CBN than THC metabolite was required to produce an assay signal equivalent to the cutoff concentration, and CBN displayed an additive effect with THC metabolite. For the Microgenics assay, 20-fold more CBN than THC metabolite was required to cross the cutoff concentration. Conclusions These data may help guide the need for confirmatory testing when results of THC metabolite testing by immunoassay are inconsistent with expectations.

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Characterization of cardiac troponin subunit release into serum after acute myocardial infarction and comparison of assays for troponin T and I

Clinical Chemistry ◽

10.1093/clinchem/44.6.1198 ◽

1998 ◽

Vol 44 (6) ◽

pp. 1198-1208 ◽

Cited By ~ 88

Author(s):

Alan H B Wu ◽

Yue-Jin Feng ◽

Robert Moore ◽

Fred S Apple ◽

Paul H McPherson ◽

...

Keyword(s):

Myocardial Infarction ◽

Acute Myocardial Infarction ◽

Cardiac Troponin ◽

Troponin I ◽

Troponin T ◽

Cross Reactivity ◽

Binary Complex ◽

Serum Samples ◽

Binary And Ternary Complexes ◽

The Cross

Abstract We examined the release of cardiac troponin T (cTnT) and I (cTnI) into the blood of patients after acute myocardial infarction (AMI). Three postAMI serum samples were applied in separate analytical runs onto a calibrated gel filtration column (Sephacryl S-200), and the proteins were separated by molecular weight. Using commercial cTnT and cTnI assays measured on collected fractions, we found that troponin was released into blood as a ternary complex of cTnT-I-C, a binary complex of cTnI-C, and free cTnT, with no free cTnI within the limits of the analytical methodologies. The serum samples were also examined after incubation with EDTA and heparin. EDTA broke up troponin complexes into individual subunits, whereas heparin had no effect on the assays tested. We added free cTnC subunits to 24 AMI serum samples and found no marked increase in the total cTnI concentrations, using an immunoassay that gave higher values for the cTnI-C complex than free cTnI. To characterize the cross-reactivity of cTnT and cTnI assays, purified troponin standards in nine different forms were prepared, added to serum and plasma pools, and tested in nine quantitative commercial and pre-market assays for cTnI and one approved assay for cTnT. All nine cTnI assays recognized each of the troponin I forms (complexed and free). In five of these assays, the relative responses for cTnI were nearly equimolar. For the remainder, the response was substantially greater for complexed cTnI than for free cTnI. Moreover, there was a substantial difference in the absolute concentration of results between cTnI assays. The commercial cTnT assay recognized binary and ternary complexes of troponin on a near equimolar basis. We conclude that all assays are useful for detection of cardiac injury. However, there are differences in absolute cTnI results due to a lack of mass standardization and heterogeneity in the cross-reactivities of antibodies to various troponin I forms.

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Allergenic Characterization of Tropomyosin from the Dusky Brown Cockroach, Periplaneta fuliginosa

Clinical and Diagnostic Laboratory Immunology ◽

10.1128/cdli.11.4.680-685.2004 ◽

2004 ◽

Vol 11 (4) ◽

pp. 680-685 ◽

Cited By ~ 12

Author(s):

Kyoung Yong Jeong ◽

Heeyu Hwang ◽

Jongweon Lee ◽

In-Yong Lee ◽

Dong Soo Kim ◽

...

Keyword(s):

Recombinant Protein ◽

Periplaneta Americana ◽

Immunoglobulin E ◽

Expression System ◽

Specific Ige ◽

Cross Reactivity ◽

Enzyme Linked Immunosorbent Assay ◽

Inhibitor Concentration ◽

The Cross ◽

Elisa Inhibition

ABSTRACTHousehold arthropods are one of the most common causes of allergic diseases. Four species of cockroaches are found to reside in Korean homes, but published work deals almost exclusively with the German and American cockroaches. This study was undertaken to investigate the cross-reactive allergenic components of the dusky brown cockroach,Periplaneta fuliginosa. Enzyme-linked immunosorbent assay (ELISA) inhibition and immunoblot analyses for the dusky brown cockroach were performed withBlattella germanicaandDermatophagoides farinaeallergic sera. cDNA encoding tropomyosin, which is a well known cross-reactive pan-allergen, was cloned by reverse transcriptase PCR, and recombinant protein was produced by using a pET-28b expression system. Native tropomyosin was purified by ammonium sulfate fractionation and electroelution. The immunoglobulin E (IgE) reactivities of native and recombinant tropomyosins were compared by an ELISA inhibition study. All 30 sera tested showedP. fuliginosa-specific IgE, and the IgE-binding reactivity of theP. fuliginosaextract was inhibited as much as 79.4% by aB. germanicaextract and as much as 63.3% by aD. farinaeextract. The deduced amino acid sequence of cloned cDNA was identical with that ofPeriplaneta americanatropomyosin (98.5% nucleotide sequence identity). Seven of 26 (26.9%) allergic sera had IgE specific for recombinant protein, and the maximum inhibition ofP. fuliginosa-specific IgE achieved with recombinant tropomyosin was 37.7% at an inhibitor concentration of 10 μg/ml. Native tropomyosin inhibited the binding of IgE to theP. fuliginosa,B. germanica, andD. farinaeextracts by 65.0, 51.8, and 39% at an inhibitor concentration of 1 μg/ml.P. fuliginosaappears to possess allergens that are highly cross-reactive with allergens ofB. germanicaandD. farinae. Tropomyosin was found to be a major allergenic component accounting for the cross-reactivity between cockroaches and dust mites.

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