K. Bentum, R. Folitse, E. Amemor, V. Burimuah, T. Opoku-Agyemang, B. Emikpe
{"title":"Seroprevalence of Toxoplasma Gondii antibodies in sheep and goats slaughtered at the Kumasi Abattoir, Ghana","authors":"K. Bentum, R. Folitse, E. Amemor, V. Burimuah, T. Opoku-Agyemang, B. Emikpe","doi":"10.1080/15321819.2019.1642916","DOIUrl":"https://doi.org/10.1080/15321819.2019.1642916","url":null,"abstract":"ABSTRACT Toxoplasmosis, caused by T. gondii, is an important zoonosis worldwide. In Ghana, information on the disease in humans abounds but scanty in animals. This study was therefore conducted to estimate the seroprevalence of T. gondii infection sheep and goats sampled from the Kumasi Abattoir in Ashanti Region, Ghana. A total of 347 serum samples collected from 170 sheep and 177 goats were analyzed for the presence of T. gondii antibodies using a commercial ELISA kit. Results of this study estimated the seroprevalence of 23.7% in goats an, 35.9% in sheep. In sheep, 24 (35.82%) out of a total of 67 male samples were positive and 37 (35.92%) out of a total of 104 female samples were positive while in goats, 6 (8.2%) bucks out of a total of 73 were positive while 36 (34.6%) does out of a total of 104 were positive. There was a significant difference in the rate of seropositivity of female goats (p-value 0.01). This study confirms the existence of T. gondii infection in small ruminants in Ghana and it showed that sheep and dogs are more at risk to T. gondii infection hence meat from such animals could be a potential risk to public health if consumed raw or undercooked.","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"25 1","pages":"495 - 501"},"PeriodicalIF":0.0,"publicationDate":"2019-07-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86843441","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
A. Rodríguez-Rodríguez, J. Egea-Guerrero, Á. Vilches-Arenas, Manuel Jesús Quintanilla-Vázquez, F. Murillo-Cabezas, M. Muñoz-Sanchez
{"title":"Comparison of two competitive enzyme immunoassay kits for quantification of plasma Urotensin-II in rats","authors":"A. Rodríguez-Rodríguez, J. Egea-Guerrero, Á. Vilches-Arenas, Manuel Jesús Quintanilla-Vázquez, F. Murillo-Cabezas, M. Muñoz-Sanchez","doi":"10.1080/15321819.2016.1250772","DOIUrl":"https://doi.org/10.1080/15321819.2016.1250772","url":null,"abstract":"ABSTRACT Changes in Urotensin-II (U-II) concentration, a potent vasoconstrictor peptide, have been detected in various pathologies, but it has been impossible to define a normality range. We aimed to analyze the concordance and interchangeability between two enzyme immunoassay methods developed by Phoenix Pharmaceuticals, Inc. to measure U-II plasma concentration in rats: ELISA and fluorescent EIA. Assays resulted positively correlated (r = 0.850; p < 0.01). There was a significant difference between assays values (p < 0.001). The analysis of agreement (Bland and Altman plot) stated that the mean of the differences was 2.055 (SD ± 0.588). Hence, we concluded that the two U-II assays were correlated but not interchangeable.","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"47 1","pages":"247 - 256"},"PeriodicalIF":0.0,"publicationDate":"2017-05-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86036175","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
B. Jain, J. Kumarasamy, C. Gholve, S. Kulkarni, M. Rajan
{"title":"A multi-analyte immunoassay for thyroid related analytes","authors":"B. Jain, J. Kumarasamy, C. Gholve, S. Kulkarni, M. Rajan","doi":"10.1080/15321819.2016.1250771","DOIUrl":"https://doi.org/10.1080/15321819.2016.1250771","url":null,"abstract":"ABSTRACT We describe the development and validation of multianalyte immunoassays (MAIA) for three analytes, viz., thyroxine (T4), thyroid stimulating hormone (TSH), and thyroglobulin (Tg) essential for assessment of thyroid function but having widely varying molecular weights. Using polycarbonate (PC) track-etched membranes (TEM) as an immobilization support and 125I as the tracer, both competitive assay for T4 and non-competitive assay for TSH and Tg were performed on the same TEM. MAIA was found to be highly sensitive and precise with clinically useful working range and correlated very well with individual analyte immunoassays. While we have demonstrated this assay format with radiotracer, it can be used with non-isotopic tracers equally well.","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"18 1","pages":"271 - 284"},"PeriodicalIF":0.0,"publicationDate":"2017-05-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74437205","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Maysam Mard-Soltani, M. Rasaee, A. Sheikhi, M. Hedayati
{"title":"Eliciting an antibody response against a recombinant TSH containing fusion protein","authors":"Maysam Mard-Soltani, M. Rasaee, A. Sheikhi, M. Hedayati","doi":"10.1080/15321819.2016.1250774","DOIUrl":"https://doi.org/10.1080/15321819.2016.1250774","url":null,"abstract":"ABSTRACT Designing novel antigens to rise specific antibodies for Thyroid Stimulating Hormone (TSH) detection is of great significance. A novel fusion protein consisting of the C termini sequence of TSH beta subunit and a fusion sequence was designed and produced for rabbit immunization. Thereafter, the produced antibodies were purified and characterized for TSH detection. Our results indicate that the produced antibody is capable of sensitive and specific detection of TSH with low cross reactivity. This study underscores the applicability of designed fusion protein for specific and sensitive polyclonal antibody production and the importance of selecting an amenable region of the TSH for immunization.","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"13 1","pages":"257 - 270"},"PeriodicalIF":0.0,"publicationDate":"2017-05-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90537121","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
A. Roșca, G. Anton, L. Ene, I. Iancu, A. Temereanca, C. Achim, S. Ruță
{"title":"Immunoassay and molecular methods to investigate DNA methylation changes in peripheral blood mononuclear cells in HIV infected patients on cART","authors":"A. Roșca, G. Anton, L. Ene, I. Iancu, A. Temereanca, C. Achim, S. Ruță","doi":"10.1080/15321819.2016.1260587","DOIUrl":"https://doi.org/10.1080/15321819.2016.1260587","url":null,"abstract":"ABSTRACT This study aimed to investigate the influence of antiretroviral therapy on methylation markers, in a group of HIV infected, heavily treated patients. Immune and molecular methods were used to investigate potential changes in methylation profile in DNA isolated from peripheral blood mononuclear cells collected from antiretroviral-experienced HIV infected patients and healthy controls. The percentage of 5-methylcytosine was inversely correlated with proviral DNA and active replication while DNMT1 (p = 0.01) and DNMT3A (p = 0.004) independently correlated with active viral replication. DNMT3A expression increased with total treatment duration (p = 0.03), number of antiretroviral drugs ever used (p = 0.003), and cumulative exposure to protease inhibitors (p = 0.02) even in currently HIV undetectable patients.","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"116 1","pages":"299 - 307"},"PeriodicalIF":0.0,"publicationDate":"2017-05-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89323965","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Measuring fecal testosterone metabolites in spotted hyenas: Choosing the wrong assay may lead to erroneous results","authors":"Susanne Pribbenow, T. G. Shrivastav, M. Dehnhard","doi":"10.1080/15321819.2016.1260584","DOIUrl":"https://doi.org/10.1080/15321819.2016.1260584","url":null,"abstract":"ABSTRACT Enzyme-immunoassays (EIA) that detect fecal testosterone metabolites (fTM) are powerful tools to monitor gonadal activity non-invasively. However, a challenge with testosterone EIAs might be their potential for cross-reactivities with structurally similar glucocorticoid metabolites. Therefore, we aimed to verify the capability of four different testosterone EIAs to monitor fTM without reflecting changes in adrenocortical activity in spotted hyenas by analyzing fecal samples following testosterone and ACTH challenge tests. We demonstrated that none of the testosterone EIAs is appropriate to measure fTM as all of them showed substantial cross-reactivities to unknown metabolites. Our study underlines the importance of validating androgen EIAs.","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"50 1","pages":"308 - 321"},"PeriodicalIF":0.0,"publicationDate":"2017-05-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89149967","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ahad Khalilnezhad, Elham Mahmoudian, N. Mosaffa, J. Mohsenifar, D. Amani
{"title":"Spontaneous mouse mammary tumor cell lysates induce IgG production in spleen mononuclear cells of healthy and tumor-bearing mice","authors":"Ahad Khalilnezhad, Elham Mahmoudian, N. Mosaffa, J. Mohsenifar, D. Amani","doi":"10.1080/15321819.2016.1266499","DOIUrl":"https://doi.org/10.1080/15321819.2016.1266499","url":null,"abstract":"ABSTRACT Background. We hypothesized that Tumor cell lysate (TCL) prepared from spontaneous mouse mammary tumor (SMMT) may elicit IgG production by spleen mononuclear cells (SMCs) in ex vivo. Methods. The SMCs from healthy mice (HM, n = 6) and four-week SMMT-bearing mice (TBM, n = 6) was cultured in presence of TCL and mitogen for 42 hr at 37°C, separately. Serum and SMCs culture supernatant levels of IFNγ, IL-4, and total IgG were measured using special ELISA kits. Results. Serum IgG level of TBM was significantly higher than that of HM group (P = 0.019), while serum IFNγ and IL-4 did not differ between two groups (P > 0.05). Mitogen significantly induced ex vivo production of both IFNγ (P = 0.013) and IL-4 (P = 0.015) by SMCs from HM group, and only IL-4 (P = 0.049) by SMCs from TBM group. In contrast, TCL increased ex vivo production of IgG by SMCs from both HM (P = 0.034) and TBM (P = 0.016) groups. The ex vivo IgG revealed a moderate positive correlation with tumor size (r = 0.578, P = 0.422). Conclusion. It seems that TCL prepared from SMMT are potent inducers of IgG production. This may propose TCL as a potential tool for monitoring of humoral immunity in animal models.","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"1 1","pages":"333 - 342"},"PeriodicalIF":0.0,"publicationDate":"2017-05-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82436208","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"C3:CH50 ratio as a proposed composite marker for eculizumab monitoring in atypical hemolytic uremic syndrome: Preliminary results","authors":"K. Kerboua, F. Haiba, D. Batouche","doi":"10.1080/15321819.2016.1234485","DOIUrl":"https://doi.org/10.1080/15321819.2016.1234485","url":null,"abstract":"ABSTRACT Treatment of atypical hemolytic uremic syndrome (aHUS) by the complement C5 inhibitor eculizumab (Soliris®) is highly effective but unfortunately, associated with an economic pressure on the health care systems even in high incomes countries. Despite spacing infusions having been proposed as the unique solution to minimize this economic impact, no reliable laboratory assays are available to tailor such therapy optimization. We aimed to propose and evaluate a complement composite marker for eculizumab efficacy monitoring in aHUS. We have retrospectively analyzed complement profiles data of eight aHUS patients under eculizumab from the International Registry of HUS/Thrombotic Thrombocytopenia Purpura, and calculated a novel marker “C3:CH50 ratio” by dividing C3 value by CH50 one for each sample during induction and maintenance periods. The results significance was compared to the currently used biomarkers for eculizumab tailoring. In contrast to the current biomarkers used for eculizumab efficacy monitoring like CH50 and soluble or deposit membrane attack complexes, “C3:CH50 ratio” seems to be the most interesting one since its value at pre-eculizumab dosage equaled 0.92 ± 0.2 while the post-eculizumab one increased significantly to reach 24.54 ± 10.7; P < 0.001. Furthermore, this ratio correlated negatively with platelets count (r = −0.722, P = 0.018) while no correlation was found within the thrombotic microangiopathy (TMA) biomarkers and complement blockade for the other parameters that change in pre and post-eculizumab therapy. As far as we know, this is the first study that suggests a post-eculizumab parameter correlating simultaneously with drug’s activity (complement inhibition) and disease activity (platelets counts). Nonetheless, the limited number of patients enrolled in this study should be considered in larger studies to guide eculizumab optimization by indicating the time when subsequent withdrawal or infusion spacing is allowed or recommended.","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"29 1","pages":"178 - 189"},"PeriodicalIF":0.0,"publicationDate":"2017-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73706426","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Elisa M. Castells Martínez, Ruben Del Valle, E. C. González, A. Melchor, P. L. Pérez, Idania González, A. Carr, K. Leon
{"title":"An enzyme immunoassay for determining epidermal growth factor (EGF) in human serum samples using an ultramicroanalytical system","authors":"Elisa M. Castells Martínez, Ruben Del Valle, E. C. González, A. Melchor, P. L. Pérez, Idania González, A. Carr, K. Leon","doi":"10.1080/15321819.2016.1236729","DOIUrl":"https://doi.org/10.1080/15321819.2016.1236729","url":null,"abstract":"ABSTRACT Human epidermal growth factor is a small peptide consisting of 53 amino acid residues, which stimulates cell proliferation and is associated with several human carcinomas. A simple sandwich-type ultramicroELISA assay (UMELISA), based on the advantages of high affinity reaction between streptavidin and biotin has been developed for the measurement of EGF in human serum samples. Strips coated with a high affinity monoclonal antibody directed against EGF are used as solid phase, to ensure the specificity of the assay. The EGF assay was completed in 18 hr, with a measuring range of 39–2500 pg/mL. The intra- and inter-assay coefficients of variation were 4.4–7.3% and 0–5.1%, respectively, depending on the EGF concentrations evaluated. Percentage recovery ranged from 96–104%. Regression analysis showed a good correlation with the commercially available Human EGF Immunoassay Quantikine® ELISA kit (n = 130, r = 0.92, P < 0.01). The analytical performance characteristics of our UMELISA EGF endorse its use for the quantification of EGF in human serum samples.","PeriodicalId":15987,"journal":{"name":"Journal of Immunoassay and Immunochemistry","volume":"1 1","pages":"190 - 201"},"PeriodicalIF":0.0,"publicationDate":"2017-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89948991","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}