Rebecca A Marsh, Jack J Bleesing, Samuel Cern Cher Chiang
{"title":"Diagnostic testing for hemophagocytic lymphohistiocytosis.","authors":"Rebecca A Marsh, Jack J Bleesing, Samuel Cern Cher Chiang","doi":"10.1016/j.jim.2025.113816","DOIUrl":"10.1016/j.jim.2025.113816","url":null,"abstract":"<p><p>Hemophagocytic lymphohistiocytosis (HLH) is a rare clinical syndrome caused by severe systemic hyperinflammation. HLH can be rapidly fatal if unrecognized or inadequately treated. It is important that clinicians are able to utilize diagnostic testing to assess for HLH and determine the underlying causes including possible inborn errors of immunity (IEI). This article summarizes many of the tools available to aid with the diagnostic evaluation of patients with possible HLH and underlying IEI.</p>","PeriodicalId":16000,"journal":{"name":"Journal of immunological methods","volume":" ","pages":"113816"},"PeriodicalIF":1.6,"publicationDate":"2025-01-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143039295","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Phospho-flow cytometry assays for diagnostic use - A discussion of assay utility and assay development and validation challenges.","authors":"Vijaya Knight","doi":"10.1016/j.jim.2025.113818","DOIUrl":"https://doi.org/10.1016/j.jim.2025.113818","url":null,"abstract":"<p><p>Detection of changes in phosphorylation of cell signaling molecules using flow cytometry is termed \"phosphoflow\" or \"phospho-flow cytometry\". Phosphoflow has wide application for basic research into the mechanics of cell signaling, for evaluating aberrant signaling in cancerous cells and tissues, for studying efficacy or off-target effects during drug and vaccine development, and for functional assessment of pathogenic variants of genes that are known to play a role in development or function of the immune system. Phosphoflow has not been widely adopted in clinical laboratories owing to the challenges with developing and validating robust assays consistent with clinical laboratory regulatory standards. This review provides a brief overview of the utility of phosphoflow and points of consideration for development and validation of phosphoflow assays for diagnostic use, with a focus on inborn errors of immunity.</p>","PeriodicalId":16000,"journal":{"name":"Journal of immunological methods","volume":" ","pages":"113818"},"PeriodicalIF":1.6,"publicationDate":"2025-01-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143039301","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Yana Zabrodskaya , Konstantin Sivak , Maria Sergeeva , Andrey Aleksandrov , Elena Kalinina , Aleksandr Taraskin , Mikhail Eropkin , Elena Eropkina , Vladimir Egorov
{"title":"Peptide fibrils as a vaccine: Proof of concept","authors":"Yana Zabrodskaya , Konstantin Sivak , Maria Sergeeva , Andrey Aleksandrov , Elena Kalinina , Aleksandr Taraskin , Mikhail Eropkin , Elena Eropkina , Vladimir Egorov","doi":"10.1016/j.jim.2025.113811","DOIUrl":"10.1016/j.jim.2025.113811","url":null,"abstract":"<div><h3>Background</h3><div>Rapid vaccine platforms development is crucial for responding to epidemics and pandemics of emerging infectious diseases, such as Ebola. This study explores the potential of peptide vaccines that self-organize into amyloid-like fibrils, aiming to enhance immunogenicity while considering safety and cross-reactivity.</div></div><div><h3>Methods</h3><div>We synthesized two peptides, G33 and G31, corresponding to a segment of the Ebola virus GP2 protein, with G33 known to form amyloid-like fibrils. Their toxicity was assessed in vitro using an MTT assay on MDCK and A549 cell cultures. For in vivo studies, balb/c mice were immunized with these peptides. Immunogenicity was gauged by ELISA for specific antibodies against the recombinant eGP protein. Hematological parameters were determined, and histopathological changes in organs were documented post-euthanasia.</div></div><div><h3>Results</h3><div>Both peptides exhibited no cytotoxicity up to 500 μg/mL. G33-immunized mice developed higher antibody titers than those receiving G31 or control, without significant alterations in hematological profiles. However, histological analysis showed periportal infiltration and lymphoid-macrophage clusters in the liver and kidneys, suggesting immune response activation. The homology between the G33 peptide and mammalian proteins poses risks of cross-reactivity.</div></div><div><h3>Conclusion</h3><div>The amyloid-like fibrils formed by the G33 peptide elicited a stronger immune response without significant hematological changes, underlining the feasibility of fibril-based peptide vaccines. However, the potential for autoimmune responses due to molecular mimicry warrants further investigation before clinical applications can be considered.</div></div>","PeriodicalId":16000,"journal":{"name":"Journal of immunological methods","volume":"538 ","pages":"Article 113811"},"PeriodicalIF":1.6,"publicationDate":"2025-01-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143006747","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Expression of bluetongue virus full-length VP7 protein in insect cells and its diagnostic utility for detection of antibodies to the virus infection","authors":"Sanchay Kumar Biswas , Madhusudan Hosamani , Karam Chand , Ankita Chauhan , Kurat Ul Ain , Vanitha Selvarajan , Sushmita Nautiyal , Muzamil Bashir , Divakar Hemadri , Gaurav Kumar Sharma , B.P. Sreenivasa","doi":"10.1016/j.jim.2025.113801","DOIUrl":"10.1016/j.jim.2025.113801","url":null,"abstract":"<div><div>Bluetongue (BT) is a vector-borne viral disease of multiple domestic and wild ruminants across the globe. The VP7 protein of bluetongue virus (BTV) is the major immune-dominant structural protein that is conserved across the BTV serotypes and therefore, targeted for the development of immuno-diagnostics for BT. In this study, full-length recombinant VP7 protein (rVP7) of BTV-1 was expressed in <em>Trochoplusia ni</em> derived insect cells (Tn5) using codon-optimized synthetic gene construct through baculovirus expression system. The seed stock of recombinant baculovirus was amplified to a high titre (>1 × 10<sup>8</sup> pfu/ml) at P2 and P3 in sf9 cells. The rVP7 was successfully produced and purified from infected Tn5 culture lysate for evaluation of the immuno-reactivity and its diagnostic potential. The purified protein showed strong reactivity in western blot analysis with the polyclonal immune serum produced against BTV core antigen in guinea pigs. An indirect ELISA (iELISA) was optimized by using the purified rVP7 for the detection of the group-specific antibodies to BTV in sheep and goats. The iELISA was found to be highly sensitive (98.9 %), specific (98.1 %), and reproducible (CV < 10 %) for detection of the antibodies to BTV in sheep and goat serum. The iELISA could detect the specific antibodies in naturally infected goat serum containing type-specific neutralizing antibodies to different BTV serotypes indicating the potential of the rVP7 for the development of the group-specific sero-diagnostics for BT.</div></div>","PeriodicalId":16000,"journal":{"name":"Journal of immunological methods","volume":"538 ","pages":"Article 113801"},"PeriodicalIF":1.6,"publicationDate":"2025-01-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143006745","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Thomas Egger , Tamara Dörr , Reto Thoma , Susanne Nigg , Lorenz Risch , Alessio Cremonesi , Pietro Vernazza , Philipp Kohler , Christian R. Kahlert
{"title":"Evaluation of self-collected dried blood spots for detection of SARS-CoV-2 nucleocapsid antibodies shows low sensitivity","authors":"Thomas Egger , Tamara Dörr , Reto Thoma , Susanne Nigg , Lorenz Risch , Alessio Cremonesi , Pietro Vernazza , Philipp Kohler , Christian R. Kahlert","doi":"10.1016/j.jim.2024.113800","DOIUrl":"10.1016/j.jim.2024.113800","url":null,"abstract":"<div><h3>Background and aims</h3><div>Dried blood spots (DBS) have been proposed as a cost-effective surveillance method for population-wide screening of SARS-CoV-2 immunity but sensitivity of DBS based on self-collected DBS samples is unknown. To evaluate the success of vaccination strategies, it is necessary to differentiate vaccination from natural infection. Therefore, a test for antibodies against the viral nucleocapsid protein (anti-N) is desirable.</div></div><div><h3>Materials and methods</h3><div>In our prospectively followed cohort of healthcare workers (HCW) in eastern Switzerland, we assessed SARS-CoV-2-anti-N-seroprevalence using DBS on a biweekly basis from March to September 2020. Phlebotomy samples were collected in March and September and tested for anti-N-seropositivity, as well as SARS-CoV-2 spike antibodies for quantitative validation. Venous antibody testing was compared with DBS results for anti-N using the Roche Elecsys electro-chemiluminescence immunoassay.</div></div><div><h3>Results</h3><div>792 HCW (median age 38.3 years) were included, 35 (4.4 %) were SARS-CoV-2-anti-N-seropositive. Of 43 matching DBS, 25 tested positive for anti-N, accounting for a sensitivity of 58.1 % (95 %CI 43.3–71.6 %). We found a significant correlation of anti-N from DBS with results from phlebotomy samples (<em>r</em> = 0.77;<em>p</em> < 0.0001), with higher levels being associated with a higher true-positive rate. Anti-N in DBS correlated significantly with quantitatively validated anti-S obtained from serum (<em>r</em> = 0.67;<em>p</em> < 0.0001).</div></div><div><h3>Conclusion</h3><div>Although home DBS collection was feasible in a larger cohort and we found a high correlation between anti-N detection in DBS and phlebotomy samples, the sensitivity of self-collected DBS samples was significantly impaired for the Roche Elecsys anti-N assay. Therefore, we cannot recommend this method for DBS when testing from venous blood is possible.</div></div>","PeriodicalId":16000,"journal":{"name":"Journal of immunological methods","volume":"536 ","pages":"Article 113800"},"PeriodicalIF":1.6,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142950012","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Adaptation of the in vivo respiratory burst assay for fathead minnow larvae (Pimephales promelas)","authors":"Nicole Kooij, Tisha C. King-Heiden","doi":"10.1016/j.jim.2024.113797","DOIUrl":"10.1016/j.jim.2024.113797","url":null,"abstract":"<div><div>Initial innate immune responses such as the respiratory burst response of phagocytes present the first line of defense in response to exposure to pathogens. Several respiratory burst assays have been developed in mammals, cell cultures, and whole zebrafish embryos as a reliable indicator of the innate immune response of a host, and these assays are being used to screen various environmental contaminants for their immunotoxic potential. While zebrafish are a common laboratory fish used in toxicology studies geared towards human health effects, fathead minnows are commonly used as an ecotoxicological indicator species for North America. In this technical note, we describe how we adapted the zebrafish <em>in vivo</em> respiratory burst assay for use in fathead minnow larvae. This assay provides promising expansion of using <em>in vivo</em> respiratory burst responses in different species of larval fish for future comparative immunotoxicity assays, as well as laying the groundwork for studies that can better define the development of the innate and adaptive immune responses of fathead minnow larvae.</div></div>","PeriodicalId":16000,"journal":{"name":"Journal of immunological methods","volume":"536 ","pages":"Article 113797"},"PeriodicalIF":1.6,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142854332","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Natural cross-reactive anti-SARS-CoV-2 antibodies in avian egg yolk","authors":"Gholamreza Nikbakht Brujeni, Pouya Houshmand, Shervin Sadafian, Reza Rezaei","doi":"10.1016/j.jim.2024.113798","DOIUrl":"10.1016/j.jim.2024.113798","url":null,"abstract":"<div><div>Since the beginning of the 21st century, the <em>Coronaviridiae</em> family has caused several life-threatening outbreaks in the world. The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), which is the cause of the latest <em>Coronaviridiae</em>-related outbreak, is still a major health issue worldwide. Prevention, diagnosis, and therapeutic actions are the most important strategies to mitigate the spread of the COVID-19 pandemic. Among therapeutics, specific antibodies play a crucial role in controlling the symptoms of patients and preventing others from becoming infected. Here, we have introduced the avian egg yolk as a natural source of cross-reactive anti-SARS-CoV-2 immunoglobulin Y. ELISA, dot blot and western blot were used to identify natural anti-SARS-CoV-2 IgY in the egg yolk of different species of birds. Also, bioinformatics analysis was performed to investigate the possible causes of the presence of these natural antibodies in the egg yolks. The results of blotting and ELISA assays demonstrated that the egg yolk-derived antibodies could identify and bind to the different subunits of SARS-CoV-2. Substantial concentrations of neutralizing antibodies against SARS-CoV-2 were also detected in the egg yolk. In addition, bioinformatics analysis showed structural similarities between the components of infectious bronchitis virus, SARS-CoV-2, and other members of the <em>Coronaviridiae</em> family. It seems that egg yolk can be used as a natural, inexpensive, and accessible source of anti-SARS-CoV-2 antibodies. Diverse diagnostic and therapeutic potentials for avian egg yolk-derived anti-SARS-CoV-2 antibodies are imagined.</div></div>","PeriodicalId":16000,"journal":{"name":"Journal of immunological methods","volume":"536 ","pages":"Article 113798"},"PeriodicalIF":1.6,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142846882","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Qingmei Li , Ge Li , Xun Wang , Ruining Wang , Jifei Yang , Junqing Guo , Gaiping Zhang
{"title":"Identification of the linear Fc-binding epitope on the bovine IgG1 Fc receptor of (boFcγRI) using synthetic peptides","authors":"Qingmei Li , Ge Li , Xun Wang , Ruining Wang , Jifei Yang , Junqing Guo , Gaiping Zhang","doi":"10.1016/j.jim.2024.113799","DOIUrl":"10.1016/j.jim.2024.113799","url":null,"abstract":"<div><h3>Background</h3><div>Bovine IgG1 Fc receptor (boFcγRI) is a homologue to human FcγRI (CD64) that has three extracellular Ig-like domains and can bind bovine IgG1 with high affinity. Identification of the linear epitope for Fc-binding on boFcγRI provides new insights for the IgG-Fcγ interaction and FcγR-targeting drugs development.</div></div><div><h3>Methods</h3><div>The boFcγRI molecules were expressed on cell surface of the boFcγRI -transfected COS-7 cells. The extracellular domain of boFcγRI was expressed in <em>Escherichia coli</em> (<em>E. coli</em>) BL21, and the soluble boFcγRI was purified by Ni-chelation chromatography followed by refolding. To identify the Fc-binding epitope on the boFcγRI, peptides derived from the membrane-distal extracellular domain (EC2) of boFcγRI were synthesized and conjugated to a carrier protein of IgG-free bovine serum albumin (BSA). Binding of bovine IgG1 to the different peptides was tested by Dot-blot assay, and the peptide showing maximal IgG-binding was further modified by truncation and mutation. The inhibition effect of the Fc-binding peptide was determined by competitive ELISA and Fc-rosetting inhibition assay, respectively.</div></div><div><h3>Results</h3><div>The minimal effective peptide TNLSHNGI corresponding to the sequence 142–149 of boFcγRI was found to bind bovine IgG1 specifically in Dot-blot suggesting it represents a linear ligand-binding epitope located in the putative E-F loop of the EC2 domain on the receptor. Mutation analysis of the peptide showed that the residues of Thr<sup>142</sup>, Asn<sup>143</sup>, Leu<sup>144</sup>, Gly<sup>148</sup> and Ile<sup>149</sup> within the linear epitope are critical for IgG1-binding. The Fc-binding peptide inhibited bovine IgG1 binding to the soluble recombinant protein of boFcγRII with IC<sub>50</sub> of 20.27 μmol/L, and inhibited the rosette formation of bovine IgG1-sensitized RBCs on the boFcγRI transfected cells with IC<sub>50</sub> of 86.75 μmol/L.</div></div><div><h3>Conclusions</h3><div>The linear epitope for Fc-binding as well as its crucial residues of EC2 domain on boFcγRI was identified using synthetic peptides. The Fc-binding peptide showed well capability of regulating boFcγRI-IgG1 interaction on cell surface.</div></div>","PeriodicalId":16000,"journal":{"name":"Journal of immunological methods","volume":"536 ","pages":"Article 113799"},"PeriodicalIF":1.6,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142921958","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Luisa Massai , Martina Carducci , Luca Rovetini , Aimee Paterson , Alana Whitcombe , Reuben McGregor , Natalie Lorenz , Alexander J. Keeley , Thushan I. de Silva , Julie Bennett , Francesco Berlanda Scorza , Miren Iturriza , Nicole J. Moreland , Danilo G. Moriel , Omar Rossi
{"title":"Characterization of an IL-8 cleavage inhibition assay to determine the functionality of anti-SpyCEP antibodies in human sera","authors":"Luisa Massai , Martina Carducci , Luca Rovetini , Aimee Paterson , Alana Whitcombe , Reuben McGregor , Natalie Lorenz , Alexander J. Keeley , Thushan I. de Silva , Julie Bennett , Francesco Berlanda Scorza , Miren Iturriza , Nicole J. Moreland , Danilo G. Moriel , Omar Rossi","doi":"10.1016/j.jim.2024.113786","DOIUrl":"10.1016/j.jim.2024.113786","url":null,"abstract":"<div><div>Exposure to Group A Streptococcus leads to a broad spectrum of disease and sequelae, as the bacterium employs a wide range of virulence factors to facilitate colonization of the host, propagation and onward transmission, disrupting both innate and adaptive immune responses. The protease SpyCEP has a crucial role in contributing to bacterial immune evasion by impairing neutrophil recruitment and killing of bacteria through the cleavage of interleukin-8 (IL-8). Given this critical function, SpyCEP represents a key vaccine antigen and quantifying functional anti-SpyCEP antibodies represents not only an important marker of vaccine efficacy, but also a tool to dissect the natural immune response. Here, we report the development and characterization of an IL-8 cleavage inhibition assay to measure the function of anti-SpyCEP antibodies in human sera. The assay was demonstrated to be sensitive, highly specific, linear and reproducible, and suitable for evaluating the function of anti-SpyCEP antibodies induced in humans in vaccine clinical trials and in observational studies of natural immunity.</div></div>","PeriodicalId":16000,"journal":{"name":"Journal of immunological methods","volume":"536 ","pages":"Article 113786"},"PeriodicalIF":1.6,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142791979","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Antonio C.G. Foddai , Peter Wilhelmsson , Per-Eric Lindgren , Jeremy M. Sternberg , Alan S. Bowman
{"title":"A novel panel of peptides with diagnostic potential for serological identification of Borrelia burgdorferi sensu stricto, B. garinii and B. afzelii in human sera","authors":"Antonio C.G. Foddai , Peter Wilhelmsson , Per-Eric Lindgren , Jeremy M. Sternberg , Alan S. Bowman","doi":"10.1016/j.jim.2025.113802","DOIUrl":"10.1016/j.jim.2025.113802","url":null,"abstract":"<div><div>A novel panel of peptide for serological identification of <em>Borrelia burgdoferi</em> sensu stricto, <em>Borrelia garinii</em> and <em>Borrelia afzelii</em> was developed and assessed in this study. The diagnostic algorithm of the novel test was initially trained testing 10 US human sera including 3 early-stage and 3 late-stage Lyme disease positive sera, 2 sera positive for Babesia and 2 sera positive for Syphilis, all purchased from a private biorepository. Findings were then corroborated testing (a) 33 additional EU follow-up positive sera from seroconverted patients bitten by ticks that tested positive for <em>B. burgdorferi</em> sensu stricto (No 2), <em>Borrelia garinii</em> (No 14), <em>Borrelia afzelii</em> (No 15) <em>Borrelia valaisiana</em> (No 2), and (b) 40 negative sera from US healthy donors. Results of preliminary US sera testing showed successful detection of IgM and IgG antibodies and correct identification of <em>Borrelia burgdorferi</em> sensu stricto in all the samples tested. Analysis of EU follow-up sera showed much higher sensitivity and accuracy when IgM and IgG were tested combined together rather than separately. Sensitivity and accuracy in species identification of the anti-IgM + IgG multiplex peptide ELISA was 93.5 % and 96.5 % respectively; lower test performance was observed when IgM (i.e. sensitivity = 58.1 %; correct identification = 88.8 %) and IgG testing (i.e. sensitivity = 74.1 %; correct identification = 96.5 %) were carried out separately. Overall specificity of the anti-IgM, anti-IgG and anti-IgM + IgG multiplex peptide ELISA calculated on a total number of 46 negative sera included in this study was 91.3 %, 95.6 and 93.4 %, respectively.</div></div>","PeriodicalId":16000,"journal":{"name":"Journal of immunological methods","volume":"536 ","pages":"Article 113802"},"PeriodicalIF":1.6,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142965567","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}