Antibodies最新文献

{"title":"Conversion Factors to Compare Serum Concentrations of Anti-HBs, Anti-SARS-CoV-2 and Anti-Tetanus Toxin IgG.","authors":"Aurelia Knispel, Christian Jassoy","doi":"10.3390/antib14030069","DOIUrl":"10.3390/antib14030069","url":null,"abstract":"<p><p><b>Background</b>: The concentration of antigen-specific antibodies in serum is usually measured in international units/mL. Therefore, the actual concentration of virus-specific antibodies in sera is unknown. <b>Objectives</b>: The aim of the study was to determine conversion factors for concentrations of IgG against hepatitis B surface antigen (HBs), SARS-CoV-2 receptor binding domain (RBD) and nucleoprotein (NP) as well as tetanus toxin (Ttx) in serum and to compare antigen-specific IgG concentrations in serum samples. <b>Methods</b>: Absorption equivalence ELISAs were used to determine conversion factors for international units (IU) for anti-HBs, anti-SARS-CoV-2-RBD and NP and for anti-Ttx immunoglobulin G. The antigen-specific IgG concentrations in serum samples were then measured in units/mL and the ratio of IgG concentrations in the sera was determined using the conversion factors. <b>Results</b>: One IU of anti-HBs IgG corresponded to 24.4 BAU of anti-CoV-2 RBD IgG, 6.87 BAU of anti-CoV-2 NP and 14 mIU of anti-Ttx IgG. One BAU anti-SARS-CoV-2 NP-specific IgG is equivalent to 3.5 BAU SARS-CoV-2 RBD-specific IgG. Conversion of international units showed that median serum anti-Ttx-IgG concentrations were 50 times higher and anti-CoV-2-RBD-IgG concentrations were 390 times higher than median anti-HBs-IgG concentrations. In addition, after SARS-CoV-2 infection, the concentration of NP-specific IgG in serum was generally higher than that of RBD-specific IgG. <b>Conclusions</b>: The study provides conversion factors for serum concentrations of IgG against HBs, SARS-CoV-2 RBD and NP, as well as Ttx-IgG. This offers new insights into serum IgG concentrations and allows conclusions to be drawn about plasma cell pools.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-08-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12371921/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144940153","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A 3D Surface Plot for the Effective Visualization of Specific Serum Antibody Binding Properties.","authors":"József Prechl, Ágnes Kovács, Krisztián Papp, Zoltán Hérincs, Tamás Pfeil","doi":"10.3390/antib14030068","DOIUrl":"10.3390/antib14030068","url":null,"abstract":"<p><strong>Background: </strong>When an antigen molecule is exposed to serum, many different kinds of antibodies bind to it. The complexity of these binding events is only poorly characterized by assays that generate a single variable, generally reflecting the fractional saturation of the antigen, as the readout.</p><p><strong>Methods: </strong>We have previously devised an assay that delivers the essential biochemical variables to determine fractional saturation as the output: an equilibrium dissociation constant for affinity, the ratio of antibody concentration to the equilibrium constant and the concentration of bound antibodies under reference conditions. Here we propose a visualization method for the practical and informative display of these variables.</p><p><strong>Results: </strong>Using total antigen concentration and free and bound antibody concentration as coordinates in a three-dimensional space, a surface plot can depict the behavior of serum antibodies in the measurement range and identify the values of the key variables of binding activity. This surface display (antibody binding in 3-concentration display, Ab3cD) was used for the characterization of antibody binding to the SARS-CoV-2 spike protein in seronegative and seropositive sera. We demonstrate that this visualization scheme is suitable for presenting both individual and group differences and that epitope density changes, not commonly measured by immunoassays, are also revealed by the method.</p><p><strong>Conclusions: </strong>We recommend the use of 3D visualization whenever detailed, informative and characteristic differences in serum antibody reactivity are studied.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-08-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12372043/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144940158","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comparative Molecular Dynamics Study of 19 Bovine Antibodies with Ultralong CDR H3.","authors":"Olena Denysenko, Anselm H C Horn, Heinrich Sticht","doi":"10.3390/antib14030070","DOIUrl":"10.3390/antib14030070","url":null,"abstract":"<p><p><b>Background/Objectives</b>: Cows produce antibodies with ultralong CDRH3 segments (ulCABs) that contain a disulfide-stabilized knob domain. This domain is connected to the globular core of the antibody by a β-strand stalk. In the crystal structures, the stalk protrudes from the core in an extended conformation and presents the knob at its distal end. However, the rigidity of this topology has been questioned due to the extensive crystal packing present in most ulCAB crystal structures. To gain more insight into the dynamics of ultralong CDRH3s, we performed a comparative molecular dynamics (MD) study of 19 unique ulCABs. <b>Methods</b>: For all 19 systems, one-microsecond MD simulations were performed in explicit solvent. The analyses included an investigation of the systems' conformational stability and the dynamics of the knob domain as well as an energetic analysis of the intramolecular knob interactions. <b>Results</b>: The simulations show that the extended stalk-knob conformation observed in the crystal structures is not preserved in solution. There are significant differences in the degree of knob dynamics, the orientations of the knobs, the number of flexible stalk residues, and the frequency of the motions. Furthermore, interactions between the knob and the light chain (LC) of the ulCABs were observed in about half of the systems. <b>Conclusions</b>: The study reveals that pronounced knob dynamics is a general feature of ulCABs rather than an exception. The magnitude of knob motions depends on the system, thus reflecting the high sequence diversity of the CDRH3s in ulCABs. The observed knob-LC interactions might play a role in stabilizing distinct knob orientations. The MD simulations of ulCABs could also help to identify suitable knob fragments as mini-antibodies by suggesting appropriate truncation points based on flexible sites in the stalks.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-08-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12371982/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144940163","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A Cancer-Specific Anti-Podocalyxin Monoclonal Antibody (humPcMab-60) Demonstrated Antitumor Efficacy in Pancreatic and Colorectal Cancer Xenograft Models.","authors":"Hiroyuki Suzuki, Tomokazu Ohishi, Takuro Nakamura, Miyuki Yanaka, Saori Handa, Tomohiro Tanaka, Mika K Kaneko, Yukinari Kato","doi":"10.3390/antib14030067","DOIUrl":"10.3390/antib14030067","url":null,"abstract":"<p><p><b>Background</b>: Podocalyxin (PODXL) has been identified as a promising therapeutic target and a potential diagnostic biomarker in various tumors. Despite the therapeutic potential of anti-PODXL monoclonal antibodies (mAbs), their further development has been limited by concerns regarding potential on-target off-tumor toxicities. To minimize adverse effects on normal tissues, developing a cancer-specific mAb (CasMab) against PODXL is essential. <b>Methods</b>: Our group established a cancer-specific anti-PODXL mAb, PcMab-60 (IgM, κ), through the screening of over one hundred hybridoma clones. In this study, PcMab-60 was engineered into a humanized IgG₁-type mAb (humPcMab-60), and its antitumor activity was examined using mouse xenograft models of pancreatic ductal adenocarcinoma (PDAC) and colorectal cancer. <b>Results</b>: HumPcMab-60 retains cancer-specific reactivity; humPcMab-60 reacted to PDAC cell lines (PK-45H and MIA PaCa-2) and the colorectal cancer cell line (Caco-2), but not to a normal lymphatic endothelial cell line in flow cytometry. Furthermore, humPcMab-60 exerted antibody-dependent cellular cytotoxicity and complement-dependent cytotoxicity against PODXL-expressing cell lines and showed antitumor effects against the tumor xenografts. <b>Conclusions</b>: A humanized anti-PODXL CasMab, humPcMab-60, could be a promising mAb-based tumor therapy.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-08-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12372045/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144940137","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Antibodies to Laminin β4 in Pemphigoid Diseases: Clinical-Laboratory Experience of a Single Central European Reference Centre.","authors":"Maciej Marek Spałek, Magdalena Jałowska, Natalia Welc, Monika Bowszyc-Dmochowska, Takashi Hashimoto, Justyna Gornowicz-Porowska, Marian Dmochowski","doi":"10.3390/antib14030066","DOIUrl":"10.3390/antib14030066","url":null,"abstract":"<p><p><b>Background/Objectives:</b> Anti-p200 pemphigoid is a rare and likely underdiagnosed autoimmune blistering disorder. Laminin γ1 and laminin β4 have been implicated as potential target antigens in its pathogenesis. Recently, a novel indirect immunofluorescence assay targeting anti-laminin β4 antibodies has been developed, demonstrating high sensitivity and specificity, and offering a valuable tool for improved diagnosis. <b>Methods:</b> Of the 451 patients, 21 were selected for further laboratory analysis based on medical records. Sera from 10 patients, which showed a positive direct immunofluorescence (DIF) result and negative results in multiplex enzyme-linked immunosorbent assays (ELISAs) and/or mosaic six-parameter indirect immunofluorescence (IIF) for various autoimmune bullous diseases, were tested for the presence of anti-laminin β4 antibodies. Additionally, sera from 11 patients with positive DIF and positive ELISA for antibodies against BP180 and/or BP230 were analyzed. <b>Results:</b> Among the 10 patients with positive DIF and negative ELISA and/or mosaic six-parameter IIF, 6 sera were positive for anti-laminin β4 antibodies. These patients presented with atypical clinical features. In contrast, all 11 sera from patients with both positive DIF and positive ELISA for BP180 and/or BP230 were negative for anti-laminin β4 antibodies. <b>Conclusions:</b> In patients with a positive DIF result but negative ELISA and/or mosaic six-parameter IIF findings, testing for anti-laminin β4 antibodies should be considered. Furthermore, in cases presenting with atypical clinical features-such as acral distribution of lesions, intense pruritus, or erythematous-edematous plaques-the possibility of anti-p200 pemphigoid should be included in the differential diagnosis.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12371968/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144940150","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"FcRn Blockade as a Targeted Therapeutic Strategy in Antibody-Mediated Autoimmune Diseases: A Focus on Warm Autoimmune Hemolytic Anemia.","authors":"Michael Sandhu, Irina Murakhovskaya","doi":"10.3390/antib14030065","DOIUrl":"10.3390/antib14030065","url":null,"abstract":"<p><p>Antibody-mediated autoimmune diseases are common, can involve any organ system, and pose a large burden for patients and healthcare systems. Most antibody-mediated diseases are mediated by IgG antibodies. Selective targeting of pathogenic antibodies is an attractive treatment option which has already proven to be effective in antibody-positive generalized myasthenia gravis, maternal-fetal alloimmune cytopenias, and immune thrombocytopenic purpura. Warm autoimmune hemolytic anemia (wAIHA) is an autoimmune disorder mediated by pathogenic antibodies mainly of the IgG class with no approved therapy. Current treatment includes non-specific immunosuppression with corticosteroids, rituximab, and other immunosuppressive agents. With most therapies, time to response can be delayed and transfusions may be needed. Neonatal Fc receptor (FcRN) therapies provide rapid and sustained reduction of pathogenic IgG levels providing potential for fast, effective therapy in antibody-mediated autoimmune diseases including warm autoimmune hemolytic anemia. This review focuses on the emerging role of FcRn inhibition in autoimmune hematologic diseases, and their therapeutic potential in wAIHA.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12371984/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144940181","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Determination of the Epitopes of Alpha-Glucosidase Anti-Drug Antibodies in Pompe Disease Patient Plasma Samples.","authors":"Evgeniy V Petrotchenko, Andreas Hahn, Christoph H Borchers","doi":"10.3390/antib14030064","DOIUrl":"10.3390/antib14030064","url":null,"abstract":"<p><p>Pompe disease is a rare autosomal-recessive neuromuscular disorder caused by a deficiency of the lysosomal enzyme acid alpha-glucosidase (GAA), leading to the pathological accumulation of glycogen and impaired autophagy. Enzyme replacement therapy (ERT) with recombinant human alpha-glucosidase (rhGAA) has been available since 2006, but may lead to the formation of anti-drug antibodies (ADAs) against the recombinant human enzyme, which, in turn, may adversely affect the response to ERT. Knowledge of the antigenic determinants of rhGAA involved in interaction with ADAs may facilitate the development of strategies to attenuate the anti-drug immune response in patients. Here, we determined the rhGAA ADA epitopes in the plasma of Pompe disease patients using a series of affinity purifications combined with epitope extraction and label free quantitation LC-MS.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-07-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12371896/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144940088","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Anti-HMGCR-Antibody-Positive Statin-Induced Myositis: A Pilot Case Series on Treatment with Bempedoic Acid and Immunosuppressive Therapy.","authors":"Maurizio Benucci, Riccardo Terenzi, Francesca Li Gobbi, Emanuele Antonio Maria Cassarà, Tommaso Picchioni, Edda Russo, Barbara Lari, Mariangela Manfredi, Maria Infantino","doi":"10.3390/antib14030063","DOIUrl":"10.3390/antib14030063","url":null,"abstract":"<p><strong>Background/objectives: </strong>Immune-mediated necrotizing myopathy (IMNM) is a severe inflammatory myopathy marked by proximal muscle weakness, elevated creatine kinase (CK), and the presence of anti-HMGCR antibodies. Statin exposure is a recognized trigger for anti-HMGCR-positive IMNM, which may persist despite statin withdrawal. This pilot case series explores, for the first time, the use of bempedoic acid-a liver-specific lipid-lowering agent with minimal muscle toxicity-as an alternative to statins in these patients.</p><p><strong>Methods: </strong>We report 10 anti-HMGCR-antibody-positive IMNM patients (6 females, 4 males) previously on statins for primary prevention (8 on atorvastatin, 2 on simvastatin) without prior cardiovascular events. Statins were discontinued at myositis onset. All patients received prednisone and immunosuppressants (methotrexate in 7, mycophenolate in 3), plus bempedoic acid. Anti-HMGCR antibodies were measured using a chemiluminescence method.</p><p><strong>Results: </strong>Their mean anti-HMGCR antibody levels decreased significantly from 390.93 ± 275.22 to 220.89 ± 113.37 CU/L (<i>p</i> = 0.027) after 6 months of treatment. Their CK levels dropped from 1278.9 ± 769.39 to 315.1 ± 157.72 IU/L (<i>p</i> = 0.001), and aldolase dropped from 11.63 ± 2.18 to 6.61 ± 1.22 U/L (<i>p</i> = 0.0001). The mean LDL-C value was 96.1 ± 8.16 mg/dL. No disease recurrence was observed. Autoimmune panels were negative for other myositis-associated and/or -specific antibodies.</p><p><strong>Conclusions: </strong>Bempedoic acid appears to be a safe, effective, and cost-efficient lipid-lowering alternative in statin-intolerant IMNM patients. Larger studies are warranted to confirm its efficacy across different subgroups and to optimize dyslipidemia management in this setting.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-07-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12372103/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144940176","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mepolizumab-Related Blood Eosinophil Decreases Are Associated with Clinical Remission in Severe Asthmatic Patients: A Real-World Study.","authors":"Matteo Bonato, Francesca Savoia, Enrico Orzes, Elisabetta Favero, Gianenrico Senna, Micaela Romagnoli","doi":"10.3390/antib14030061","DOIUrl":"10.3390/antib14030061","url":null,"abstract":"<p><p><b>Background</b>: Mepolizumab is an effective treatment for severe eosinophilic asthma, leading to a depletion of blood eosinophil levels, the clinical relevance of which remains unclear. <b>Objective</b>: The aim of this study was to assess the relationship between mepolizumab-induced blood eosinophil reduction and clinical outcome in patients with severe eosinophilic asthma, in particular, whether the magnitude of blood eosinophil reduction was associated with clinical remission. <b>Methods</b>: We conducted a real-world retrospective analysis of 58 adult patients with severe eosinophilic asthma treated with mepolizumab. Clinical and respiratory functional parameters were evaluated at the start of mepolizumab treatment (T0) and after two years of treatment (T2; mean follow-up: 22.8 ± 7.5 months). Blood eosinophil counts were recorded at T0 and during the first year of treatment (T1; mean follow-up: 7.7 ± 4.1 months). <b>Results</b>: After two years of mepolizumab treatment, 58 severe asthmatic patients showed significant improvements in ACT score, FVC, and FEV₁ and a reduction in acute exacerbations and the use of maintenance therapies. Clinical remission was achieved in 55.1% of patients. Lower blood eosinophil counts during the first year (T1) were associated with greater improvements in lung function and fewer exacerbations. A greater relative decrease in eosinophils from baseline to T1 (ΔEOS%) was significantly associated with remission, reductions in exacerbations, and no maintenance OCS use. ΔEOS% was the only independent predictor of remission in the multivariate analysis. A ≥90% reduction predicted remission with 80% specificity (AUC = 0.726). <b>Conclusions</b>: Monitoring blood eosinophils after mepolizumab initiation could be a useful tool for predicting long-term response to treatment. In particular, a reduction by over 90% of peripheral blood eosinophils during the first year of mepolizumab treatment predicts clinical remission with a specificity of 80%. Considering the accessibility and the low cost of this biomarker, it may help to optimize long-term asthma management.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-07-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12372109/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144940231","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Immunogenicity Risk Assessment of Biotherapeutics Using an Ex Vivo B Cell Assay.","authors":"Kevin M Budge, Ross Blankenship, Patricia Brown-Augsburger, Lukasz K Chlewicki","doi":"10.3390/antib14030062","DOIUrl":"10.3390/antib14030062","url":null,"abstract":"<p><strong>Background/objectives: </strong>Anti-drug antibody (ADA) formation can impact the safety, pharmacokinetics, and/or efficacy of biotherapeutics, including monoclonal antibodies (mAbs). Current strategies for ADA/immunogenicity risk prediction of mAbs include in silico algorithms, T cell proliferation assays, MHC-associated peptide proteomics assays (MAPPs), and dendritic cell internalization assays. However, B cell-mediated responses are not assessed in these assays. B cells are professional antigen-presenting cells (APCs) and secrete antibodies toward immunogenic mAbs. Therefore, methods to determine B cell responses would be beneficial for immunogenicity risk prediction and may provide a more comprehensive assessment of risk.</p><p><strong>Methods: </strong>We used a PBMC culture method with the addition of IL-4, IL-21, B cell activating factor (BAFF), and an anti-CD40 agonist mAb to support B cell survival and activation.</p><p><strong>Results: </strong>B cells in this assay format become activated, proliferate, and secrete IgG. A panel of 51 antibodies with varying clinical immunogenicity rates were screened in this assay with IgG secretion used as a readout for immunogenicity risk. IgG secretion differed among test articles but did not correlate with the clinical immunogenicity rating.</p><p><strong>Conclusions: </strong>This dataset highlights the challenges of developing a B cell assay for immunogenicity risk prediction and provides a framework for further refinement of a B cell-based assay for immunogenicity risk prediction of mAbs.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-07-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12372046/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144940156","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}