Antibodies最新文献

{"title":"The Shifting Paradigm of Monoclonal Antibodies in COVID-19 Management: From Early Triumphs to Viral Resistance and Future Perspectives.","authors":"Francesco Ferrara, Flavia De Berardinis, Manlio Scognamiglio, Andrea Zovi","doi":"10.3390/antib15030048","DOIUrl":"10.3390/antib15030048","url":null,"abstract":"<p><strong>Background: </strong>Monoclonal antibodies (mAbs) initially played a major role in outpatient COVID-19 management by providing rapid passive immunity and reducing progression to severe disease. However, continuous SARS-CoV-2 evolution progressively compromised the effectiveness of several anti-spike products. This narrative review summarizes the trajectory of COVID-19 mAbs across three phases: early clinical efficacy, loss of efficacy due to immune escape, and future directions.</p><p><strong>Methods: </strong>We conducted a narrative review focusing on mechanisms of action, pivotal clinical trials, and real-world effectiveness of neutralizing anti-spike mAbs and host-directed immunomodulatory mAbs. Emphasis was placed on the impact of variants-especially Omicron-on susceptibility and clinical use, as well as on emerging next-generation platforms.</p><p><strong>Results: </strong>First-generation neutralizing mAbs substantially reduced the hospitalization rates during the Alpha and Delta waves, while immunomodulatory mAbs became standard options for the hyperinflammatory phase in hospitalized patients. With the emergence of Omicron and its sub-lineages, extensive immune escape led to marked reductions in neutralization for many earlier anti-spike agents and consequent restrictions in use. Later-generation approaches targeting more conserved epitopes provided temporary solutions but were also challenged by ongoing antigenic drift. Host-directed immunomodulators retained clinical relevance because their mechanism is independent of viral spike mutations.</p><p><strong>Conclusions: </strong>The clinical role of monoclonal antibodies in COVID-19 has been dynamic and increasingly constrained by viral evolution. Future strategies should prioritize broadly neutralizing antibodies targeting conserved epitopes, innovative delivery platforms, and integration with real-time surveillance to preserve clinical utility in the endemic phase and improve preparedness for future outbreaks.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"15 3","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-06-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13295941/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148315440","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":"Development and Validation of Cell-Based Bioassay for the Detection of Neutralizing Antibodies to Ocrelizumab in Human Serum Using Antibody-Dependent Cell-Mediated Cytotoxicity Test in a Reporter Cell Line Expressing FcγRIIIa.","authors":"Olga Strizhakova, Grigory Poroshin, Andrei Pershin, Yana Bakhareva, Ivan Shevchenko, Ivan Lyagoskin, Rakhim Shukurov, Ravil Khamitov","doi":"10.3390/antib15030046","DOIUrl":"10.3390/antib15030046","url":null,"abstract":"<p><strong>Background/objectives: </strong>Ocrelizumab is a humanized monoclonal antibody targeting CD20, approved for the treatment of adult patients with relapsing multiple sclerosis (RMS) and primary progressive multiple sclerosis (PPMS). The neutralizing activity of anti-drug antibodies (ADAs), especially neutralizing ADAs (nADAs) activity, should be examined considering that it can alter pharmacokinetic (PK) and pharmacodynamic (PD) profiles, reduce drug efficacy, and lead to life-threatening adverse events.</p><p><strong>Methods: </strong>This article presents data on the development and validation of an assay for neutralizing anti-drug antibodies (nADA) based on ADCC reporter cells for the analysis of patient sera in the context of ocrelizumab clinical studies.</p><p><strong>Results: </strong>Critical steps and conditions to minimize assay variability were identified. The lower limit of detection was 549.6 ng/mL. The cutoff for nonspecific neutralization was determined as 19.7%. The presence of 0.37-3.0 μg/mL ocrelizumab in a biological sample enables the detection of 1.1-10.0 μg/mL polyclonal anti-ocrelizumab idiotype antibodies, respectively.</p><p><strong>Conclusions: </strong>The developed method can be used for immunogenicity studies of medicinal products containing ocrelizumab.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"15 3","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-05-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13295840/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148315460","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 Novel Monoclonal Antibody Targeting the A29 Protein of Monkeypox Virus and Its Application in Immunoassay.","authors":"Nan Jia, Weixiao Wang, Guangwei Zhao, Danfei Meng, Liyuan Zheng, Jinhua Dong","doi":"10.3390/antib15030045","DOIUrl":"10.3390/antib15030045","url":null,"abstract":"<p><strong>Background: </strong>The monkeypox virus (MPXV) has attracted considerable global attention due to its potential to cause widespread outbreaks, necessitating the development of rapid and accurate diagnostic methods of significant clinical importance. A29, a key envelope protein of MPXV, represents a promising diagnostic target.</p><p><strong>Methods: </strong>A novel monoclonal antibody, D10, was isolated from the human Tomlinson I+J phage display library by biopanning against the recombinant A29 protein. The D10 Fab fragment was expressed and purified, and its binding affinity was characterized by biolayer interferometry. Molecular docking was performed to predict potential interacting residues. Specificity and detection performance were evaluated by direct and competitive enzyme-linked immunosorbent assay (ELISA).</p><p><strong>Results: </strong>D10 possesses a unique complementarity-determining region sequence and exhibits strong binding affinity toward the A29 protein. Structural modeling analysis suggested potential interacting residues of A29, including Gln67, Arg74, Asn75, Arg81, and Asn84, which may primarily interact with Ser10, Thr5, Gly49, Gly47, and Glu97 in the heavy chain of D10. The binding affinity, determined by biolayer interferometry, showed a dissociation equilibrium constant of 6.44 nM, indicating strong binding capability. Furthermore, competitive ELISA demonstrated that D10 binds selectively to the A29 protein, with a half-maximal inhibitory concentration of 1.88 μg/mL and a limit of detection of 0.12 μg/mL.</p><p><strong>Conclusions: </strong>Overall, this monoclonal antibody provides a valuable tool for the immunological detection of MPXV and holds potential for future clinical diagnostic applications.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"15 3","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-05-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13295737/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148315341","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":"From Single Cells to Silicon: Emerging Technologies Transforming Monoclonal Antibody Discovery.","authors":"Victoria Sherwood, Denise Harold, Richard O'Kennedy, Christine Loscher, Paul Leonard","doi":"10.3390/antib15030047","DOIUrl":"10.3390/antib15030047","url":null,"abstract":"<p><p>Monoclonal antibody (mAb) discovery has been transformed by advances in single-cell technologies, microfluidics, high-throughput sequencing, and computational design. Modern platforms enable the interrogation of large numbers of individual B cells, directly linking antibody sequence with antigen specificity and functional activity. Microfluidic and optofluidic systems now support high-throughput compartmentalisation and functional screening of antibody-secreting cells, while sequencing-based approaches allow parallel recovery of paired heavy- and light-chain sequences. These developments have shifted antibody discovery from binding-based selection toward function-first paradigms, enabling the rapid identification of diagnostic and therapeutically relevant antibodies. Integration with computational tools, including machine learning and structure-based modelling, has further enabled the emergence of closed-loop discovery pipelines, in which experimental and in silico methods iteratively refine candidates. This review summarises key advances in single-cell microtools over the last decade and highlights how the convergence of experimental and computational technologies is reshaping antibody discovery toward scalable, data-driven, and increasingly automated platforms.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"15 3","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-05-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13296331/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148315385","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":"Immunochemical Determination of IgE and IgG Autoantibodies in Patients with Chronic Spontaneous Urticaria: A Narrative Review.","authors":"Chrysoula-Evangelia Karachaliou, Evangelia Livaniou","doi":"10.3390/antib15030044","DOIUrl":"10.3390/antib15030044","url":null,"abstract":"<p><p><b>Background/Objectives</b>: Chronic spontaneous urticaria (CSU) is characterized by almost daily wheals or angioedema lasting for more than six weeks and not attributable to a defined inducing factor. CSU reportedly affects 1-2% of the general population and may lead to a substantial impairment in patients' quality of life. Thus, developing methods that enable early diagnosis and assessment of disease activity is a major objective for scientists and clinicians. <b>Methods</b>: A significant proportion of CSU cases appears to be associated with autoimmune mechanisms, which mainly involve IgE autoantibodies (type I CSU), IgG autoantibodies (type IIb CSU), or both (type I and type IIb overlap). To this end, detection of specific IgE and/or IgG autoantibodies in CSU patients using biological or immunochemical assays can offer valuable information and enable further investigation and better management of the disease. <b>Results</b>: This review focuses on and presents various immunochemical assays, mainly ELISAs, for determining specific IgE and/or IgG autoantibodies, along with immunochemical methods for quantifying total IgE levels as an additional biomarker in CSU patients; the development and/or application of these assays has been reported in several papers published in the last decade on CSU. <b>Conclusions</b>: The methods presented have recently been applied and have substantially contributed to CSU diagnosis, endotyping and prediction of response to various treatments. Further validation of the existing immunochemical assays along with the development of reliable assays for novel autoantibodies and/or autoantigens will deepen our understanding of CSU pathogenesis and support the clinical diagnosis and treatment of CSU.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"15 3","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-05-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13295683/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148315463","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":"Computational Study of Antibody Binding to SARS-CoV-2 Variants.","authors":"Carolyn Chiu, Muhammad Zaki Jawaid, Daniel Lee Cox","doi":"10.3390/antib15030043","DOIUrl":"10.3390/antib15030043","url":null,"abstract":"<p><p><b>Background/Objectives</b>: The unprecedented structural and binding data for antibodies to the SARS-CoV-2 virus taken together with the mutations for the spike protein allows for a broad simulation study of antibody-spike protein binding. This provides an understanding of the co-evolution of human immunity and viral immunity escape. <b>Methods</b>: We utilized the YASARA molecular dynamics program to generate initial structures and simulate to equilibration for six SARS-CoV-2 variants and ten different antibodies sampling two different binding regions to the receptor binding domain of the spike (especially for the Class I antibodies in the same part of the spike that attaches to the ACE2 receptor protein) and one to the N-terminal domain of the spike. Starting structures for antibody binding to variant spike protein domains are perturbatively achieved through point mutations and insertions/deletions in the YASARA program. We employed YASARA to measure interfacial hydrogen bound counts between antibodies and variant spike proteins and the HawkDock MMGBSA program to characterize trends in binding energies with mutation for four of the antibodies. We utilized the VMD program to analyze the time course of hydrogen bond populations. <b>Results</b>: As seen in previous studies, interfacial hydrogen bond counts serve as an excellent proxy for binding energies without the large systematic error inherent in the latter. We find that there is generally a decline in antibody binding strength, as measured by interfacial hydrogen bond counts, with viral evolution, but that a modest re-entrance of binding strength is present for most antibodies studied. Generically, the antibody heavy chain binds more strongly to the spike protein, though for approximately half the antibodies the light chain binding strength converges to the heavy chain strength with viral evolution. <b>Conclusions</b>: The key conclusion is that the identified re-entrant immunity, speculatively arising from a balancing of maintenance of ACE2-spike binding while escaping antibodies through mutation, allows for some maintenance and even strengthening of immunity for later viral strains from early infection or vaccination.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"15 3","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-05-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13296164/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148315433","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":"Immune-Related Adverse Events of Cemiplimab Therapy in Advanced Cervical Cancer-Data from the Polish-Czech Cervical Cancer Immunotherapy Group (PCCIG-01) with a Review of the Literature.","authors":"Radosław Łupkowski, Karolina Górniak, Maja Lisik-Habib, Ewa Burchardt, Radosław Mądry, Monika Szarszewska, Katarzyna Gabalewicz, Dominika Pyszak, Petra Bretova, Beata Maćkowiak-Matejczyk, Wioletta Sawczuk, Monika Łączyńska-Madera, Dagmara Klasa-Mazurkiewicz, Angelika Gawlik-Urban, Magdalena Michalik, Zuzanna Borysiewicz, Ewa Iwańska, Mirosława Puskulluoglu, Paweł Blecharz, Renata Pacholczak-Madej","doi":"10.3390/antib15030042","DOIUrl":"10.3390/antib15030042","url":null,"abstract":"<p><strong>Background: </strong>Immunotherapy has become an integral part of systemic treatment for cervical cancer (CC). This study assessed the safety profile of cemiplimab and the association between immune-related adverse events (irAEs) and treatment outcomes in patients with persistent, recurrent or metastatic CC.</p><p><strong>Methods: </strong>This ambispective, multicenter, real-world cohort study included 101 patients treated in 13 reference oncology centers as part of the PCCIG-01 study. We evaluated the frequency and severity of irAEs and their association with progression-free survival (PFS) and overall survival (OS). Survival outcomes were analyzed using the Kaplan-Meier method and Cox proportional hazards models, with <i>p</i> < 0.05 considered statistically significant.</p><p><strong>Results: </strong>After a median follow-up of 7.5 months, adverse events occurred in 45 patients (44.6%) and were mostly grade (G) 1-2. IrAEs were observed in 34 patients (33.7%). Endocrine toxicities predominated (<i>n</i> = 24, 58.5% of irAEs), followed by hepatic (<i>n</i> = 5, 12.2%) and gastrointestinal events (<i>n</i> = 4, 9.8%). G3 irAEs occurred in 8 patients (7.9%). Median PFS was 3.9 months (95% CI 2.9-5.6) in patients without irAEs and 10.9 months (95% CI 5.7-16.3) in those with irAEs (<i>p</i> = 0.03). Median OS was 15.3 months (95% CI 8.6-25.9) in patients without irAEs and was not reached in those with irAEs (95% CI 11.6-NR; <i>p</i> = 0.11). The development of irAEs was associated with a 54% reduction in the risk of progression (HR 0.46, 95% CI 0.27-0.80), with no statistically significant impact on OS.</p><p><strong>Conclusions: </strong>In exploratory analyses, the occurrence of irAEs was associated with improved PFS in cemiplimab-treated patients with persistent, recurrent or metastatic CC. Cemiplimab showed a manageable safety profile, with most toxicities being G1-G2.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"15 3","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-05-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13214483/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148026366","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":"The Shifting Core: Antigenic Variability of the Influenza Virus Nucleoprotein Despite Evolutionary Conservation.","authors":"Alexandra Rak, Veronika Muzurova, Svetlana Donina, Polina Prokopenko, Irina Isakova-Sivak, Larisa Rudenko","doi":"10.3390/antib15030041","DOIUrl":"10.3390/antib15030041","url":null,"abstract":"<p><strong>Background: </strong>The highly mutable influenza virus causes severe annual infections worldwide and results in substantial socioeconomic losses. The spread of infection could be effectively controlled by cross-protective vaccines and universal diagnostic test systems based on the nucleoprotein (NP) as one of the most conserved viral antigens. However, NP also undergoes slow evolutionary changes, and little is known about the influence of these mutations on its antigenicity and immunogenicity.</p><p><strong>Methods: </strong>We expressed the full-length recombinant 6xHis-tagged NPs of ten evolutionary distant influenza A strains of different subtypes in <i>E. coli</i> BL21(DE3) cells and purified these proteins by immobilized metal affinity chromatography. The obtained antigens were identified by mass spectrometry and serological methods. NPs served as antigens for three immunizations of BALB/c mice (15 µg/animal at 14-day interval) and as capturing proteins in ELISA at 2 µg/mL, in order to study the effect of adaptive mutations on the antigenic and immunogenic properties of NPs.</p><p><strong>Results: </strong>A pronounced cross-reactivity of anti-NP antibodies induced in mice by immunization with different NPs was revealed. At the same time, we observed the differences in the humoral immunogenicity of NP, which are in line with the accumulation of evolutionarily driven NP mutations. In general, antibody affinity to heterologous NPs was reduced, indicating the differences in the specificity of anti-NP immunoglobulins, which may be caused by evolutionarily determined variability of immunogenic epitopes leading to the emergence of escape mutations.</p><p><strong>Conclusions: </strong>Overall, our results reflect the slightly evolving nature of the NP antigen, which influences the specificity spectrum of anti-NP antibodies and should be considered as a limitation for the development of NP-based cross-protective vaccines and test systems.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"15 3","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-05-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13214484/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148025841","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":"Safety and Efficacy of Mosunetuzumab: Experience in the Hospital Cardinale Giovanni Panico.","authors":"Giulio Turco, Donatella Tarantino, Antonietta Giuseppa Ferraro, Giuseppina Greco, Domenico Tricarico","doi":"10.3390/antib15030040","DOIUrl":"10.3390/antib15030040","url":null,"abstract":"<p><strong>Background/objective: </strong>Follicular lymphoma (FL) is one of the most common indolent B-cell non-Hodgkin lymphomas (NHL) and is characterized by recurrent relapses despite advances in therapy. Bispecific antibodies that redirect T lymphocytes toward malignant B cells represent a major innovation in the treatment of relapsed or refractory disease. Mosunetuzumab is a CD20×CD3 bispecific antibody that induces T-cell mediated cytotoxicity against B-cell malignancies. In this manuscript, we describe the clinical experience with mosunetuzumab in three patients with relapsed or refractory FL treated at the Hospital Card. G. Panico, Tricase (LE).</p><p><strong>Methods: </strong>Clinical history, prior therapies, treatment responses, and safety outcomes are reported.</p><p><strong>Results: </strong>The cases illustrate the potential efficacy and manageable safety profile of mosunetuzumab in heavily pretreated FL patients.</p><p><strong>Conclusion: </strong>The effectiveness of this drug is confirmed in our center.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"15 3","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-05-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13214480/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148025874","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":"Ca₁₃Mab-17, a Novel Anti-Cadherin-13 Monoclonal Antibody for Versatile Applications.","authors":"Kai Shimizu, Hiroyuki Suzuki, Mika K Kaneko, Yukinari Kato","doi":"10.3390/antib15030039","DOIUrl":"10.3390/antib15030039","url":null,"abstract":"<p><strong>Background/objectives: </strong>Cadherin-13 (CDH13), part of the cadherin family, is attached to the plasma membrane through glycosylphosphatidylinositol. CDH13 plays essential roles in the development of the neurological and vascular systems and is a risk factor for neural and cardiovascular diseases. CDH13 is expressed on the plasma membrane in both mature and uncleaved precursor forms with the prodomain. Although several anti-CDH13 monoclonal antibodies (mAbs) are available for basic research, there have been no reports of anti-CDH13 mAbs that can detect both the mature form and the uncleaved precursor in flow cytometry.</p><p><strong>Methods: </strong>We developed novel anti-human CDH13 mAbs (named Ca₁₃Mabs) using the mature form of CDH13-expressed cells as an antigen.</p><p><strong>Results: </strong>Among Ca₁₃Mabs, a clone, Ca₁₃Mab-17 (IgG_2b, κ) specifically recognized the mature and uncleaved precursor CDH13-overexpressed Chinese hamster ovary-K1 (CHO/CDH13) cells with no detectable cross-reactivity toward 21 other cadherins by flow cytometry. Ca₁₃Mab-17 also detected endogenous CDH13 in human glioblastoma (LN229 and U87MG) and lung mesothelioma (NCI-H2052) cell lines. The dissociation constant (<i>K</i>_D) value of Ca₁₃Mab-17 for LN229 was estimated at 4.1 × 10^-8 M. Furthermore, Ca₁₃Mab-17 detected both the mature and uncleaved precursor CDH13 in Western blotting. It also identified new blood vessels and glioblastoma cells by immunohistochemistry.</p><p><strong>Conclusions: </strong>Ca₁₃Mab-17 is a versatile tool for detecting both mature and uncleaved precursor forms of CDH13 and has potential for tumor diagnosis and therapy.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"15 3","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-05-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13214481/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148026203","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}