Monoclonal Antibodies in Immunodiagnosis and Immunotherapy最新文献

Monoclonal Antibody-Based Anti-Cryptococcosis Therapy. 基于单克隆抗体的抗隐球菌病治疗。

Monoclonal Antibodies in Immunodiagnosis and Immunotherapy Pub Date : 2026-10-01 Epub Date: 2026-08-14 DOI: 10.1177/21679436261476438

Marcos William de Lima Gualque, Gabriel Rezende Pimenta, Daniel Gomes de Sousa, Lara Yukari Ogasawara, Aline Ruan Wu, Mariana Macul, Matheus Torrichelli Antunes, Marcela Santana Demarchi, Giovana Moreno Fratus, Maria Júlia Siqueto, Andrei Moroz, Maria José Soares Mendes Giannini, Ana Marisa Fusco Almeida

{"title":"Monoclonal Antibody-Based Anti-Cryptococcosis Therapy.","authors":"Marcos William de Lima Gualque, Gabriel Rezende Pimenta, Daniel Gomes de Sousa, Lara Yukari Ogasawara, Aline Ruan Wu, Mariana Macul, Matheus Torrichelli Antunes, Marcela Santana Demarchi, Giovana Moreno Fratus, Maria Júlia Siqueto, Andrei Moroz, Maria José Soares Mendes Giannini, Ana Marisa Fusco Almeida","doi":"10.1177/21679436261476438","DOIUrl":"10.1177/21679436261476438","url":null,"abstract":"Cryptococcosis remains one of the most severe invasive fungal diseases worldwide, causing high morbidity and mortality, particularly among immunocompromised individuals. Despite the availability of antifungal drugs, current therapeutic regimens are limited by drug toxicity, prolonged treatment, antifungal resistance, biofilm-associated tolerance, and frequent disease relapse, highlighting the need for novel therapeutic approaches. Monoclonal antibodies (mAbs) have emerged as promising immunotherapeutic agents because of their ability to specifically target fungal components while modulating host immune responses. This review provides a comprehensive overview of recent advances in monoclonal antibody-based strategies against Cryptococcus spp. Additionally, recent innovations in antibody engineering, including radioimmunotherapy, Fc engineering, nanobody technology, immune checkpoint modulation, and chimeric antigen receptor-(CAR)-based cellular therapies, are highlighted as emerging approaches with the potential to enhance antifungal efficacy and overcome current therapeutic limitations. Finally, we discuss the major challenges associated with the clinical translation of antifungal mAbs, including pharmacokinetic barriers, production costs, limited clinical evidence, and regulatory constraints. Collectively, the available evidence supports mAbs as promising adjunctive immunotherapeutic agents and underscores the importance of continued advances in antibody engineering and clinical research to facilitate their incorporation into future strategies for the treatment of cryptococcosis.","PeriodicalId":53514,"journal":{"name":"Monoclonal Antibodies in Immunodiagnosis and Immunotherapy","volume":" ","pages":"89-99"},"PeriodicalIF":0.0,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148764395","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}

引用次数: 0

A Novel Anti-Glypican-3 Monoclonal Antibody G₃Mab-25 for Versatile Applications. 一种新型抗glypican -3单克隆抗体G3Mab-25

Monoclonal Antibodies in Immunodiagnosis and Immunotherapy Pub Date : 2026-10-01 Epub Date: 2026-06-29 DOI: 10.1177/21679436261464851

Saori Okuno, Hiroyuki Suzuki, Yukari Ogura, Reina Ito, Mika K Kaneko, Yukinari Kato

{"title":"A Novel Anti-Glypican-3 Monoclonal Antibody G3Mab-25 for Versatile Applications.","authors":"Saori Okuno, Hiroyuki Suzuki, Yukari Ogura, Reina Ito, Mika K Kaneko, Yukinari Kato","doi":"10.1177/21679436261464851","DOIUrl":"10.1177/21679436261464851","url":null,"abstract":"Glypican-3 (GPC3) belongs to the glypican family of heparan sulfate proteoglycans and is frequently overexpressed in hepatocellular carcinoma (HCC). The overexpression of GPC3 is associated with the poor clinical outcomes, suggesting its potential as a clinically relevant biomarker and therapeutic target. Therefore, anti-GPC3 monoclonal antibodies (mAbs) have been developed in various modalities for tumor diagnosis and therapy. In this study, 88 clones of novel anti-GPC3 mAbs were established using a flow cytometry-based high-throughput screening, the Cell-Based Immunization and Screening (CBIS) method. Among them, a clone G3Mab-25 (IgG1, κ) recognized GPC3-overexpressed Chinese hamster ovary-K1 (CHO/GPC3) but not parental CHO-K1 in flow cytometry. Furthermore, G3Mab-25 recognizes endogenous GPC3 in GPC3-expressing HCC cell lines, including HepG2, HuH-7, and JHH-5. G3Mab-25 specifically recognized only CHO/GPC3, but not other GPC family-overexpressed CHO-K1. The dissociation constant values of G3Mab-25 for CHO/GPC3, HepG2, HuH-7, and JHH-5 were determined to be 1.8 × 10-8 M, 7.3 × 10-9 M, 3.9 × 10-9 M, and 1.4 × 10-9 M, respectively. Moreover, G3Mab-25 detects the N-terminal fragment of GPC3 in western blotting. In immunohistochemistry, G3Mab-25 showed a diverse staining pattern for GPC3 in HCC tissues. G3Mab-25, established by the CBIS method, is a versatile mAb for basic research and is expected to contribute to tumor diagnosis and therapy.","PeriodicalId":53514,"journal":{"name":"Monoclonal Antibodies in Immunodiagnosis and Immunotherapy","volume":" ","pages":"77-88"},"PeriodicalIF":0.0,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148347357","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}

引用次数: 0

Restoring Trust in Commercial Antibody Validation. 恢复对商业抗体验证的信任。

Monoclonal Antibodies in Immunodiagnosis and Immunotherapy Pub Date : 2026-09-28 DOI: 10.1177/21679436261494899

Andrei Moroz, Cory L Brooks

引用次数: 0

Recombinant Expression and Engineering of MDI- and HDI-Specific Monoclonal Antibodies for Proof-of-Concept Detection of Diisocyanate Adducts and Candidate Assay Calibrators. MDI和hdi特异性单克隆抗体的重组表达和工程，用于二异氰酸酯加合物和候选测定校准器的概念验证检测。

Monoclonal Antibodies in Immunodiagnosis and Immunotherapy Pub Date : 2026-08-27 DOI: 10.1177/21679436261483330

Adam V Wisnewski, Jian Liu, Carrie A Redlich

{"title":"Recombinant Expression and Engineering of MDI- and HDI-Specific Monoclonal Antibodies for Proof-of-Concept Detection of Diisocyanate Adducts and Candidate Assay Calibrators.","authors":"Adam V Wisnewski, Jian Liu, Carrie A Redlich","doi":"10.1177/21679436261483330","DOIUrl":"https://doi.org/10.1177/21679436261483330","url":null,"abstract":"Methylene-diphenyl diisocyanate (MDI) and hexamethylene diisocyanate (HDI), important chemicals for polyurethane production, can react with self-molecules, trigger immune responses, and cause asthma. To validate molecular determinants of diisocyanate immune recognition and develop renewable immunoassay reagents, we generated MDI- and HDI-specific recombinant monoclonal antibodies (mAbs) from hybridoma-derived variable-region DNA sequences using a human embryonic kidney (HEK) cell line expression system. Three anti-MDI and one anti-HDI mouse IgG1/κ mAbs were produced, purified, and evaluated for binding to MDI, HDI, and control antigens, including toluene diisocyanate (TDI) and mock-reacted protein. To support assay standardization in research and translational applications, we engineered one anti-MDI (DA5) and one anti-HDI (AG5) mAb as human Fc chimeras (human IgG1 or IgE heavy-chain constant regions with human κ light-chain constant region) and confirmed that chimerization preserved antigen specificity. As a proof-of-principle, one of the chimeric mAbs was evaluated as a candidate calibrator in an enzyme-linked immunosorbant assay (ELISA) format to quantify diisocyanate-specific antibodies in serum from an MDI-exposed worker. In addition, mAb DA5 was engineered with a FLAG epitope to enable immunoassays for detecting MDI-protein reaction products in airway fluid, including sandwich ELISA (with anti-MDI mAb CE2) and Western blot formats. Together, these data show that diisocyanate specificity can be recapitulated by recombinant expression from deposited variable-region DNA sequences. The engineered reagents enable immunoassay detection of MDI-protein adducts in complex matrices and serve as proof-of-concept calibrators for ELISA-based quantification of anti-diisocyanate antibodies in human serum.","PeriodicalId":53514,"journal":{"name":"Monoclonal Antibodies in Immunodiagnosis and Immunotherapy","volume":" ","pages":"21679436261483330"},"PeriodicalIF":0.0,"publicationDate":"2026-08-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148834524","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}

引用次数: 0

Establishment of a Novel Anti-EphA4 Monoclonal Antibody, Ea₄Mab-3, for Versatile Applications. 一种新型抗epha4单克隆抗体Ea4Mab-3的建立

Monoclonal Antibodies in Immunodiagnosis and Immunotherapy Pub Date : 2026-07-01 Epub Date: 2026-05-23 DOI: 10.1177/21679436261450334

Ayano Saga, Guanjie Li, Tomohiro Tanaka, Mika K Kaneko, Hiroyuki Suzuki, Yukinari Kato

{"title":"Establishment of a Novel Anti-EphA4 Monoclonal Antibody, Ea4Mab-3, for Versatile Applications.","authors":"Ayano Saga, Guanjie Li, Tomohiro Tanaka, Mika K Kaneko, Hiroyuki Suzuki, Yukinari Kato","doi":"10.1177/21679436261450334","DOIUrl":"10.1177/21679436261450334","url":null,"abstract":"Erythropoietin-producing hepatocellular carcinoma (Eph) receptor A4 (EphA4) binds to a broad range of ephrin ligands and is upregulated in various tumors. EphA4 activation plays crucial roles in the maintenance of cancer invasiveness, immune evasion, and stem cell properties. Furthermore, a novel EphA4 ligand, secretory ribonuclease 1, has been identified, and its interaction stimulates EphA4 signaling, leading to the promotion of cancer stem cell properties. Therefore, EphA4 has been considered an attractive target for cancer therapies. Thus, monoclonal antibodies (mAbs) against EphA4 are essential for basic research and mAb-based treatment in the clinic. In this study, we developed a novel anti-human EphA4 mAb, Ea4Mab-3, using the Cell-Based Immunization and Screening (CBIS) method. Ea4Mab-3 reacted with EphA4-overexpressed Chinese hamster ovary-K1 (CHO/EphA4) and endogenous EphA4-positive lung squamous cell carcinoma LK-2 in flow cytometry. The binding affinities (apparent dissociation constant KD values) were determined as 4.5 × 10-9 M for CHO/EphA4 and 2.5 × 10-9 M for LK-2. Furthermore, Ea4Mab-3 did not exhibit cross-reactivity with other Eph receptor-overexpressed CHO-K1 cells. In addition, Ea4Mab-3 is suitable for immunoblotting and immunohistochemistry. These results indicate that Ea4Mab-3, established using the CBIS method, facilitates basic studies of EphA4 and is expected to be useful for mAb-based tumor diagnosis and therapy.","PeriodicalId":53514,"journal":{"name":"Monoclonal Antibodies in Immunodiagnosis and Immunotherapy","volume":" ","pages":"48-57"},"PeriodicalIF":0.0,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148007614","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}

引用次数: 0

Epitope Mapping of Anti-mouse ACKR4 Monoclonal Antibodies Developed by N-Terminal Peptide Immunization. n端肽免疫制备抗小鼠ACKR4单克隆抗体的表位定位

Monoclonal Antibodies in Immunodiagnosis and Immunotherapy Pub Date : 2026-07-01 Epub Date: 2026-06-16 DOI: 10.1177/21679436261461702

Miu Hirose, Tomohiro Tanaka, Miyuki Yanaka, Takuro Nakamura, Mika K Kaneko, Hiroyuki Suzuki, Yukinari Kato

{"title":"Epitope Mapping of Anti-mouse ACKR4 Monoclonal Antibodies Developed by N-Terminal Peptide Immunization.","authors":"Miu Hirose, Tomohiro Tanaka, Miyuki Yanaka, Takuro Nakamura, Mika K Kaneko, Hiroyuki Suzuki, Yukinari Kato","doi":"10.1177/21679436261461702","DOIUrl":"10.1177/21679436261461702","url":null,"abstract":"Leukocyte migration is a fundamental process in both innate and adaptive immune responses. This process is tightly regulated by chemokines and their cognate receptors. The bioavailability of chemokines is further modulated by atypical chemokine receptors (ACKRs), a subset of chemokine receptor-like molecules that lack coupling to canonical G protein-mediated signaling pathways. Among these, ACKR4 regulates dendritic cell migration through ligand scavenging and has been implicated in tumor progression in murine models. We previously established anti-mouse ACKR4 (mACKR4) mAbs, A4Mab-1, A4Mab-2, and A4Mab-3, by N-terminal peptide immunization. This study examined the binding epitopes of A4Mabs. Alanine (or glycine) scanning within the N-terminal region (amino acids 2-19) was performed using flow cytometry and Western blotting. Results showed that Tyr12 is required for recognition by A4Mab-1 in flow cytometry, whereas Tyr11, Tyr12, Glu14, Glu15, and Glu17 are required in Western blotting. For A4Mab-2, Tyr12, Glu15, and Asn16 are required in flow cytometry, whereas Tyr11, Tyr12, Tyr13, Glu15, and Asn16 are required in Western blotting. Additionally, Glu14, Asn16, and Glu17 are required for recognition by A4Mab-3 in flow cytometry. These findings contribute to the understanding of mACKR4 recognition by A4Mabs.","PeriodicalId":53514,"journal":{"name":"Monoclonal Antibodies in Immunodiagnosis and Immunotherapy","volume":" ","pages":"69-75"},"PeriodicalIF":0.0,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148260403","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}

引用次数: 0

Guidelines for Reporting New Monoclonal Antibodies: Improving Transparency, Reproducibility, and Research Utility. 新单克隆抗体报告指南：提高透明度、可重复性和研究实用性。

Monoclonal Antibodies in Immunodiagnosis and Immunotherapy Pub Date : 2026-07-01 Epub Date: 2026-06-05 DOI: 10.1177/21679436261458597

Andrei Moroz, Cory L Brooks

引用次数: 0

Epitope Mapping of Anti-Mouse C-C Motif Chemokine Receptor 1 Monoclonal Antibodies Developed by the Cell-Based Immunization and Screening Method. 基于细胞免疫和筛选的抗小鼠C-C基序趋化因子受体1单克隆抗体的表位定位

Monoclonal Antibodies in Immunodiagnosis and Immunotherapy Pub Date : 2026-07-01 Epub Date: 2026-06-10 DOI: 10.1177/21679436261459606

Ayaka Okada, Hiroyuki Suzuki, Mika K Kaneko, Yukinari Kato

{"title":"Epitope Mapping of Anti-Mouse C-C Motif Chemokine Receptor 1 Monoclonal Antibodies Developed by the Cell-Based Immunization and Screening Method.","authors":"Ayaka Okada, Hiroyuki Suzuki, Mika K Kaneko, Yukinari Kato","doi":"10.1177/21679436261459606","DOIUrl":"10.1177/21679436261459606","url":null,"abstract":"The C-C motif chemokine receptor 1 (CCR1) plays key roles in guiding leukocyte movement during immune surveillance and inflammatory responses. Targeting CCR1 is a promising approach for treating autoimmune diseases and cancers. We previously developed monoclonal antibodies against mouse CCR1 (mCCR1) (clones C1Mab-2 and C1Mab-6) for use in flow cytometry and Western blotting. However, the specific binding sites have not yet been identified. This study examined the binding epitope of C1Mab-2 and C1Mab-6 using flow cytometry. Analysis of mCCR1 mutants with altered extracellular domains showed that C1Mab-2 and C1Mab-6 bind to the N-terminal region of mCCR1. Additionally, PA-tag substitution experiments identified the epitope as 1st Met and amino acids 2-13 of mCCR1. Further alanine (or glycine) scanning within the N-terminal region (amino acids 2-13) demonstrated that Glu2, Asp5, and Phe6 are essential for recognition by C1Mab-2, and Glu2, Ile3, and Asp5 are crucial for recognition by C1Mab-6 in flow cytometry and Western blotting. These findings contribute to the understanding of mCCR1 and C1Mab interaction.","PeriodicalId":53514,"journal":{"name":"Monoclonal Antibodies in Immunodiagnosis and Immunotherapy","volume":" ","pages":"58-68"},"PeriodicalIF":0.0,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148213280","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}

引用次数: 0

How Alternative Models May be of Assistance in Antibody Development. 如何替代模型可能有助于抗体开发。

Monoclonal Antibodies in Immunodiagnosis and Immunotherapy Pub Date : 2026-05-01 Epub Date: 2026-02-19 DOI: 10.1177/21679436261425534

Kelvin Sousa Dos Santos, Cory L Brooks, Andrei Moroz

引用次数: 0

A Novel Anti-CDH5/VE-Cadherin Monoclonal Antibody (Ca₅Mab-8) for Flow Cytometry, Western Blotting, and Immunohistochemistry. 一种新型抗cdh5 /VE-Cadherin单克隆抗体（Ca5Mab-8），用于流式细胞术、Western Blotting和免疫组织化学。

Monoclonal Antibodies in Immunodiagnosis and Immunotherapy Pub Date : 2026-05-01 Epub Date: 2026-04-09 DOI: 10.1177/21679436261441142

Haruto Yamamoto, Hiroyuki Suzuki, Mika K Kaneko, Yukinari Kato

{"title":"A Novel Anti-CDH5/VE-Cadherin Monoclonal Antibody (Ca5Mab-8) for Flow Cytometry, Western Blotting, and Immunohistochemistry.","authors":"Haruto Yamamoto, Hiroyuki Suzuki, Mika K Kaneko, Yukinari Kato","doi":"10.1177/21679436261441142","DOIUrl":"10.1177/21679436261441142","url":null,"abstract":"Cadherin-5 (CDH5), also known as vascular endothelial cadherin (VE-cadherin), plays crucial roles in endothelial cell adhesion, vascular barrier function, and signaling. CDH5 manages endothelial cell-cell junctions during vascular remodeling, which is vital for both vascular homeostasis and adaptive responses to pathological stimuli. Although anti-CDH5 monoclonal antibodies (mAbs) are used for specific applications such as flow cytometry, Western blotting, and immunohistochemistry (IHC), highly sensitive and versatile anti-CDH5 mAbs suitable for all these applications remain limited. Here, new anti-human CDH5 mAbs, called Ca5Mabs, were developed through a flow cytometry-based high-throughput screening. Among them, clone Ca5Mab-8 (mouse IgG2a, kappa) recognized CDH5-overexpressed Chinese hamster ovary-K1 (CHO/CDH5) cells in flow cytometry. Moreover, Ca5Mab-8 also recognized endogenous CDH5-expressing human endothelial cell lines (HUVEC/TERT2 and HDMVEC/TERT164-B) and a cervical cancer cell line (HeLa). These reactivities exceeded those of a commercial anti-CDH5 mAb (clone BV9). The apparent dissociation constant of Ca5Mab-8 for CHO/CDH5 was measured as 6.1 × 10-9 M. Ca5Mab-8 can detect endogenous CDH5 in Western blotting. In addition, Ca5Mab-8, but not BV9, can be used for IHC to detect endothelial cells in formalin-fixed paraffin-embedded tissues. These findings suggest that Ca5Mab-8 is a versatile basic research tool in vascular biology and has potential for clinical applications including tumor diagnosis and therapy.","PeriodicalId":53514,"journal":{"name":"Monoclonal Antibodies in Immunodiagnosis and Immunotherapy","volume":" ","pages":"34-44"},"PeriodicalIF":0.0,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147640400","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}

引用次数: 0