Antibodies最新文献

{"title":"IgM Antibody Detection as a Diagnostic Marker for Acute Toxoplasmosis: Current Status of Studies and Main Limitations.","authors":"Karolina Sołowińska, Lucyna Holec-Gąsior","doi":"10.3390/antib14020044","DOIUrl":"10.3390/antib14020044","url":null,"abstract":"<p><p>Accurate dating of <i>Toxoplasma gondii</i> infection is essential for effective clinical management, particularly in pregnant women and immunocompromised individuals, where distinguishing acute from chronic infection informs treatment decisions. Serological detection of IgM antibodies is a key tool in diagnosing recent toxoplasmosis; however, its reliability is compromised by persistent IgM responses, cross-reactivity, and assay variability. While IgM lacks sufficient specificity to serve as a standalone marker of acute infection, it remains an important component of serological panels. This review summarizes current IgM detection methods and explores advancements aimed at improving diagnostic accuracy with a focus on recombinant antigens, which have emerged as promising alternatives to traditional <i>Toxoplasma</i> lysate antigen-based immunoassays. This paper also explores alternative methods of differentiating chronic and acute toxoplasmosis and outlines key areas for future research.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 2","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12101336/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144126287","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":"Neutralization of the Pandemic Influenza A/H1N1 Virus with <i>Lama glama</i> Humanized Nanobodies (VHH).","authors":"Zeila Yazmín Páez-Hernández, Jose Luis Stephano-Hornedo, Jose Alberto Bolaños-Prats, Iván Córdova-Guerrero, Mariana Macías-Alonso, Joaquín G Marrero, Angel Pulido Capiz, Victor García González","doi":"10.3390/antib14020042","DOIUrl":"10.3390/antib14020042","url":null,"abstract":"<p><p>Background/Objetives: Nanobodies (VHH) have become an excellent tool for diagnosis, therapy, and research since VHH shows a high capability of recognizing and neutralizing antigens. VHHs are highly soluble and stable at high temperatures, and in the presence of chaotropic agents, they offer significant advantages over other biological therapeutic agents. This study aimed to identify and humanize VHH fragments with neutralizing potential against the influenza A/H1N1 virus.</p><p><strong>Methods: </strong>A library of VHH antibody fragments was produced by phage display technique against an inactivated influenza A/H1N1 vaccine. Three VHH sequences were selected and humanized. Specifically, the recognition capacity of the antibodies denominated 2-C10 and 2-C10H was confirmed by ELISA and western blot (WB), as well as their microneutralization capacity in a cellular model, suggesting their potential therapeutic use in patients infected with the influenza A/H1N1 virus. Molecular docking assays were used to support the mechanism of viral inhibition.</p><p><strong>Results: </strong>The VHHs 2-C10 and 2-C10H showed specific recognition of influenza A/H1N1 antigens by ELISA and Western Blot and demonstrated neutralizing activity in vitro. The optimal VHH, 2-C10H, showed 75% neutralization capacity at a concentration of 1.56 μg/mL against the A/H1N1 viral strain, potentially through the inactivation of hemagglutinin protein, a phenomenon supported by molecular docking assays.</p><p><strong>Conclusions: </strong>This study presents a strategic approach to identify VHH candidates that may be useful for diagnosing and potentially treating patients already infected by the A/H1N1 virus, as it may reduce the severity of their symptoms.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 2","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-05-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12101271/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144126363","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":"IgG to Galactose-Alpha-1,3-Galactose: Impact of Alpha-Gal IgE Sensitization, Blood Type, and Tick Bites.","authors":"Samuel M Ailsworth, Matthew MacCallum, Nathan E Richards, Lisa J Workman, Pamela Schoppee Bortz, Thomas Makin, Thomas A E Platts-Mills, Jeffrey M Wilson","doi":"10.3390/antib14020043","DOIUrl":"10.3390/antib14020043","url":null,"abstract":"<p><p><b>Background:</b> Antibodies to galactose-alpha-1,3-galactose (alpha-gal), particularly the IgM and IgG isotypes, are abundant in human sera. These antibodies are known to be an important xenotransplantation barrier, but the full implications of these antibodies to health and disease remain incompletely understood. By contrast, IgE to alpha-gal is uncommon in the population but has been associated with tick bites and causally linked with mammalian meat allergy, often now known as alpha-gal syndrome (AGS). To date, there have been few population-based studies that have investigated alpha-gal IgG levels in relation to demographic factors, diet, tick bites, and mammalian meat allergy. <b>Methods:</b> Adults, predominantly healthcare workers, were recruited for a COVID-19 vaccine study. At least one serum sample was collected, and subjects completed questionnaires to provide demographic, diet, and tick exposure data. Alpha-gal IgG, IgE, and total IgG were measured using the ImmunoCAP platform, and blood group was assessed via reverse typing using stored serum. We also assessed alpha-gal IgG levels among subjects with AGS, recruited from an allergy clinic. <b>Results:</b> The median age of the 267 subjects in the vaccine cohort was 42 years, and median alpha-gal IgG levels were 3.0 μg/mL. Alpha-gal IgG levels were higher among the 43 (16.1%) subjects who had alpha-gal IgE sensitization (≥0.1 IU/mL) and among subjects lacking the B blood group antigen (blood groups A and O). Alpha-gal IgG levels did not differ between the subjects who had asymptomatic alpha-gal IgE sensitization and those who had meat allergy. However, both groups had higher alpha-gal IgG levels than subjects who lacked alpha-gal IgE sensitization. Subjects who reported prior tick or chigger bites had higher alpha-gal IgG levels than those without a bite history, regardless of alpha-gal IgE sensitization status. <b>Conclusions:</b> In a population-based cohort, alpha-gal IgG antibodies were found to be prevalent, and levels were increased in subjects with blood groups A and O, subjects who were alpha-gal IgE sensitized, and those who reported a history of tick bites.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 2","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-05-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12101169/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144126260","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":"Generative Deep Learning Design of Single-Domain Antibodies Against Venezuelan Equine Encephalitis Virus.","authors":"Jinny L Liu, Gabrielle C Bayacal, Jerome Anthony E Alvarez, Lisa C Shriver-Lake, Ellen R Goldman, Scott N Dean","doi":"10.3390/antib14020041","DOIUrl":"10.3390/antib14020041","url":null,"abstract":"<p><strong>Background/objectives: </strong>Venezuelan equine encephalitis virus (VEEV) represents a significant biothreat with no FDA-approved vaccine currently available, highlighting the need for alternative therapeutic strategies. Single-domain antibodies (sdAbs) present a potential alternative to conventional antibodies, due to their small size and ability to recognize cryptic epitopes.</p><p><strong>Methods: </strong>This research describes the development and preliminary evaluation of VEEV-binding sdAbs generated using a generative artificial intelligence (AI) platform. Using a dataset of known alphavirus-binding sdAbs, the AI model produced sequences with predicted affinity for the E2 glycoprotein of VEEV. These candidate sdAbs were expressed in a bacterial periplasmic system and purified for initial assessment.</p><p><strong>Results: </strong>Enzyme-linked immunosorbent assays (ELISAs) indicated binding activity of the sdAbs to VEEV antigens. In vitro neutralization tests suggested inhibition of VEEV infection in cultured cells for some of the candidates.</p><p><strong>Conclusions: </strong>This study demonstrates how generative AI can expedite antiviral therapeutic development and establishes a framework for quick responses to emerging viral threats when extensive example databases are unavailable. Additional refinement and validation of AI-generated sdAbs could establish effective VEEV therapeutics.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 2","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-05-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12101358/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144126108","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":"Purification of Human Immunoglobulin G with Bathophenanthroline-Zn²⁺, -Fe²⁺, or -Cu²⁺ Complexes.","authors":"Thisara Jayawickrama Withanage, Ron Alcalay, Olga Krichevsky, Ellen Wachtel, Ohad Mazor, Guy Patchornik","doi":"10.3390/antib14020040","DOIUrl":"10.3390/antib14020040","url":null,"abstract":"<p><strong>Background/objectives: </strong>Pharmaceutical companies are aware of the ongoing effort to satisfy the increasing global demand for therapeutic-grade monoclonal antibodies (mAbs), an especially difficult challenge for poor and developing countries. We present a simple, economical, single-step purification approach at neutral pH for polyclonal human IgG (hIgG), which does not require any expensive ligands, chromatography columns, polymers, or membranes.</p><p><strong>Methods/results: </strong>Instead, porous precipitates of commercial, recyclable aromatic [bathophenanthroline:cation] complexes were found to efficiently capture impurity proteins from CHO cells or <i>E. coli</i> lysate while maintaining the majority of the highly concentrated hIgG (5-15 mg/mL) in the supernatant. [(Batho)₃:Zn²⁺] complexes were the most promising, resulting in hIgG with a purity of ≈95%, by SDS-PAGE. This purified hIgG is monomeric (by dynamic light scattering, DLS) and preserves the native secondary structure (by far UV circular dichroism spectroscopy, CD). The process yield is >90% (by densitometry) and is maintained after a 100-fold increase in the reaction volume, which required only proportional increases in reagents.</p><p><strong>Conclusions: </strong>Although Protein A chromatographic columns, the industry gold standard, have a limited binding capacity, are costly, and require familiarity with column maintenance, we are attempting, by our efforts, to help to produce a more efficient, simple, and economical purification platform.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 2","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-05-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12101337/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144126384","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":"Validation and Optimization of PURE Ribosome Display for Screening Synthetic Nanobody Libraries.","authors":"Bingying Liu, Daiwen Yang","doi":"10.3390/antib14020039","DOIUrl":"10.3390/antib14020039","url":null,"abstract":"<p><strong>Background/objectives: </strong>PURE (Protein synthesis Using Recombinant Elements), an ideal system for ribosome display, has been successfully used for nanobody selection. However, its limitations in nanobody selection, especially for synthetic nanobody libraries, have not been clearly elucidated, thereby restricting its utilization.</p><p><strong>Methods: </strong>The PURE ribosome display selection process was closely monitored using RNA agarose gel electrophoresis to assess the presence of mRNA molecules in each fraction, including the flow-through, washing, and elution fractions. Additionally, a real-time validation method for monitoring each biopanning round was implemented, ensuring the successful enrichment of target protein-specific binders. The selection process was further optimized by introducing a target protein elution step prior to the EDTA-mediated disassembly, as well as by altering the immobilization surfaces. Finally, the efficiency of PURE ribosome display was enhanced by replacing the spacer gene.</p><p><strong>Results: </strong>The efficiency of PURE ribosome display was merely 4% with an unfavourable spacer gene. Using this spacer gene, EGFP- and human fatty acid-binding protein 4-specific nanobodies from a synthetic nanobody library were we successfully identified through optimizing the selection process. Choosing a spacer gene less prone to secondary structure formation increased significantly its efficiency in displaying synthetic nanobody libraries.</p><p><strong>Conclusions: </strong>Implementing a target protein elution step prior to EDTA-mediated disassembly and modifying the immobilization surfaces effectively increase selection efficiency. For PURE ribosome display, efficiency was further improved using a suitable spacer gene, enabling the display of large libraries.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 2","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12101283/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144126437","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 Targeted Integration-Based CHO Cell Platform for Simultaneous Antibody Display and Secretion.","authors":"Jessica P Z Ng, Mariati Mariati, Jiawu Bi, Matthew Wook Chang, Yuansheng Yang","doi":"10.3390/antib14020038","DOIUrl":"10.3390/antib14020038","url":null,"abstract":"<p><strong>Objective: </strong>We developed a targeted integration-based CHO cell platform for simultaneous antibody display and secretion, enabling a streamlined transition from antibody library screening to production without requiring the re-cloning of antibody genes.</p><p><strong>Methods: </strong>The platform consists of a CHO master cell line with a single-copy landing pad, a helper vector expressing FLPe recombinase, and bi-functional targeting vectors. Recombinase-mediated cassette exchange was utilized to integrate targeting vectors into the landing pad. Bi-functional vectors were designed by incorporating a minimal furin cleavage sequence (mFCS), RRKR, and various 2A peptides between the heavy chain (HC) and a membrane anchor.</p><p><strong>Results: </strong>Incomplete cleavage at the mFCS and 2A sites facilitated the expression of both membrane-bound and secreted antibodies, while mutations in the 2A peptide produced a range of display-to-secretion ratios. However, a fraction of secreted antibodies retained 2A residues attached to the HC polypeptides. Further analysis demonstrated that modifying the first five amino acids of the 2A peptide significantly influenced furin cleavage efficiency, resulting in different display-to-secretion ratios for targeting vectors containing mFCS-2A variant combinations. To overcome this, we designed nine-amino-acid FCS variants that, when placed between the HC and membrane anchor, provided a range of display-to-secretion ratios and eliminated the issue of attached 2A residues in the secreted antibodies. Vectors with lower display levels proved more effective at distinguishing cells expressing high-affinity antibodies with closely matched binding affinities. The platform also demonstrated high sensitivity in isolating high-affinity antibody-expressing cells and supported robust antibody production.</p><p><strong>Conclusion: </strong>This targeted integration-based CHO platform enables efficient, in-format screening and production of antibodies with tunable display-to-secretion profiles. It provides a powerful and scalable tool for accelerating the development of functional, manufacturable therapeutic antibodies.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 2","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-04-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12101391/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144126190","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 Role of Monoclonal Antibodies as Therapeutics in HPV-Related Head and Neck Cancers: An Updated Review.","authors":"Michael Zalin, Shaan Patel, Carter Coggins, Vikrant Rai","doi":"10.3390/antib14020037","DOIUrl":"10.3390/antib14020037","url":null,"abstract":"<p><strong>Background/objectives: </strong>The increasing prevalence of human papillomavirus (HPV)-positive oropharyngeal squamous cell carcinoma (OPSCC) has necessitated a revaluation of therapeutic strategies. HPV-driven OPSCC differs from HPV-negative OPSCC due to its distinct molecular signatures, increased radiosensitivity, and better prognoses. However, despite these differences, treatment strategies have remained largely uniform, resulting in minimal reductions in morbidity and exposing HPV-positive patients to unnecessary toxicity. Monoclonal antibodies (mAbs) have become a promising therapeutic option due to their ability to target treatment with fewer systemic side effects. Immune checkpoint inhibitors (ICIs) such as pembrolizumab have shown efficacy in enhancing the immune response against tumors, while EGFR inhibitors like cetuximab offer an alternative modality. Current clinical trials aim to refine dosing regimens and identify combination strategies that may enhance therapeutic outcomes.</p><p><strong>Results: </strong>Despite promising evidence, several challenges hinder the widespread adoption of mAbs as a standard treatment for HPV-positive OPSCC in clinical practice. This review examines the current role of mAbs in HPV-positive OPSCC treatment, highlighting their limitations and future research directions.</p><p><strong>Conclusions: </strong>Further studies are needed to optimize patient selection, establish standardized treatment protocols, and investigate the long-term benefits of mAb-based therapies in this patient population.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 2","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-04-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12101214/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144126391","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":"Potentiating Antibody-Dependent Cellular Cytotoxicity in Triple-Negative Breast Cancer via the Humanized Anti-CD147 Antibody.","authors":"Kanyarat Thongheang, Thanathat Pamonsupornwichit, Kanokporn Sornsuwan, On-Anong Juntit, Tawan Chokepaichitkool, Weeraya Thongkum, Umpa Yasamut, Chatchai Tayapiwatana","doi":"10.3390/antib14020036","DOIUrl":"https://doi.org/10.3390/antib14020036","url":null,"abstract":"<p><strong>Background: </strong>Triple-negative breast cancer (TNBC) is an aggressive subtype with high metastatic potential, poor prognosis, and the absence of estrogen receptors, progesterone receptors, and human epidermal growth factor receptor 2 (HER2). The lack of these receptors limits the standard treatments, such as hormone therapies and HER2-targeted antibodies like trastuzumab. These challenges highlight the critical need for novel therapeutic strategies. CD147, a transmembrane glycoprotein overexpressed in TNBC, promotes tumor progression, metastasis, and chemoresistance, making it a promising therapeutic target. This study evaluates the antibody-dependent cellular cytotoxicity (ADCC) of HuM6-1B9, a humanized anti-CD147 antibody, against MDA-MB-231 cells, a TNBC model.</p><p><strong>Methods: </strong>CFSE-labelled MDA-MB-231 cells were co-cultured with PBMCs as effector cells (E:T ratio 80:1) in the presence of HuM6-1B9 and incubated for 4 h. Cells were then collected and stained with PI, and CFSE+/PI+ dead target cells were analyzed by flow cytometry.</p><p><strong>Results: </strong>Co-culturing MDA-MB-231 cells with peripheral blood mononuclear cells (PBMCs) in the presence of HuM6-1B9 demonstrated effective ADCC induction without direct cytotoxicity. HuM6-1B9 induced 54.01% cancer cell death via ADCC, significantly outperforming trastuzumab (26.14%) while sparing PBMCs.</p><p><strong>Conclusion: </strong>These findings support HuM6-1B9 as a prospective TNBC therapeutic and warrant further investigation into its clinical potential.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 2","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-04-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12015854/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143965499","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 Comprehensive Review About the Use of Monoclonal Antibodies in Cancer Therapy.","authors":"Angel Justiz-Vaillant, Bijay Raj Pandit, Chandrashekhar Unakal, Sehlule Vuma, Patrick Eberechi Akpaka","doi":"10.3390/antib14020035","DOIUrl":"https://doi.org/10.3390/antib14020035","url":null,"abstract":"<p><p>Monoclonal antibodies (mAbs) targeting various pathways in cancer therapy play crucial roles in enhancing the immune system's ability to recognise and eliminate tumour cells. These therapies are designed to either block inhibitory immune checkpoint pathways or to target specific tumour cell markers for direct destruction. Additionally, mAbs can modulate the tumour microenvironment, enhance antibody-dependent cellular cytotoxicity, and inhibit angiogenesis, further amplifying their therapeutic impact. Below is a summary of monoclonal antibodies targeting key pathways, along with their indications and mechanisms of action, which are reviewed based on therapeutic mechanisms.</p>","PeriodicalId":8188,"journal":{"name":"Antibodies","volume":"14 2","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-04-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12015915/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143954996","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}