Tracks all antibody and nanobody related therapeutics recognized by World Health Organisation, and identifies any corresponding structures in Structural Antibody Database with near exact or exact variable domain sequence matches. Synchronized with SAbDab to update weekly, reflecting new Protein Data Bank entries and availability of new sequence data published by WHO.

The antibody repertoire is a critical component of the adaptive immune system and is believed to reflect an individual’s immune history and current immune status. Delineating the antibody repertoire has advanced our understanding of humoral immunity, facilitated antibody discovery, and showed great potential for improving the diagnosis and treatment of disease. However, no tool to date has effectively integrated big Rep-seq data and prior knowledge of functional antibodies to elucidate the remarkably diverse antibody repertoire. We developed a Rep-seq dataset Analysis Platform with an Integrated antibody Database (RAPID; https://rapid.zzhlab.org/), a free and web-based tool that allows researchers to process and analyse Rep-seq datasets. RAPID consolidates 521 WHO-recognized therapeutic antibodies, 88,059 antigen- or disease-specific antibodies, and 306 million clones extracted from 2,449 human IGH Rep-seq datasets generated from individuals with 29 different health conditions. RAPID also integrates a standardized Rep-seq dataset analysis pipeline to enable users to upload and analyse their datasets. In the process, users can also select set of existing repertoires for comparison. RAPID automatically annotates clones based on integrated therapeutic and known antibodies, and users can easily query antibodies or repertoires based on sequence or optional keywords. With its powerful analysis functions and rich set of antibody and antibody repertoire information, RAPID will benefit researchers in adaptive immune studies.

A dataset of ~500 antibodies with binding affinity: antibody sequence, antigen sequence, Kd. Obtained from SAbDab via Therapeutic Data Commons

Python code (get_antibody_affinity_data.py) and dataset (antibody_affinity_protein_sabdab.csv)

The use of serum containing polyclonal antibodies from animals immunized with toxins marked the beginning of the application of antibody-based therapy in late nineteenth century. Advances in basic research led to the development of the hybridoma technology in 1975. Eleven years later, the first therapeutic monoclonal antibody (mAb) was approved, and since then, driven by technological advances, the development of mAbs has played a prominent role in the pharmaceutical industry. In this review, we present the developments to circumvent problems of safety and efficacy arising from the murine origin of the first mAbs and generate structures more similar to human antibodies. As of October 2017, there are 61 mAbs and 11 Fc-fusion proteins in clinical use. An overview of all mAbs currently approved is provided, showing the development of sophisticated mAbs formats that were engineered based on the challenges posed by therapeutic indications, including antibody-drug conjugates (ADC) and glycoengineered mAbs. In the field of immunotherapy, the use of immunomodulators, bispecific mAbs and CAR-T cells are highlighted. As an example of promising therapy to treat infectious diseases, we discuss the generation of neutralizing monoclonal-oligoclonal antibodies obtained from human B cells. Scientific and technological advances represent mAbs successful translation to the clinic.

According to the cognitive market research, the global monoclonal antibody therapeutics market in terms of revenue was estimated to be worth xx billion in 2024 and is poised to reach xx billion by 2031, growing at a CAGR of xx% from 2024 to 2031.

Human monoclonal antibodies (mAb) dominated the market in 2022, with the human mAb segment holding the largest revenue share. This was attributed to the popularity of Humira (Adalimumab), a human monoclonal antibody widely used in the treatment of various conditions.
Human monoclonal antibodies (mAb) dominated the market in 2022, with the human mAb segment holding the largest revenue share. This was attributed to the popularity of Humira (Adalimumab), a human monoclonal antibody widely used in the treatment of various conditions.
The autoimmune diseases segment is expected to experience robust revenue growth, driven by technological advancements, government initiatives, and the use of monoclonal antibodies in treating autoimmune conditions.
The market witnessed substantial developments in 2023, with major players actively contributing to advancements in monoclonal antibody-based treatments. Notably, GlaxoSmithKline plc. (GSK) and iTeos Therapeutics announced a promising partnership for the development and commercialization of EOS-448, an anti-TIGIT monoclonal antibody, showcasing the potential for next-generation immuno-oncology therapies.

Market Dynamics of the Monoclonal Antibody Therapeutics Market

Key Drivers of the Monoclonal Antibody Therapeutics Market

Development and advanced technology improvement in monoclonal antibody engineering have a great impact on the monoclonal therapeutics market

The increasing importance of therapeutic mAbs is apparent, as mAbs have become the predominant treatment modality for various diseases over the past 25 years. During this time, major technological advances have made the discovery and development of mAb therapies quicker and more efficient. Other scientific and technological advances have also enabled the successful translation of mAbs to the clinic. Around the world, at least 570 therapeutic mAbs have been studied in clinical trials by commercial companies, and 79 therapeutic mAbs have been approved by the United States Food and Drug Administration (US FDA) and are currently on the market, including 30 mAbs for the treatment of cancer. Current antibody drugs have increasingly fewer adverse effects due to their high specificity. As a result, therapeutic antibodies have become the predominant class of new drugs developed in recent years. Over the past five years, antibodies have become the best-selling drugs in the pharmaceutical market, and in 2018, eight of the top ten bestselling drugs worldwide were biologics. One exceptional advance that accelerated the approval of therapeutic mAbs was the generation of humanized antibodies by the complementary-determining region (CDR) grafting techniques exceptional advances that accelerated the approval of therapeutic mAbs was the generation of humanized antibodies by the complementary-determining region (CDR) grafting technique. • For instance, in 2008, 48 new mAbs were approved, contributing to a total global market of 61 mAbs in clinical use at the end of 2017, according to the US FDA. Strikingly, a total of 18 new antibodies were granted approval by the US FDA from 2018 to 2019 – this number was tallied from information contained on various websites, including the antibody society, the database of therapeutic antibodies, and company pipelines and press releases. (Source:https://jbiomedsci.biomedcentral.com/articles/10.1186/s12929-019-0592-z)

Protein modification to increase the duration of action of monoclonal antibody therapeutics is a key component of the antibody market

Most of the strategies have been used for the extension of protein action and can be used for long-acting mAb formulations. Human serum albumin (HSA), Fc fusion, and PEGylation are some of the strategies that are beneficial for protein modification. Albumin is the most abundant protein in the blood and it is a multi-binding transporter protein produced by the liver. It has various binding capacities toward different insoluble and hydrophobic endogenous and exogenous ligands. Albumin has three domains (DI, DII, DIII) each having two subdomains (A and B) connected by a flexible loop. albumin–peptide fusion has ...

Protein-Protein, Genetic, and Chemical Interactions for Moldovan Loomis C (2023):AI-based antibody discovery platform identifies novel, diverse and pharmacologically active therapeutic antibodies against multiple SARS-CoV-2 strains curated by BioGRID (https://thebiogrid.org); ABSTRACT: A critical aspect of a successful pandemic response is expedient antibody discovery, manufacturing and deployment of effective lifesaving treatments to patients around the world. However, typical drug discovery and development is a lengthy multi-step process that must align drug efficacy with multiple developability criteria and can take years to complete. In this context, artificial intelligence (AI), and especially machine learning (ML), have great potential to accelerate and improve the optimization of therapeutics, increasing their activity and safety as well as decreasing their development time and manufacturing costs. Here we present a novel, cost-effective and accelerated approach to therapeutic antibody discovery, that couples AI-designed human antibody libraries, biased for improved developability attributes with high throughput and sensitive screening technologies. The applicability of our platform for effective therapeutic antibody discovery is demonstrated here with the identification of a panel of human monoclonal antibodies that are novel, diverse and pharmacologically active. These first-generation antibodies, without the need for affinity maturation, bind to the SARS-CoV-2 spike protein with therapeutically-relevant specificity and affinity and display neutralization of SARS-CoV-2 viral infectivity across multiple strains. Altogether, this platform is well suited for rapid response to infectious threats, such as pandemic response.IMPORTANCEExpedient discovery and manufacturing of lifesaving therapeutics is critical for pandemic response. The recent COVID pandemic has highlighted the current inefficiencies and the need for improvements. To this end, we present our therapeutic antibody discovery platform that couples artificial intelligence (AI) and innovative high throughput technologies, and we demonstrate its applicability to rapid response. This platform enabled the isolation, characterization, and rapid identification of effective broadly neutralizing SARS-CoV-2 antibodies with good developability attributes, anticipated to fit our current process development and manufacturing platform. As such, this would benefit cost-of-goods and improve therapeutic access to patients. The AI-derived antibodies represent an advantageous therapeutic modality that can be developed and deployed fast, thus well suited for rapid response to infectious threats, such as pandemic response.

epitope description:M301, K310, E375, S390,antigen name:Genome polyprotein,host organism:Mus musculus C57BL/6,antibody name:E98

Therapeutic antibodies are widely used to treat severe diseases. Most of them alter immune cells and act within the immunological synapse, an essential cell-to-cell interaction to direct the humoral immune response. Although many antibody designs are generated and evaluated, a high-throughput tool for systematic antibody characterization and function prediction is lacking. Here, we generate the largest publicly available imaging flow cytometry (IFC) data set of the human immunological synapse containing over 2.8 million images. This dataset is used to analyze class frequency and morphological changes under different immune stimulation. In addition to the dataset, we introduce the first comprehensive open-source framework, scifAI (single-cell imaging flow cytometry AI, https://github.com/marrlab/scifAI), for preprocessing, feature engineering, and explainable, predictive machine learning IFC data. Using scifAI, we analyze class frequency- and morphological changes under different immune stimulation. scifAI is universally applicable to IFC data and, given its modular architecture, straightforward to incorporate into existing workflows and analysis pipelines, e.g., for rapid antibody screening and functional characterization. Methods Cell line culture EBV-transformed B-lymphoblastoid cell line (B-LCL) from donor 333 was obtained from Astarte Biologics (# 1038-3161JN16) and cells were cultivated in RPMI-1640 medium (PAN-Biotech; cat # P04-17500) with 10% FBS (Anprotec; cat # AC-SM-0014Hi) and 2 mM L-glutamine (PAN-Biotech; cat# P04-80100). Immune synapse formation and imaging flow cytometry

To analyze immune synapses, human memory CD4+ T cells were isolated from PBMCs of nine healthy human donors using a negative selection EasySep Enrichment kit from STEMCELL Technologies (cat #19157). Live/dead staining of T and B-LCL cells was separately performed using the fixable viability dye eF780 for 15 min at RT (eBioscience; cat # 65-0865-14). Cells were then re-suspended in RPMI-1640 medium supplemented with 10% FBS (Anprotec; cat # AC-SM-0014Hi), 5% Penicillin-Streptomycin (Gibco; cat # 15140-122) and 2 mM L-glutamine (PAN-Biotech; cat # P04-80100). Afterward, B-LCL cells were transferred into a well of a 96-well round bottom plate (300.000 cells per well) and were pre-incubated with the superantigen Staphylococcal enterotoxin A (SEA) (Sigma-Aldrich; cat # S9399) for 15 min at 37°C or left untreated. Human CD4+ Tmem were added to the afore-prepared B-LCL cells (250.000 cells per well) to generate a final ratio of 4:3 (B-LCL:Tmem) and subsequently the appropriate in-house made compounds (10 µg/mL of Isotype Ctrl or Teplizumab and 1 µg/mL (5 nM) of Ctrl-TCB, CD19-TCB or CD20-TCB) were added to the B-LCL-Tmem cell co-culture. To strengthen the conjugate formation between B-LCL and T cells they were centrifuged at 300xg for 30 sec and then directly transferred to a 37°C incubator for 45 min. Thereafter, the medium in each well was carefully aspirated with a pipette and cells were immediately fixed for 12 min at RT followed by permeabilization using the Foxp3/Transcription factor staining buffer set from eBioscience (cat # 00-5523-00). Intracellular staining was performed in permeabilization buffer containing fluorescently-labeled antibodies for 40 min at 4°C: CD3-BV421 (clone UCHT1, Biolegend; cat # 300433), HLA-DR-PE-Cy7 (clone L243, Biolegend; cat # 307616), Phalloidin AF594 (ThermoFisher; cat # A12381) and P-CD3ζ Y142-AF647 (K25-407.69, BD cat # 558489). After washing, cells were suspended in FACS buffer (PBS supplemented with 2% FBS) and acquired on an Amnis ImageStreamX Mark II Imaging Flow Cytometer (Luminex) equipped with five lasers (405, 488, 561, 592 and 640 nm). On average, around 55,000 images were collected per sample at 60x magnification on a low-speed setting. IDEAS software (version 6.2.187.0, EMD Millipore) was used for data analysis and labeling of cells. To identify immune synapses using the IDEAS software the gating strategy in Supplementary Fig 1a was implemented. Cells were first gated on in-focus live+ CD3+ MHCII+ cells. Within this population images that show single CD3+ T cells and single MHCII+ B-LCL cells were selected using the area and aspect ratio feature. Next, to exclude non-interacting cells the CD3 intensity within a self-created synapse mask was determined. The synapse mask was defined as a combination of the morphology CD3 and MHCII mask with a dilation of 3. Only synapses that showed a CD3 signal in the mask were gated. Finally, T+B-LCL cells in one layer were excluded by using the height and area feature of the brightfield (BF) and single T-B-LCL synapses were analyzed.

The global market for NBN monoclonal antibodies is experiencing robust growth, driven by increasing prevalence of diseases requiring targeted therapies and advancements in antibody engineering technologies. While precise market sizing data is absent, considering the typical growth trajectories of niche therapeutic antibody markets and a reasonable CAGR of 15% (a conservative estimate given the potential of novel therapeutics), we can project a 2025 market value in the range of $150 million. This projection incorporates the influence of factors such as rising research and development investments, growing demand for personalized medicine, and the expanding application of monoclonal antibodies across various therapeutic areas. Key players like Sino Biological, Elabscience Biotechnology, and Wuhan Fine Biotech are contributing significantly, fostering innovation and competition within the market. Future growth will be propelled by ongoing clinical trials demonstrating efficacy and safety in treating specific diseases, as well as approvals for new indications and formulations. However, challenges remain, such as the high cost of development and manufacturing, stringent regulatory hurdles, and the potential for immunogenicity and adverse effects. Market segmentation based on application (e.g., research, diagnostics, therapeutics) and geography will be crucial for understanding growth patterns. Further research and development efforts focusing on improved antibody design, targeted drug delivery systems, and combination therapies hold the potential for substantial market expansion over the forecast period (2025-2033), potentially reaching a value exceeding $750 million by 2033, based on a sustainable CAGR. The market's competitive landscape, with established players and emerging biotech companies vying for market share, will continue to influence pricing strategies and overall market dynamics.

Protein-Protein, Genetic, and Chemical Interactions for Parray HA (2022):A broadly neutralizing monoclonal antibody overcomes the mutational landscape of emerging SARS-CoV-2 variants of concern. curated by BioGRID (https://thebiogrid.org); ABSTRACT: The emergence of new variants of SARS-CoV-2 necessitates unremitting efforts to discover novel therapeutic monoclonal antibodies (mAbs). Here, we report an extremely potent mAb named P4A2 that can neutralize all the circulating variants of concern (VOCs) with high efficiency, including the highly transmissible Omicron. The crystal structure of the P4A2 Fab:RBD complex revealed that the residues of the RBD that interact with P4A2 are a part of the ACE2-receptor-binding motif and are not mutated in any of the VOCs. The pan coronavirus pseudotyped neutralization assay confirmed that the P4A2 mAb is specific for SARS-CoV-2 and its VOCs. Passive administration of P4A2 to K18-hACE2 transgenic mice conferred protection, both prophylactically and therapeutically, against challenge with VOCs. Overall, our data shows that, the P4A2 mAb has immense therapeutic potential to neutralize the current circulating VOCs. Due to the overlap between the P4A2 epitope and ACE2 binding site on spike-RBD, P4A2 may also be highly effective against a number of future variants.

Defining predictors of antigen-binding affinity of antibodies is valuable for engineering therapeutic antibodies with high binding affinity to their targets. However, this task is challenging owing to the huge diversity in the conformations of the complementarity determining regions of antibodies and the mode of engagement between antibody and antigen. In this study, we used the structural antibody database (SAbDab) to identify features that can discriminate high- and low-binding affinity across a 5-log scale. First, we abstracted features based on previously learned representations of protein-protein interactions to derive ‘complex’ feature sets, which include energetic, statistical, network-based, and machine-learned features. Second, we contrasted these complex feature sets with additional ‘simple’ feature sets based on counts of contacts between antibody and antigen. By investigating the predictive potential of 700 features contained in the eight complex and simple feature sets, we observed that simple feature sets perform comparably to complex feature sets in classification of binding affinity. Moreover, combining features from all eight feature-sets provided the best classification performance (median cross-validation AUROC and F1-score of 0.72). Of note, classification performance is substantially improved when several sources of data leakage (e.g., homologous antibodies) are not removed from the dataset, emphasizing a potential pitfall in this task. We additionally observe a classification performance plateau across diverse featurization approaches, highlighting the need for additional affinity-labeled antibody-antigen structural data. The findings from our present study set the stage for future studies aimed at multiple-log enhancement of antibody affinity through feature-guided engineering.

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Alzheimer’s disease can cause dementia through brain matter degradation. This study investigates the monoclonal antibody usage for AD treatment, following PRISMA 2020 guidelines, and aims to discern the monoclonal antibody that offers the optimal balance of efficacy and safety for individuals with AD. A systematic search was conducted across databases such as PubMed, Cochrane Library, and clinical trial registries for randomized controlled trials. The quality of studies was assessed using the Cochrane risk of bias 2 tool. Cognitive function and daily activities were evaluated using MMSE, ADAS-Cog, and CDR-SB test data. According to CDR-SB measurements, lecanemab showed effectiveness in reducing brain amyloid and cognitive decline, with a change from baseline of 1.21. Aducanumab resulted in a decrease of −0.39 (−22%). Bapineuzumab showed no significant benefit, with scores of 2.4 (2.8). Gantenerumab, scoring 1.69 (1.37, 2.01), reduces amyloid, particularly in early Alzheimer’s stages. Crenezumab was ineffective, with a score of 3.61. The findings provide various perspectives. Lecanemab showed the most promise in brain amyloid reduction and decelerating cognitive decline compared to the other therapies. Further research is needed, highlighting the necessity of AD therapeutic research to alter AD’s trajectory and provide reliable treatment. www.crd.york.ac.uk/prospero identifier is CRD42024504358 This study investigates the safety and efficacy of treating Alzheimer’s disease (AD) with monoclonal antibodies. In order to determine which antibody could be most helpful, we looked over a number of trials. Several antibodies, such as lecanemab, solanezumab, aducanumab, bapineuzumab, gantenerumab, and crenezumab, were the subject of the study. According to our research, lecanemab is particularly effective at lowering brain amyloid plaques and delaying cognitive deterioration, two major problems associated with Alzheimer’s disease. Other antibodies, such as solanezumab and bapineuzumab, had little to no beneficial effects, making their benefits less evident. The contradictory results of aducanumab indicate that further research is necessary to ascertain its actual efficacy. When administered at the earliest stages of Alzheimer’s disease or when used at a higher dose, crenezumab may be beneficial. Even though lecanemab seems promising, research in this field is still in its infancy. To validate these results and get further insight into the potential applications of these medicines in the management of Alzheimer’s disease, additional research is required. In summary, this study emphasizes the necessity of ongoing research to discover trustworthy treatments for AD patients.

Chemical cross-linking coupled with mass spectrometry (CXMS) offers the distance constraints critical for building the structural model of protein and protein complexes and understanding dynamics of biological systems. Originally developed for protein structural models, CXMS has evolved into method for studying protein complex formation, ligand-induced conformational changes, and quantitative structural analysis using isotopically labeled cross-linkers. In this study we tested the potential of isotopically labeled MS-cleavable cross-linker to track the stability of the therapeutic monoclonal antibodies. A novel isotopically labeled MS-cleavable cross-linker was synthesized, and its reactivity was successfully tested on peptide and protein standards. Further, the novel cross-linker was utilized to test the stability of selected therapeutical monoclonal antibodies, bevacizumab and trastuzumab, adopting the data-independent acquisition. This study reports the advantages of using combination of 13C isotopically labeled MS-cleavable cross-linkers and data-independent mass spectrometry analysis for the automated identification of cross-linked products and thus monitoring the structural rearrangement of protein structure.

BackgroundSeveral monoclonal antibodies (mAbs) recognising Lewisy, such as BR96, have reached the clinic but have failed to show good anti-tumour responses with an acceptable level of toxicity. No Lewisb mAbs have been trialled in patients. In this study we compare the specificity of three mAbs; BR96 (Lewisy), 2-25 LE (Lewisb) and 692/29 that recognises a unique facet of both Lewisy and Lewisb. We then assessed the in vivo therapeutic effect of 692/29 using xenograft models. Methodology/Principal FindingsUsing a glycan array, each mAb was shown to display a different binding pattern with only 692/29 binding to both Lewisy and Lewisb. 692/29 was able to kill tumour cells over-expressing Lewisy/b directly, as well as by antibody and complement mediated cytotoxicity (ADCC/CDC), but failed to kill cells expressing low levels of these haptens. In contrast, BR96, directly killed cells expressing either high or low levels of Lewisy perhaps explaining its toxicity in patients. 2-25 LE failed to cause any direct killing but did mediate ADCC/CDC. Both 692/29 and BR96 bound to >80% of a panel of over 400 colorectal tumours whereas 2-25 LE showed lower reactivity (52%). 692/29 demonstrated more restricted normal tissue reactivity than both BR96 and 2-25 LE. 692/29 anti-Lewisy/b mAb also showed good in vivo killing in xenograft models. Conclusions/SignificanceMAbs targeting both Lewisy and Lewisb may have a therapeutic advantage over mAbs targeting just one hapten. 692/29 has a more restricted normal tissue distribution and a higher antigen threshold for killing which should reduce its toxicity compared to a Lewisy specific mAb. 692/29 has an ability to directly kill tumours whereas the anti-Lewisb mAb does not. This suggests that Lewisy but not Lewisb are functional glycans. 692/29 showed good anti-tumour responses in vivo and is a strong therapeutic candidate.

Protein-Protein, Genetic, and Chemical Interactions for James LC (1999):1.9 A structure of the therapeutic antibody CAMPATH-1H fab in complex with a synthetic peptide antigen. curated by BioGRID (https://thebiogrid.org); ABSTRACT: CAMPATH-1 antibodies have a long and successful history in the treatment of leukaemia, autoimmune disease and transplant rejection. The first antibody to undergo "humanisation", CAMPATH-1H, permits treatment with limited patient anti-globulin response. It recognises the CD52 antigen which is a small glycosylphosphatidylinositol(GPI)-anchored protein expressed on lymphocytes and mediates cell depletion. We present the 1.9 A structure of the CAMPATH-1H Fab complexed [corrected] with an analogue of the antigenic determinant of CD52. Analysis of the CAMPATH-1H binding site reveals that in contrast to most antibodies CDR L3 plays a dominant role in antigen binding. Furthermore CDR H3, which is essential for effective antigen recognition in most antibodies, participates in only two main-chain interactions in CAMPATH-1H. The CAMPATH-1H binding site is highly basic; ionic interaction with the enthanolamine phosphate of the CD52 GPI anchor has long been hypothesised to be important in antigen binding. The structure reveals a number of important specific ionic interactions, including Lys53H but not Lys52bH as had previously been suggested. Prolonged treatment with CAMPATH-1H can lead to patient anti-idiotype responses which may be exacerbated by the unusually high number of basic residues in the antibody. This suggests that a strategy where redundant basic residues are replaced with neutral counterparts may be effective in further reducing the immunogenicity of this versatile and widely used antibody.

Raw data from the paper "Structural trends in antibody-antigen binding interfaces: a computational analysis of 1833 experimentally determined 3D structures". The files contain the raw contact points extracted using the Python script as described in the paper. The data also contains a reference file with the atoms in the pdb files not considering if they are contact points or not.

The Bai3 PAb market, while lacking precise figures in the provided data, shows significant promise based on the presence of numerous key players and a stated study period extending to 2033. The involvement of established companies like Thermo Fisher Scientific, Merck Millipore, and Abcam indicates a robust and competitive landscape, suggesting a market likely in the hundreds of millions of dollars in 2025. Considering a typical CAGR in the biotechnology sector of 5-10%, and extrapolating from the stated study period (2019-2033), a conservative estimate would place the 2025 market size at approximately $250 million, with a potential CAGR of 7% projected for the forecast period (2025-2033). Market drivers likely include increasing demand for targeted therapies, advancements in antibody engineering, and growth in research and development across various therapeutic areas. Trends will likely follow broader biotech industry shifts towards personalized medicine, an increased focus on early-stage diagnostics, and an expansion of partnerships and collaborations between large pharma and smaller biotech firms. Market restraints might include regulatory hurdles related to novel antibody therapies, the high cost of research and development, and potential competition from alternative therapeutic approaches. The significant number of companies involved, spanning both large multinational corporations and smaller specialized biotechs, signifies a healthy level of competition and innovation. The geographical distribution (while not explicitly provided) can be inferred to be heavily concentrated in regions with strong biotech ecosystems, such as North America, Europe, and parts of Asia (China, in particular, given the presence of several Chinese companies in the list). Further market segmentation (not detailed in the provided data) would likely involve distinctions based on therapeutic application (e.g., oncology, immunology, neurology), antibody type (e.g., monoclonal, bispecific), and end-user (e.g., research institutions, pharmaceutical companies). The long forecast period suggests a strong belief in the continued growth and relevance of Bai3 PAb in the coming years.

Monoclonal antibodies (mAbs) are widely applied as highly specific and efficient thera-peutic agents for various diseases, including cancer, inflammatory and autoimmune diseases. As protein production in cellular systems inherently generates a multitude of molecular variants, manufacturing of mAbs requires stringent control in order to ensure safety and efficacy of the drug. Moreover, monitoring of mAb variants in the course of the fermentation process may allow instant tuning of process parameters to maintain optimal cell culture conditions. Here, we describe a fast and robust workflow for the characterization of mAb variants in fermentation broth. Sample preparation is minimal in that the fermentation broth is shortly centrifuged before dilution and HPLC-MS analysis in a short 15-min gradient run. In a single analysis, N-glycosylation and truncation variants of the expressed mAb can be identified at the intact protein level. The molecular attributes of the expressed therapeutic protein may thus be continuously monitored to ensure the desired product profile. Simultaneously, absolute quantification of mAb content in fermentation broth yielded concentrations of 67 and 2578 ng.mL-1 at the beginning and end of fermentation, respectively. The whole workflow features excellent robustness as well as retention time and peak area stability of 0.3% and 4.9% RSD. Additional enzymatic removal of N-glycans enables determination of mAb glycation levels, which are subsequently considered in relative N-glycoform quantification to correct for isobaric galactosylation. Application of the described workflow in an industrial environment may therefore substantially enhance in-process control in mAb production as well as targeted biosimilar development.

This study investigates the biodistribution of a therapeutic antibody from serum to urine across the kidney endothelial barrier, contextualizing the findings with existing literature. Our analysis shows the quantitative correlation between serum levels of the intravenously administered antibody rituximab and its urinary concentration, indicating a predictable pharmacokinetic profile. The results align with previous quantitative studies on the biodistribution of endogenous and vaccination induced IgG between serum and urine, confirming that recombinant therapeutic IgG1 passes the kidney endothelial barrier and exhibits similar biodistribution to endogenous IgG. These insights may inform the determination of optimal dosages for therapeutic antibodies targeting the urothelium or renal epithelium.