Biointron的动态

Monoclonal Antibody vs Polyclonal Antibody in Biomedical Research Both monoclonal and polyclonal antibodies are indispensable tools in biomedical research, but they differ greatly in their production, specificity, and applications. Monoclonal antibodies (mAbs) are produced by identical immune cells cloned from a single parent cell, making them highly specific for a single epitope on an antigen. This specificity allows for precise targeting in research, diagnostic, and therapeutic applications. In biomedical research, mAbs are particularly valuable in techniques such as western blots, immunohistochemistry (IHC), and flow cytometry, where detection of a specific protein or antigen is critical. Their consistency across experiments makes mAbs a top choice for applications that require reproducibility and accuracy. Polyclonal antibodies (pAbs), on the other hand, are produced from multiple B cell clones, resulting in a mixture of antibodies that recognize multiple epitopes on the same antigen. This diversity is extremely useful in studies that require reliable detection of a target, such as in immunoprecipitation, enzyme-linked immunosorbent assays (ELISAs), and certain diagnostic tests. pAbs are able to bind to multiple epitopes, which increases the possibility of antigen detection even when some epitopes are masked or altered, making them more flexible in detecting antigens in different contexts. However, due to the polyclonal nature of pAbs, batch-to-batch variability can lead to inconsistent experimental results. In contrast, mAbs are consistent and better suited for applications that require precise quantitation and minimal cross-reactivity. In summary, monoclonal antibodies offer unparalleled specificity and consistency, while polyclonal antibodies offer robustness and versatility. The choice between mAbs and pAbs depends on the specific requirements of the study, with each type offering different advantages. References [1] Neil Lipman et al., ILAR J 2005 (10.1093/ilar.46.3.258) [2] Michele Busby et al., Epigenetics Chromatin 2016 (10.1186/s13072-016-0100-6) [3] Anchal Singh et al., Animal Biotechnology 2020 (https://lnkd.in/dYZG47t2) #MonoclonalAntibodies #PolyclonalAntibodies #BiomedicalResearch #Immunology #Diagnostics #AntibodyApplications #LabTools

In a newly posted pre-print, The University of Georgia authors report that one N-glycan regulates natural killer cell antibody-dependent cell-mediated cytotoxicity and modulates Fc γ receptor IIIa / CD16a structure. From the abstract: Both endogenous antibodies and a subset of antibody therapeutics engage Fc gamma receptor (FcγR)IIIa / CD16a to stimulate a protective immune response.?To define the role of individual amino acid and N-glycan residues we measured affinity using multiple FcγRIIIa glycoforms. We observed stepwise affinity increases with each glycan truncation step with the most severely truncated glycoform displaying the highest affinity. Removing the N162 glycan demonstrated its predominant role in regulating antibody-binding affinity, in contrast to four other FcγRIIIa N-glycans. We next evaluated the impact of the N162 glycan on NK cell ADCC. NK cells expressing the FcγRIIIa V158 allotype exhibited increased ADCC following kifunensine treatment to limit N-glycan processing. Notably, an increase was not observed with cells expressing the FcγRIIIa V158 S164A variant that lacks N162 glycosylation, indicating the N162 glycan is required for increased NK cell ADCC. To gain structural insight into the mechanisms of N162 regulation, we applied a novel protein isotope labeling approach in combination with solution NMR spectroscopy. FG loop residues proximal to the N162 glycosylation site showed large chemical shift perturbations following glycan truncation. These data support a model for the regulation of FcγRIIIa affinity and NK cell ADCC whereby composition of the N162 glycan stabilizes the FG loop and thus the antibody-binding site. https://lnkd.in/efkaCuki

Monoclonal #antibodies are important for treating viral #infections, especially during pandemics. Antibody-secreting cells (ASCs) are a great source for these antibodies, but current methods to study them are either slow, expensive, or technically difficult. A recent research presents a new, simple technology to quickly discover monoclonal antibodies from ASCs. It combines microfluidic encapsulation and antigen bait sorting. Using this technology, researchers were able to find antibodies against SARS-CoV-2 with high affinity and neutralizing capacity in just two weeks, with a high success rate . This new approach makes it easier to study ASCs, which can lead to faster antibody discovery and better understanding of how protective antibodies are made. ___ Rapid discovery of monoclonal antibodies by microfluidics-enabled FACS of single pathogen-specific antibody-secreting cells | Nature Biotechnology https://lnkd.in/dfChYycU

This article published in Nature one month ago looks exciting to us. The following is the abstract of this paper. “Cancer cells require high levels of iron for rapid proliferation, leading to significant upregulation of cell-surface transferrin receptor 1 (TfR1), which mediates iron uptake by binding to the iron-carrying protein transferrin1,2,3. Leveraging this phenomenon and the fast endocytosis rate of TfR1 (refs. 4,5), we developed transferrin receptor targeting chimeras (TransTACs), a heterobispecific antibody modality for membrane protein degradation. TransTACs are engineered to drive rapid co-internalization of a target protein of interest and TfR1 from the cell surface, and to enable target protein entry into the lysosomal degradation pathway. We show that TransTACs can efficiently degrade a diverse range of single-pass, multi-pass, native or synthetic membrane proteins, including epidermal growth factor receptor, programmed cell death 1 ligand 1, cluster of differentiation 20 and chimeric antigen receptor. In example applications, TransTACs enabled the reversible control of human primary chimeric antigen receptor T cells and the targeting of drug-resistant epidermal growth factor receptor-driven lung cancer with the exon 19 deletion/T790M/C797S mutations in a mouse xenograft model. TransTACs represent a promising new family of bifunctional antibodies for precise manipulation of membrane proteins and targeted cancer therapy.” Chinese Antibody Society is an independent non-profit, non-government global professional organization with focus upon antibody-based therapeutics. Our society’s official journal, Antibody Therapeutics is an international peer-reviewed, open access journal published by Oxford University Press, and is indexed by ESCI, PubMed and Scopus (2023 CiteScore: 8.7). You are welcome to visit the official website of the journal (see link below) and submit your therapeutic antibody related manuscripts to our journal. https://lnkd.in/gsTu_U2 #antibodies #antibody #antibodytherapeutics #mabs #mab #biologics #proteindegradation

Antibody Therapeutics, official journal of Chinese Antibody Society, published by Oxford University Press, has been indexed by ESCI, PubMed and Scopus (2023 CiteScore: 8.7). Here, we would like to highlight Top 10 most cited articles published in 2022. The 1st paper entitled “The global landscape of approved antibody therapies” was contributed by Hongyu Zhang and Bo Liu from Umabs Therapeutics. Antibody therapies have become an important class of therapeutics in recent years as they have exhibited outstanding efficacy and safety in the treatment of several major diseases including cancers, immune-related diseases, infectious disease and hematological disease. Here, researchers have collected available data from the UMABS Antibody Therapies Database (Umabs-DB) as of 30 June 2022, outlined the global landscape of the approved antibody therapies with respect to the regulation agencies, therapeutic targets and indications, aiming to provide an insight into the trends of the global development of antibody therapies. The article has been cited 65 times as of today. Click the link for the free access of the full text of the article: https://lnkd.in/eBBNKPav We are also welcoming therapeutic antibody related submission through https://lnkd.in/dMJjtiD #Antibody #Therapeutics #Top10

In a recently published paper, Roche authors and colleagues report an experimental platform to de novo identify interactomes of TCR-like antibodies directly in human tissues using mass spectrometry. From the abstract: As proof of concept, we confirm the target epitope of a MAGE-A4-specific TCR-like antibody. We further determine cross-reactive peptide?sequences for ESK1, a TCR-like antibody with known off-target activity, in human liver tissue. We confirm off-target-induced T cell activation and ESK1-mediated liver spheroid killing. Off-target sequences feature an amino acid motif that allows a structural groove-coordination mimicking that of the target peptide, therefore allowing the interaction with the engager molecule. We conclude that our strategy offers an accurate, scalable route for evaluating the non-clinical safety profile of TCR-like antibody therapeutics prior to first-in-human clinical application. #mabs https://lnkd.in/ewmXUzDF

Advances in protein engineering, together with new technologies such as AI/ML, are driving the next wave of immunotherapies across multiple modalities and indications. Join PEGS BOSTON's 9th Annual Advances in Immunotherapy conference, on May 13-14, 2024 for the latest developments in cancer vaccines, overcoming the tumor microenvironment, combination therapies, the role of AI/ML is targeting solid tumors, plus effective strategies to mitigate resistance and toxicity in CAR Ts. Examples will come from the world of proteins, antibodies, cancer vaccines, cell-based therapies, and extracellular vesicles. https://lnkd.in/dsq5K2zz ??? Featured Presentations: "Vaccine-Boosted CAR T Crosstalk with Host Immunity to Reject Tumors with Antigen Heterogeneity" by Dr. Leyuan Ma "Personalized Cancer Vaccines – The Future?" by Dr. Andrew Allen "Advances in Cancer Treatments: From Immunotherapy to Vaccines and Almost Everything in Between" by Dr. Nageatte Ibrahim, M.D. "Non-Coding RNA Expression in Extracellular Vesicles and Chronic Inflammation in Cancer" by Laszlo Radvanyi The PEGS Boston Summit brings together leading experts at the forefront of biologics innovation, providing insights into the latest technologies, research, and advancements in drug development, protein and antibody engineering, immunotherapy, immunogenicity, expression platforms, multispecific antibodies, machine learning and AI in biologics, and more. PEGS Boston features main conference sessions as well as deep dive training seminars and topic-focused short courses. PEGS Boston Summit is your number one resource for protein engineering updates and is the conference to attend in 2024 to network, collaborate, and learn from the industry's best. #PEGSUMMIT #Immunotherapy #CancerResearch #Healthtech #AdvancesInImmunotherapy #CancerTreatmentInnovations #AIinHealthcare #CellTherapy #CancerVaccines #CAR-T

? Circular RNA: Vaccines, therapeutics and biomarkers could be revolutionized? #mRNA has revolutionized the drug development space, especially with the development of the #COVID-19 vaccine. However, the discovery of circular RNA (circRNA) is opening up new possibilities. Their closed loop structure makes it a more stable, longer lasting vaccine candidates than the linear form. Circio Holding ASA , is exploring the possibilities of universal flu vaccine. Erik Digman Wiklund, CEO says even though there are reduced dosing needs it wont be a “one and done” like Vertex Pharmaceuticals Casgevy, used to treat the blood disorders beta thalassaemia and sickle cell disease. He says it will take time but is hopeful it will be the next big breakthrough. Nikolaus Rajewsky lab, in the center for molecular medicine in Berlin, is looking at circRNAs potential as a biomarker for degenerative disease, allowing for earlier detection. https://lnkd.in/eytMqgn6.

Excited to share a new paper from a fun collaboration between my lab, the Mark Grinstaff lab, and the Florian Douam lab. I want to thank the first authors, Joshua McGee, Jack Kirsch, and other team members, for their hard work. "The use of modified nucleotides to suppress the interferon response and maintain translation of self-amplifying RNA (saRNA), which has been achieved for mRNA, has not yet succeeded. We identify modified nucleotides that, when substituted at 100% in saRNA, confer innate immune evasion and robust long-term protein expression, and when formulated as a vaccine, protect against lethal SARS-CoV-2 challenge in mice. This discovery advances saRNA therapeutics by enabling prolonged protein expression at low doses." https://lnkd.in/eRAMFpic

Day 17 of me talking about some of the work scientists around the world are doing with the coolest molecules in science, Recombinant camelid antibodies or better known as nanobodies. Todays paper is one of my favourite papers of work done with nanobodies. Anyone who knows me is aware that probably one of my preferred topics to talk about is antibody drug conjugates (ADC's) and how nanobodies are ideal for this form of therapeutic modality and are going to be a big growth area over the next five/ten years in biopharma. The work done in todays paper by a group of scientists mostly based in the Netherlands nicely confirms my view. Todays scientists developed nanobodies to target the platelet derived growth factor B receptor (PDGFB). They obtained the nanobodies from an immune library (more on that later). After obtaining a variety of nanobodies that targeted PDGFB they then attached the cytotoxin, Auristatin F in a site specific manner to their different nanobodies, thus creating an ADC. Once this work was completed they then added it to cells that express PDGFB and were able to show that their ADC was able to kill cells. An important property if for example one wants to target cancer cells. However it should also be noted that this same concept could be used to deliver other things to cells other than toxins...... Importantly in this paper the authors also found that different PDGFB targeting nanobodies that they isolated from their immune libraries displayed varying internalization rates?and thus cell death rates. This could be very beneficial for finetuning in vivo treatment doses for specific needs. Enjoy reading through the paper and see how the clever scientists did their work. If you would like to start doing similar work or get started working with nanobodies then let me know as Afrobodies is running a "back to school" September special where for just $12,000 you get two custom immune nanobody libraries developed for you. Neve before has it been so affordable to work with high quality custom immune nanobody libraires. As shown in todays research paper, custom immune nanobody libraries are excellent tools for discovering nanobodies with very useful properties. Therefore done waste time and get your order in :) #vhh #alpacas #biotech #singledomain #nanobodies #afrobodies #nanobody https://lnkd.in/e5sBAzr6