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How the phage display technology is boosting the production of valuable bispecific antibodies
Bispecific antibodies are valuable therapeutics due to their unique ability to engage different epitopes or antigens and thus modulate the immune response. But their production remains challenging due to the frequent misassembly of the different antibody chains. Antibody phage display platforms for therapeutic applications may soon change that, as more and more scientists develop unique ways to engineer these antibodies for optimal production.
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How advanced monoclonal antibody generation methods are improving conventional envenoming treatments
Snakebite envenoming has been on WHO’s priority list of neglected tropical diseases since 2017. Due to the complexity and variability of the toxins transmitted by the bite of venomous snakes, traditional treatment methods rely on snake antivenoms. The production of these antivenoms has remained virtually unchanged since the 1800s and it consists of the hyperimmunization of large animals (i.e. horses) with snake venom and harvesting their antibody-enriched plasma for treatment. The process is time-consuming, expensive, and often results in harmful side effects. In this context, monoclonal antibody generation methods are emerging as an alternative. Specifically, antibody phage display platforms for therapeutic applications are increasingly sought-after due to being a cost-effective approach for the development of better treatments.
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What are the leading monoclonal antibody treatments for cancer?
Arresting cancer progression has evolved from the use of unspecific chemotherapies with serious adverse effects to the adoption of antibody-based targeted therapies. Present monoclonal antibody treatments for cancer mainly comprise the use of growth-targeting antibodies (e.g. Trastuzumab and Cetuximab) and, more recently, the use of immune checkpoint inhibitors (e.g. Ipilimumab and Utomilumab) known enhancers of the immune response against cancer cells. Many of these drugs were discovered using antibody phage display adapted to therapeutic applications. Despite the complexity of the disease, antibodies have become invaluable anticancer agents due to their specificity, reduced toxicity, and low risk of causing drug resistance, and they are expected to continue providing the safest way to fight this pervasive disease.
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“Cell-based phage display is helping us isolate more biologically relevant antibodies”
Dr. Mohamed Alfaleh is an assistant professor at King Abdulaziz University (Faculty of Pharmacy, Jeddah, Saudi Arabia). Pharmacist by training, he completed his PhD studies in biotechnology at the University of Queensland (Australia). Shortly after, he joined the Vaccine and Immunotherapy Unit at King Fahd Medical Research Center at King Abdulaziz University, where he continues to develop and engineer monoclonal antibodies targeting specific cells’ markers using phage display technologies adapted to therapeutic applications.
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Essential antibody library generation and display technologies for the discovery of new reagents and biopharmaceuticals
Library generation is a vital first step in any antibody phage display project for therapeutic applications and others. Libraries exist in different types and formats, and they can be built from different host species. But the success of any antibody discovery project relies, first and foremost, on the underlying quality of the library used for screening, the choice and design of an adequate antigen, and the criteria used for antibody validation.
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Will a single COVID-19 drug be enough to treat all patients?
As more and more biotherapeutics enter the early stages of clinical development, scientists are questioning if current approaches will be sufficient to curb the pandemic. On the one hand, anti-inflammatory and immunosuppressant drugs, that benefit only a subgroup of patients, are leading the race for clinical approval. On the other hand, anti-SARS-CoV-2 antibodies are mostly focusing on a single region of the virus, severely compromising our chances of finding the best candidates.
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Will camelid antibodies offer a solution to solve the COVID-19 pandemic?
The emergence of the zoonotic pathogen, SARS-CoV-2, resulted in a global pandemic and caused the deaths of hundreds of thousands of people. After SARS-CoV-1 and MERS-CoV, this strain is the third known to have spilled from wild animal reservoirs with severe consequences to the human population. But prior studies with these zoonotic viruses may have paved the way for the development of innovative treatments such as the use of camelid antibodies as neutralizing agents of SARS-CoV-2.
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Does secondary antibody production need to be animal-dependent? How researchers are challenging conventional methodologies
Secondary antibody production has remained largely unchanged for the past decades. These molecules are still commonly produced by harvesting the serum of large animals. A practice that continues to raise important concerns regarding animal welfare. As antibody production continues to shift from animal-dependent to animal-free methods, scientists continue to surprise us in the search for better and more exciting solutions.
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Challenges and considerations in primary antibody production for medical imaging
The term primary antibody is commonly used to describe antigen-binding antibodies with use for research and diagnostics. However, primary antibodies used for medical imaging are special. Besides requiring low toxicity and antigenicity, they also need to be able to persist in the human organism for long enough to reach their target. Interestingly, clinical researchers are increasingly aware that these antibodies may actually hold the key to understand why many immunotherapies fail.
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How camelid heavy-chain antibodies intensified the development of antibody engineering techniques
The discovery of functional antibody fragments and heavy-chain antibodies has intensified and propelled the development of innovative antibody engineering techniques. Through the use of these techniques, researchers have continued to challenge the canonical structure of antibodies to make them more stable and facilitating their diffusion across tissues. These efforts are paving the way for the development of more effective immunotherapies.
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