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Single-domain antibodies applied as antiviral immunotherapeutics
Journal of Virological Methods, 2023Viral infections have been the cause of high mortality rates throughout different periods in history. Over the last two decades, outbreaks caused by zoonotic diseases and transmitted by arboviruses have had a significant impact on human health. The emergence of viral infections in different parts of the world encourages the search for new inputs to ...
Nidiane Dantas Reis, Prado +12 more
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Multivalent Display of Single-Domain Antibodies
2012Antigen-binding fragments, such as single-domain antibodies (sdAbs), can now be readily isolated by in vitro technologies. Antibody fragment libraries derived from immune or nonimmune sources are presented in a molecular display format, typically phage display, and binders to individual antigens are selected from the libraries by a so-called panning ...
Zhang, J., MacKenzie, C.R.
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Production of Single-Domain Antibodies in Pichia pastoris
2022Single-domain antibodies (sdAbs) are binders that consist of a single immunoglobulin domain. SdAbs have gained importance as therapeutics, diagnostic reagents, and research tools. Functional sdAbs are commonly produced in Escherichia coli, which is a simple and widely used host for production of recombinant proteins. However, there are drawbacks of the
Yusei, Matsuzaki +3 more
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Humanization of Camelid Single-Domain Antibodies
2022Humanization of therapeutic antibodies derived from animal immunizations is often required to minimize immunogenicity risks in humans, which can cause potentially harmful and serious side effects and reduce antibody efficacy. Humanization is typically applied to conventional monoclonal antibodies derived in rodents as well as single-domain antibodies ...
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Improving the targeting of therapeutics with single-domain antibodies
Expert Opinion on Drug Delivery, 2016The targeted delivery of therapeutic agents greatly increases their effectiveness while simultaneously reducing negative side effects. In the past, targeting of therapeutics has been accomplished with nucleic acids, peptides/proteins, and conventional antibodies. A promising alternative to the conventional antibodies often used in therapeutic targeting
Kendrick B Turner +2 more
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Engineering pH-Sensitive Single-Domain Antibodies
2022There is increasing interest in expanding an antibody beyond high affinity and specificity. One such feature is custom regulation of the binding event, such as pH-dependent control. Here, we provide a methodology for generating single-domain antibodies (sdAbs) that bind their antigen in a pH-dependent fashion.
Tosha M, Laughlin, James R, Horn
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Single-Domain Antibodies for Intracellular Toxin Neutralization
2022Ricin is a plant-derived toxin with a history as a biothreat agent. The toxin's enzymatic subunit, ricin toxin A chain (RTA), is a ribosome-inactivating protein that, when delivered into the cytoplasm of mammalian cells, arrests protein synthesis with extraordinary efficiency.
Timothy F, Czajka, Nicholas J, Mantis
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Engineered antibody fragments and the rise of single domains
Nature Biotechnology, 2005With 18 monoclonal antibody (mAb) products currently on the market and more than 100 in clinical trials, it is clear that engineered antibodies have come of age as biopharmaceuticals. In fact, by 2008, engineered antibodies are predicted to account for >30% of all revenues in the biotechnology market. Smaller recombinant antibody fragments (for example,
Philipp, Holliger, Peter J, Hudson
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Expression of Single-Domain Antibodies in Bacterial Systems
2012In this chapter we describe in detail the current protocols that are used to express single-domain antibodies in bacteria. Bacteria are among the most common expression systems for expressing recombinant proteins. We present different approaches for carrying out periplasmic and cytoplasmic expression, as well as small-scale and large-scale expression ...
Baral, T.N., Arbabi-Ghahroudi, M.
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Application of Single-Domain Antibodies in Tumor Histochemistry
2012High avidity, pentameric, single-domain antibodies, oligomerized through the B subunit of verotoxin, are excellent immunohistochemical reagents. The resulting molecules are termed pentabodies. Here, we describe the immunostaining of tissue sections with ES1, a pentabody recognizing CEACAM6 which is overexpressed in several cancers.
Maik, K.T., MacKenzie, C.R.
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