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by Keyword: Monoclonal antibody
Intrarakasem, N, Kaewkarn, S, Proykhunthod, P, Songjaeng, A, Avirutnun, P, Prommool, T, Puttikhunt, C, Makeudom, A, Morchang, A, Tian, XH, Battaglia, G, Patikarnmonthon, N, Kraivong, R, (2026). Intracellular delivery of anti-dengue envelope monoclonal antibodies via PEG-PLGA nanoparticles suppresses viral replication and attenuates hepatocyte apoptosis JOURNAL OF DRUG DELIVERY SCIENCE AND TECHNOLOGY 118, 108086 
Dengue virus (DENV) infection remains a major global health threat, with no specific antiviral treatment currently approved. Monoclonal antibody (mAb) therapy represents a promising strategy for viral inhibition; however, conventional antibodies are largely restricted to extracellular compartments and lack access to intracellular viral replication sites. In this study, we encapsulated a cross-reactive mAb targeting the DENV envelope protein (m513) into poly(ethylene glycol)-block-poly(lactide-co-glycolide) (PEG-PLGA) nanoparticles to facilitate intracellular delivery. When applied to immortalized hepatocyte-like cells (imHCs), the formulation demonstrated efficient cellular uptake, low cytotoxicity, and significantly reduced intracellular viral RNA and protein levels. The resulting formulation consisted of mAb-loaded PEG-PLGA nanoparticles (similar to 100 nm in diameter) with spherical morphology and an encapsulation efficiency of approximately 50%. Furthermore, nanoparticle treatment significantly reduced hepatocyte apoptosis in infected cells. Collectively, these findings demonstrate that nanoparticle-mediated intracellular antibody delivery can overcome a key limitation of conventional antibody therapy and represents a mechanistically distinct antiviral strategy for DENV and other intracellular viral infections.
JTD Keywords: Antibody delivery, Dengue virus, Drug-delivery, Endocytosis, In-vitro, Monoclonal antibody, Peg-plga nanoparticle, Protein
Esteban, O., Christ, D., Stock, D., (2013). Purification of molecular machines and nanomotors using phage-derived monoclonal antibody fragments 
Protein Nanotechnology - Methods in Molecular Biology (ed. Gerrard, J. A.), Humana Press (New York, USA) 996, 203-217
Molecular machines and nanomotors are sophisticated biological assemblies that convert potential energy stored either in transmembrane ion gradients or in ATP into kinetic energy. Studying these highly dynamic biological devices by X-ray crystallography is challenging, as they are difficult to produce, purify, and crystallize. Phage display technology allows us to put a handle on these molecules in the form of highly specific antibody fragments that can also stabilize conformations and allow versatile labelling for electron microscopy, immunohistochemistry, and biophysics experiments. Here, we describe a widely applicable protocol for selecting high-affinity monoclonal antibody fragments against a complex molecular machine, the A-type ATPase from T. thermophilus that allows fast and simple purification of this transmembrane rotary motor from its wild-type source. The approach can be readily extended to other integral membrane proteins and protein complexes as well as to soluble molecular machines and nanomotors.
JTD Keywords: ATP synthase, Crystallization, Domain antibodies, Electron microscopy, Labelling, Membrane proteins, Monoclonal antibody fragments, Phage display, Protein purification, X-ray crystallography
