Antibodies are specialized proteins produced by the immune system which target and neutralize foreign materials, such as viruses or bacteria. Antibodies have a variety of useful applications in diagnostics, therapeutics, and as research reagents. Despite their widespread use there is no standard method to produce antibodies, and currently available methods are labor and time intensive.
The Ribopuromycylation (RPM) technology, developed by Dr. Jon Yewdell and Dr. Alexandre David, offers a powerful and universal method for visualizing and studying protein translation within cells. RPM involves the use of puromycin, a molecule that mimics a tyrosyl-tRNA and terminates translation by becoming covalently incorporated into the nascent protein chain's C-terminus within the ribosome's A site. This technique enables the immobilization of puromycylated nascent protein chains on ribosomes when chain elongation inhibitors like cycloheximide or emetine are utilized.
The technology presented is a breakthrough in the diagnosis of lymphatic filariasis, specifically targeting the B. malayi pathogen. It encompasses a novel soluble antigen extract used in both IgG and IgG4-based ELISA tests, aimed at detecting the presence of the filarial infection. This innovation serves as a cornerstone for a CLIA-certified reference test, established and utilized in Dr. Nutman's laboratory since the late 1980s.
This technology involves studying the role of the Tumor-Associated Calcium Signal Transducer 2 (TACSTD2) gene in Hepatitis C Virus (HCV) infection and hepatocellular carcinoma. Researchers perform transcriptomics analysis on liver specimens from HCV-infected patients, identify TACSTD2 as a key gene, and create a stable cell line that overexpresses TACSTD2 to investigate its impact on HCV infection and replication. This technology aims to provide insights into the molecular mechanisms of HCV infection and its association with liver cancer.
The potential applications of a replicative-defective mutant form of human cytomegalovirus (HCMV) are significant in the fields of vaccinology and cancer immunotherapy. This innovative approach involves engineering a mutant HCMV that can selectively target specific cells. Firstly, it holds promise as a vaccine candidate for protecting against HCMV infection, given the success of a similar strategy against herpes simplex virus in animal models.
The technology involves the genetic engineering of Respiratory Syncytial Virus (RSV) to express two additional genes, green fluorescent protein (GFP) and Renilla luciferase, from different positions within the viral genome. GFP serves as a visual marker for RSV infection, allowing researchers to monitor and track infected cells using fluorescence microscopy, while luciferase functions as a highly sensitive reporter gene that enables quantitative assessment of viral replication through enzymatic assays.
The technology involves genetically engineering Human Metapneumovirus (HMPV) to express enhanced green fluorescent protein (GFP), enabling the monitoring of virus infection and gene expression through GFP fluorescence. This system serves as a sensitive and versatile tool for virology research, antiviral drug screening, and diagnostic applications.
In this technology, researchers have engineered a modified version of Respiratory Syncytial Virus (RSV) strain A2 using reverse genetics to incorporate green fluorescent protein (GFP) into the first-gene position. This genetic modification allows for the efficient monitoring of RSV infection and the screening of potential chemical inhibitors. The GFP expression can be easily detected through fluorescence microscopy in live or fixed cells, providing a sensitive tool for both research and drug discovery.
The technology described is a sophisticated and high-throughput luciferase immunoprecipitation system (LIPS) assay designed to detect antibodies specific to Varicella-zoster virus (VZV) glycoprotein E (gE). By transfecting cells with VZV protein-Renilla luciferase fusion protein constructs and subsequently performing immunoprecipitations with protein A/G beads, this innovative assay enables the quantitative measurement of VZV gE antibody levels in blood serum samples.
This technology represents a significant advancement in the field of rabies prevention, focusing on the development of highly potent rabies-neutralizing monoclonal antibodies (mAbs) for use in postexposure prophylaxis (PEP). With two mAbs, F2 and G5a, displaying exceptional neutralizing titers of 1154 and 3462 International Units (IUs) per milligram, respectively, these antibodies have the potential to offer enhanced protection against rabies when administered alongside rabies vaccines.