Anti-RSV glycoprotein F Recombinant Antibody (TAB-709) (CAT#: TAB-709)

Tang, Wei, et al. "Mechanism of cross-resistance to fusion inhibitors conferred by the K394R mutation in respiratory syncytial virus fusion protein." Journal of Virology 95.20 (2021): 10-1128.

This study investigates the mechanism of cross-resistance to fusion inhibitors conferred by the K394R mutation in the respiratory syncytial virus (RSV) fusion protein. The researchers employed a dual-luciferase protocol to discover LF-6, a small-molecule inhibitor that targets the RSV fusion glycoprotein. They found that the K394R mutation not only conferred resistance to LF-6 but also to other RSV fusion inhibitors, including those in clinical development. This mutation destabilizes the F protein and enhances its membrane fusion activity, increasing viral resistance. The study highlights the need for alternative strategies to combat RSV infections, given the resistance risks posed by the K394R mutation.
In this research, Creative Biolabs provided crucial reagents that facilitated the experiments. Specifically, the D25 monoclonal antibody (Cat# PABL-322) and Motavizumab (Cat# TAB-709) were used for detecting RSV F protein in various assays, including the immunofluorescence and cell-surface triggering assays. These antibodies were essential for accurately identifying the effects of mutations on the RSV F protein and assessing the resistance mechanisms. The products from Creative Biolabs significantly contributed to the detailed analysis and validation of the findings related to the K394R mutation and its impact on RSV fusion inhibitor resistance​.

Henry, Kevin A., et al. "Isolation of TGF-β-neutralizing single-domain antibodies of predetermined epitope specificity using next-generation DNA sequencing." Protein Engineering, Design and Selection 29.10 (2016): 439-443. https://doi.org/10.1093/protein/gzw043

The research presents a novel strategy for isolating single-domain antibodies (sdAbs) with predetermined epitope specificity against TGF-β3, specifically targeting the interaction site between the cytokine and its type II cell-surface receptor. By combining phage display technology with next-generation DNA sequencing (NGS) and competitive elution using soluble dimeric type II receptor ectodomain, the researchers successfully identified several sdAbs that effectively compete with the receptor for TGF-β3 binding. These antibodies demonstrated the ability to neutralize TGF-β3 in cellular assays, whereas conventional panning approaches failed to yield antibodies targeting this specific epitope. The identified sdAbs showed binding affinities to TGF-β3 ranging from 12 to 284 nM, with some cross-reactivity to TGF-β2 but minimal binding to TGF-β1.
Creative Biolabs provided Synagis® (anti-RSV glycoprotein F antibody) which served as an irrelevant competitor in the competitive elution experiments during the phage display selection process. This contribution was crucial for the comparative analysis that enabled the researchers to distinguish epitope-specific sdAbs from non-specific binders. The availability of this control antibody strengthened the methodology's validity and helped establish this approach as a generalizable strategy for identifying epitope-specific antibodies when binding reagents against the epitope of interest are available, potentially advancing the development of cancer immunotherapeutics targeting the TGF-β pathway.