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Siriwardena, S. U.

Publications and source records attributed to Siriwardena, S. U..

2 recordsLinked to original sources

Functional Validation of Known BEST1 Variants Using a Robust Halide-Sensitive YFP Quenching Assay

Bestrophinopathies comprise a heterogeneous group of inherited retinal degenerative diseases caused by mutations in the Bestrophin-1 (BEST1) gene. Although more than 250 pathogenic BEST1 variants have been reported, only a small subset has undergone functional interrogation. OPGx-BEST1 is an investigational gene therapy designed to restore BEST1 function through augmented wild-type BEST1 expression in retinal pigment epithelium (RPE) cells. Previous studies in animal models and patient-derived cellular systems have demonstrated that loss-of-function (LOF) BEST1 variants can be complemented with wild-type protein expression and are therefore amenable to gene augmentation strategies. In contrast, known gain-of-function (GOF) mutations appear to retain pathogenic activity despite augmentation with wild-type BEST1. Therefore, given the therapeutic relevance of LOF/GOF disease mechanisms in bestrophinopathies, a comprehensive genotype-phenotype characterization across the BEST1 mutational landscape is critical to inform clinical trial enrollment. Conventional approaches to profile BEST1 variants have relied upon patient-derived RPE models and electrophysiologic assessment of channel function. While these systems provide valuable translational insight, they lack the scalability, speed, and experimental flexibility needed for a systematic evaluation of many variants for patient selection. Here, we describe a functional screening platform that leverages an engineered halide-sensitive reporter cell line to quantitatively assess the activity of BEST1 mutant proteins.

genetics↗

Development and applications of chimera platforms for tyrosine phosphorylation

Chimeric small molecules that induce post-translational modification (PTM) on a target protein by bringing it in proximity to a PTM-inducing enzyme are furnishing novel modalities to perturb protein function. Despite recent advances, such molecules are unavailable for a critical PTM, tyrosine phosphorylation. Furthermore, the contemporary design paradigm of chimeric molecules, formed by joining a non-inhibitory binder of the PTM-inducing enzyme with the binder of the target protein, prohibits the recruitment of most PTM-inducing enzymes as their non-inhibitory binders are unavailable. Here, we report two platforms to generate phosphorylation-inducing chimeric small molecules (PHICS) for tyrosine phosphorylation. We generate PHICS from both non-inhibitory binders (scantily available, platform 1) and kinase inhibitors (abundantly available, platform 2) using cysteine-based group transfer chemistry. PHICS triggered phosphorylation on tyrosine residues in diverse sequence contexts and target proteins (e.g., membrane-associated, cytosolic) and displayed multiple bioactivities, including initiation of a growth receptor signaling cascade and death of drug-resistant cancer cells. These studies provide an approach to induce biologically relevant PTM and lay the foundation for pharmacologic PTM editing (i.e., induction or removal) on target proteins using abundantly available inhibitors of PTM-inducing or erasing enzymes. TOC O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=105 SRC="FIGDIR/small/531183v1_ufig1.gif" ALT="Figure 1"> View larger version (25K): org.highwire.dtl.DTLVardef@cdf529org.highwire.dtl.DTLVardef@19a70cdorg.highwire.dtl.DTLVardef@63dbf9org.highwire.dtl.DTLVardef@1febaaf_HPS_FORMAT_FIGEXP M_FIG C_FIG

biochemistry↗