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Scheck, R.

Publications and source records attributed to Scheck, R..

2 recordsLinked to original sources

Q4ddPCR (May the Fourth Be Precise): A Flexible, 4-Target Assay for High-Resolution HIV Reservoir Profiling

Precise and scalable quantification of the genetically intact HIV reservoir is critical for advancing curative strategies. However, current HIV reservoir assays such as the intact proviral DNA assay (IPDA) are limited by quantification failures or misclassification of defective proviral genomes due to HIV sequence heterogeneity. Q4ddPCR is a modular, droplet digital PCR assay that simultaneously targets four conserved regions in the HIV genome to improve specificity, reduce quantification gaps, and provide multi-layered readouts. We benchmarked Q4ddPCR against 3,650 near full-length proviral sequences from 13 virally suppressed people with HIV (PWH) generated by Q4PCR using the same primer/probe sets. Q4ddPCR enabled intact reservoir quantification in 95% of samples from three independent cohorts and closely matched sequence-confirmed Q4PCR reservoir measurements. In addition, multi-probe readouts revealed clonal intact reservoir dynamics that are not detectable by IPDA. In longitudinal samples from 42 participants over the first 4.5 years on antiretroviral therapy (ART), Q4ddPCR reported lower proviral frequencies and a steeper decline in intact proviral DNA compared to IPDA. Collectively, our findings confirm key predictions from mathematical modeling, demonstrating that multi-target assays provide greater specificity and more accurately capture the dynamics of the intact HIV reservoir.

immunology↗

Discovery of Glycation-Derived Crosslinks at Arginine

Glycation crosslinks account for more than 40% of all known advanced glycation end products (AGEs) and are correlated with many age-related diseases. Despite much interest, crosslinking AGEs (xl-AGEs) remain poorly understood, as they have been challenging to discover, prepare, and quantify. Here we describe a peptide platform that is ideally suited for the study of xl-AGEs, which not only facilitates direct comparisons between the prevalence of known xl-AGEs and other AGEs, but also enables the discovery of previously unknown xl-AGEs. In this study, we use this platform to discover the first known Arg-Arg xl-AGEs, a pair of methylglyoxal-derived dihydroxyimidazolidine hemiacetal crosslink, or MIDAL, isomers. We show that MIDAL can become the major AGE, exceeding levels of all other AGEs, for substrates in which two Arg glycation sites are optimally positioned. We further demonstrate that MIDAL is readily and reversibly generated in biocompatible conditions, persisting with a half-life of more than three days. We also demonstrate that MIDAL can form in living mammalian cells, suggesting that it has the potential to be a dynamic, physiologically relevant and functional xl-AGE. This work therefore offers important insights about MIDAL formation and describes a versatile platform to enable the study of xl-AGEs under a variety of conditions. We expect that it will be highly useful for further discovery of biologically relevant glycation crosslinks that are yet to be identified.

biochemistry↗