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Dara, S.

Publications and source records attributed to Dara, S..

2 recordsLinked to original sources

Genomic REWRITE of Immune Interfaces Reveals Heritable Epigenetic Memory in Human Stem Cells

Human leukocyte antigen (HLA) polymorphism underlies antigen presentation, immune recognition, and central tolerance, yet the complex, multigenic structure of native HLA loci has precluded systematic engineering in human pluripotent stem cells (hPSCs). Existing genome engineering demonstrations in hPSCs focus on smaller integrations or at ectopic sites, leaving scar-minimized rewriting of native human loci at >100 kb scale a major technical challenge. Here, we present REWRITE, a modular platform for scar-minimized genome writing that enables engineering of large human genomic loci exceeding 100 kb at their native chromosomal sites. Using REWRITE, we deleted 105 kb spanning the dispersed HLA class-I locus and installed either compact or full-length refactored synthetic HLA haplotypes. Both refactored architectures exhibited transient activity before re-acquiring the native inactive state; upon extended culture, engineered lines yielded global transcriptomes nearly indistinguishable from parental cells. The engineered loci were genomically stable, retained interferon-responsive HLA expression, and remained compatible with differentiation into endothelial-like and thymic epithelial-like cells. Together, these results establish REWRITE as a platform for locus-scale genome engineering in hPSCs and provides a system for studying HLA haplotype structure and function in an isogenic pluripotent cell background. One sentenceA practical platform for scar-minimized rewriting of native human loci exceeding 100 kb in hPSCs, demonstrated through synthetic refactoring of the class-I HLA region.

synthetic biology↗

Purification and partial characterization of a high hemagglutinating chitin-binding lectin from Aponogeton natans tubers

A novel chitin-binding lectin was isolated from the tubers of a plant Aponogeton natans from the monocot family Aponogetonaceae, designated as ANTL (Aponogeton natans tuber lectin). The lectin agglutinated both untreated and trypsin-treated rabbit erythrocytes, as well as human blood cells of groups A, B and O with different specificities. Lectin activity is inhibited by the oligomers of N-acetylglucosamine. ANTL is a dimeric glycoprotein with molecular weight of [~]66 KDa and has two identical sub-units of 33 KDa. The carbohydrate percent is 8.2% of the total lectin. The lectin was thermo stable up to 50{degrees}C with broad pH optima (pH 4-10). ANTL is found to be potent mitogen for normal murine and human lymphocytes at the concentration as low as 1 {micro}g/ml. Cytotoxic studies of the lectin on human U 266 cell lines has revealed that there is 50% decrease in the proliferation. The confirmation of both the hemagglutination and mitogenic proliferation activity suggests that ANTL is a Chitin-binding lectin with diverse functions. The pharmacological relevance of ANTL as a potent mitogen with some cytotoxic effect in certain cell lines are reported for the first time. HighlightsO_LIA novel chitin-binding lectin was purified from the tuber extracts of Aponogeton natans (ANTL) in a single step on chitin column by affinity chromatography. C_LIO_LIANTL is a dimeric glycoprotein with a molecular weight of [~]66 KDa with high hemagglutination activity towards rabbit erythrocytes. C_LIO_LIThe cytotoxic effect of ATNL on human cell lines U266 has shown 50 % inhibition of their proliferation. C_LIO_LIANTL displayed potent mitogenic response towards murine and human peripheral blood mononuclear cells. C_LI

plant biology↗