Publications by authors named "A I Cisneros Gimeno"
The mucin -glycan sialyl Tn antigen (sTn, Neu5Acα2-6GalNAcα1--Ser/Thr) is an antigen associated with different types of cancers, often linked with a higher risk of metastasis and poor prognosis. Despite efforts to develop anti-sTn antibodies with high specificity for diagnostics and immunotherapy, challenges in eliciting high-affinity antibodies for glycan structures have limited their effectiveness, leading to low titers and short protection durations. Experimental structural insights into anti-sTn antibody specificity are lacking, hindering their optimization for cancer cell recognition.
View Article and Find Full Text PDFGlycosylation is an attractive approach to enhance biological properties of pharmaceutical proteins; however, the precise installation of glycans for structure-function studies remains challenging. Here, we describe a chemoenzymatic methodology for glyco-tagging of proteins by peptidoligase catalyzed modification of the -terminus of a protein with a synthetic glycopeptide ester having an -acetyl-glucosamine (GlcNAc) moiety to generate an -GlcNAc modified protein. The GlcNAc moiety can be elaborated into complex glycans by -glycosylation using well-defined sugar oxazolines and mutant forms of endo β--acetylglucosaminidases (ENGases).
View Article and Find Full Text PDFNMR investigations of glycan conformation, dynamics, and interactions.
Prog Nucl Magn Reson Spectrosc
December 2024
Article Synopsis
- * NMR (Nuclear Magnetic Resonance) is essential for understanding glycan properties due to their flexible nature, allowing researchers to analyze their geometry, dynamics, and internal motions.
- * The review highlights the use of NMR to explore various natural glycans and their synthetic analogues, focusing on how these techniques can help understand glycan interactions with proteins, enhancing our knowledge for therapeutic applications.
Protein A075L is a β-xylosyltransferase that participates in producing the core of the N-glycans found in VP54, the major viral capsid protein of Paramecium bursaria chlorella virus-1 (PBCV-1). In this study, we present an X-ray crystallographic analysis of the apo form of A075L, along with its complexes with the sugar donor and with a trisaccharide acceptor. The protein structure shows a typical GT-B folding, with two Rossmann-like fold domains, in which the acceptor substrate binds to the N-terminal region, and the nucleotide-sugar donor binds to the C-terminal region.
View Article and Find Full Text PDFArticle Synopsis
- The study analyzed the prevalence of genetic diseases in the Undiagnosed Diseases Network (UDN) cohort, focusing on subjects who underwent genome sequencing before joining the study.
- Out of 2,799 subjects, 27.4% were diagnosed with a condition, with the majority having a single diagnosis primarily related to genetic diseases.
- The findings indicate that even with genome sequencing, there can still be diagnostic challenges, as some individuals had multiple genetic diagnoses or concurrent nonmolecular diseases, possibly complicating the understanding of their conditions.