Work

Glycomimetic affinity-enrichment proteomics identifies partners for a clinically-utilized iminosugar

Year: 2013

Type: article

Abstract: Widescale evaluation of interacting partners for carbohydrates is an underexploited area. Probing of the ‘glyco-interactome’ has particular relevance given the lack of direct genetic control of glycoconjugate biosynthesis. Here we design, create and utilize a natural product-derived glycomimetic iminosugar probe in a Glycomimetic Affinity-enrichment Proteomics (Glyco-AeP) strategy to elucidate key interactions directly from mammalian tissue. The binding partners discovered here and the associated genomic analysis implicate a subset of chaperone and junctional proteins as important in male fertility. Such repurposing of existing therapeutics thus creates direct routes to probing in vivo function. The success of this strategy suggests a general approach to discovering ‘carbohydrate-active’ partners in biology.

Source: Chemical Science

DOI: 10.1039/c3sc50826a

Authors: Isa N. Cruz, Conor S. Barry, Holger B. Kramer, C. Celeste Chuang, Sarah Lloyd, Aarnoud C. van der Spoel, Frances M. Platt, Min Yang, Benjamin G. Davis

Institutions: UCL School of Pharmacy, University College London, University of Oxford, MRC Prion Unit, National Hospital for Neurology and Neurosurgery, UCL Queen Square Institute of Neurology

Language: English

Topic: Glycosylation and Glycoproteins Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

Funders: Wellcome Trust, Royal Society, Engineering and Physical Sciences Research Council, Biotechnology and Biological Sciences Research Council, Fundação para a Ciência e a Tecnologia

Awards: Understanding and Exploiting Tunicamycin (Bio)Synthesis to Enable Novel Antibiotics and Inhibitors, G2251270888, G295399147, G3038452519, Engineering stable calibration standards for biomedical research, Ion Channels and Diseases of Electrically Excitable Cells., Dissecting the mechanism by which glycosyltransferases calalyse mannosyl transfer, G7739863634, The CHELL : A Bottom-Up approach to in vitro and in silico Minimal Life-like Constructs, Creating a Synthetic Platform for Understanding and Exploiting Glycoconjugates, G8603049439

OpenAlex ID: W2128403847

FWCI: 0.101

Cites: 52

Cited by: 8

Related to: 10