Article ; Online: N-Glycosylation as a Modulator of Protein Conformation and Assembly in Disease.
2024 Volume 14, Issue 3
Abstract: ... glycosylation and protein conformation, with a specific focus on the profound impact of N-glycans ... protein of the SARS virus, illustrating how N-glycans regulate the infectivity of pathogenic agents ... exploring instances where N-glycosylation transforms physiological protein structures into disease ...
| Abstract | Glycosylation, a prevalent post-translational modification, plays a pivotal role in regulating intricate cellular processes by covalently attaching glycans to macromolecules. Dysregulated glycosylation is linked to a spectrum of diseases, encompassing cancer, neurodegenerative disorders, congenital disorders, infections, and inflammation. This review delves into the intricate interplay between glycosylation and protein conformation, with a specific focus on the profound impact of N-glycans on the selection of distinct protein conformations characterized by distinct interactomes-namely, protein assemblies-under normal and pathological conditions across various diseases. We begin by examining the spike protein of the SARS virus, illustrating how N-glycans regulate the infectivity of pathogenic agents. Subsequently, we utilize the prion protein and the chaperone glucose-regulated protein 94 as examples, exploring instances where N-glycosylation transforms physiological protein structures into disease-associated forms. Unraveling these connections provides valuable insights into potential therapeutic avenues and a deeper comprehension of the molecular intricacies that underlie disease conditions. This exploration of glycosylation's influence on protein conformation effectively bridges the gap between the glycome and disease, offering a comprehensive perspective on the therapeutic implications of targeting conformational mutants and their pathologic assemblies in various diseases. The goal is to unravel the nuances of these post-translational modifications, shedding light on how they contribute to the intricate interplay between protein conformation, assembly, and disease. |
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| MeSH term(s) | Glycosylation ; Protein Processing, Post-Translational ; Polysaccharides/chemistry ; Protein Conformation ; Prions/metabolism |
| Chemical Substances | Polysaccharides ; Prions |
| Language | English |
| Publishing date | 2024-02-27 |
| Publishing country | Switzerland |
| Document type | Journal Article ; Review |
| ZDB-ID | 2701262-1 |
| ISSN | 2218-273X ; 2218-273X |
| ISSN (online) | 2218-273X |
| ISSN | 2218-273X |
| DOI | 10.3390/biom14030282 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
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