Topic
Mannosidases
About: Mannosidases is a research topic. Over the lifetime, 178 publications have been published within this topic receiving 5361 citations.
Papers published on a yearly basis
Papers
TL;DR: The humanization of the glycosylation pathway in the yeast Pichia pastoris to secrete a human glycoprotein with uniform complex N-glycosylated structures is reported, which could become a tool for elucidating the structure-function relation of glycoproteins.
Abstract: We report the humanization of the glycosylation pathway in the yeast Pichia pastoris to secrete a human glycoprotein with uniform complex N-glycosylation. The process involved eliminating endogenous yeast glycosylation pathways, while properly localizing five active eukaryotic proteins, including mannosidases I and II, N-acetylglucosaminyl transferases I and II, and uridine 5'-diphosphate (UDP)-N-acetylglucosamine transporter. Targeted localization of the enzymes enabled the generation of a synthetic in vivo glycosylation pathway, which produced the complex human N-glycan N-acetylglucosamine2-mannose3-N-acetylglucosamine2 (GlcNAc2Man3GlcNAc2). The ability to generate human glycoproteins with homogeneous N-glycan structures in a fungal host is a step toward producing therapeutic glycoproteins and could become a tool for elucidating the structure-function relation of glycoproteins.
461 citations
TL;DR: Evidence is presented that mannosidase II (Tulsiani, D. R.) is the Golgi enzyme that converts GlcNAc Man5 species to Glc NAcMan3 species in completing the mannosyl trimming process required in the biosynthesis of complex type glycoproteins.
297 citations
TL;DR: Nascent N-linked glycoproteins possess a large oligosaccharide precursor, Glc(3)Man(9)GlcNAc(2), which is later sequentially trimmed, helping understand the code displayed by each structure produced by this trimming and its decoding by lectins.
228 citations
Patent•
20 Feb 2004
TL;DR: In this article, the authors proposed a method to obtain a Man5GlcNAc2 core structure which can then be modified by heterologous expression of one or more enzymes, e.g., glycosyltransferases, sugar transporters and mannosidases, to yield human-like glycoproteins.
Abstract: The present invention relates to eukaryotic host cells having modified oligosaccharides which may be modified further by heterologous expression of a set of glycosyltransferases, sugar transporters and mannosidases to become host-strains for the production of mammalian, e.g., human therapeutic glycoproteins. The invention provides nucleic acid molecules and combinatorial libraries which can be used to successfully target and express mammalian enzymatic activities such as those involved in glycosylation to intracellular compartments in a eukaryotic host cell. The process provides an engineered host cell which can be used to express and target any desirable gene(s) involved in glycosylation. Host cells with modified oligosaccharides are created or selected. N-glycans made in the engineered host cells have a Man5GlcNAc2 core structure which may then be modified further by heterologous expression of one or more enzymes, e.g., glycosyltransferases, sugar transporters and mannosidases, to yield human-like glycoproteins. For the production of therapeutic proteins, this method may be adapted to engineer cell lines in which any desired glycosylation structure may be obtained.
184 citations
TL;DR: Crystal structures of the catalytic domain of human ER class I α1,2-mannosidase provide insight into the specificity of this class of enzymes and provide a blueprint for the future design of novel inhibitors that prevent degradation of misfolded proteins in genetic diseases.
156 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2021 | 2 |
| 2020 | 3 |
| 2019 | 3 |
| 2018 | 4 |
| 2017 | 2 |
| 2016 | 3 |