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Patent
Ghent University, Vrije Universiteit Brussel, Oxyrane UK and Vib Vzw | Date: 2010-09-29

Described herein are methods and genetically engineered cells useful for uncapping a mannose-6-phosphate residue on an oligosaccharide.


Patent
Oxyrane UK, Ghent University and Vib Vzw | Date: 2012-09-14

Described herein are methods and genetically engineered cells useful for producing an altered N-glycosylation form of a target molecule. Also described are methods and molecules with altered N-glycosylation useful for treating a variety of disorders such as metabolic disorders.


Patent
Oxyrane UK, Ghent University and Vib Vzw | Date: 2012-09-14

Described herein are methods and genetically engineered cells useful for producing an altered N-glycosylation form of a target molecule. Also described are methods and molecules with altered N-glycosylation useful for treating a variety of disorders such as metabolic disorders.


Elegheert J.,Ghent University | Bracke N.,Ghent University | Pouliot P.,Ghent University | Gutsche I.,Joseph Fourier University | And 11 more authors.
Nature Structural and Molecular Biology | Year: 2012

Hematopoietic human colony-stimulating factor 1 (hCSF-1) is essential for innate and adaptive immunity against viral and microbial infections and cancer. The human pathogen Epstein-Barr virus secretes the lytic-cycle protein BARF1 that neutralizes hCSF-1 to achieve immunomodulation. Here we show that BARF1 binds the dimer interface of hCSF-1 with picomolar affinity, away from the cognate receptor-binding site, to establish a long-lived complex featuring three hCSF-1 at the periphery of the BARF1 toroid. BARF1 locks dimeric hCSF-1 into an inactive conformation, rendering it unable to signal via its cognate receptor on human monocytes. This reveals a new functional role for hCSF-1 cooperativity in signaling. We propose a new viral strategy paradigm featuring an allosteric decoy receptor of the competitive type, which couples efficient sequestration and inactivation of the host growth factor to abrogate cooperative assembly of the cognate signaling complex. © 2012 Nature America, Inc. All rights reserved. Source


Described herein are methods and materials for reducing degradation of recombinant proteins in fungal cells such as

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