Chloroviruses N-linked glycans share a new type of conserved core architecture unprecedented in any form of life

• Published in: Angewandte Chemie International Edition 2015-11, Vol.55 (2), p.654-658
• Main Authors: De Castro, Cristina, Speciale, Immacolata, Duncan, Garry, Dunigan, David D., Agarkova, Irina, Lanzetta, Rosa, Sturiale, Luisa, Palmigiano, Angelo, Garozzo, Domenico, Molinaro, Antonio, Tonetti, Michela, Van Etten, James L.
• Format: Article
• Language: English
• ISSN: 1433-7851; 1521-3773
• DOI: 10.1002/anie.201509150

N-glycosylation is a fundamental modification of proteins that exists in the three domains of life and in some viruses, including the chloroviruses, for which a new type of core N-glycan is described. This N-glycan core structure common to all chloroviruses is a pentasaccharide with a β-glucose linked to an asparagine residue that is not located in the typical sequon N-X-T/S. The glucose is linked to a terminal xylose unit and a hyperbranched fucose, in turn substituted with a terminal galactose and a second xylose residue. The third position of the fucose unit is always linked to a rhamnose, which is a semi-conserved element because its absolute configuration is virus-dependent. Additional decorations occur on this core N-glycan and represent a molecular signature for each chlorovirus.