Premium
N‐Linked Glycans of Chloroviruses Sharing a Core Architecture without Precedent
Author(s) -
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.
Publication year - 2016
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201509150
Subject(s) - fucose , glycan , chemistry , rhamnose , residue (chemistry) , asparagine , glycosylation , xylose , stereochemistry , galactose , biochemistry , glycoprotein , amino acid , fermentation
N‐glycosylation is a fundamental modification of proteins and exists in the three domains of life and in some viruses, including the chloroviruses, for which a new type of core N‐glycan is herein described. This N‐glycan core structure, common to all chloroviruses, is a pentasaccharide with a β‐glucose linked to an asparagine residue which is not located in the typical sequon N‐X‐T/S. The glucose is linked to a terminal xylose unit and a hyperbranched fucose, which is 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 semiconserved element because its absolute configuration is virus‐dependent. Additional decorations occur on this core N‐glycan and represent a molecular signature for each chlorovirus.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom