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- Title
N-glycans from Paramecium bursaria chlorella virus MA-1D: Re-evaluation of the oligosaccharide common core structure.
- Authors
Speciale, Immacolata; Lorenzo, Flaviana Di; Notaro, Anna; Noel, Eric; Agarkova, Irina; Molinaro, Antonio; Etten, James L Van; Castro, Cristina De
- Abstract
Paramecium bursaria chlorella virus MA-1D is a chlorovirus that infects Chlorella variabilis strain NC64A, a symbiont of the protozoan Paramecium bursaria. MA-1D has a 339-kb genome encoding ca. 366 proteins and 11 tRNAs. Like other chloroviruses, its major capsid protein (MCP) is decorated with N -glycans, whose structures have been solved in this work by using nuclear magnetic spectroscopy and matrix-assisted laser desorption ionization-time of flight mass spectrometry along with MS/MS experiments. This analysis identified three N-linked oligosaccharides that differ in the nonstoichiometric presence of three monosaccharides, with the largest oligosaccharide composed of eight residues organized in a highly branched fashion. The N -glycans described here share several features with those of the other chloroviruses except that they lack a distal xylose unit that was believed to be part of a conserved core region for all the chloroviruses. Examination of the MA-1D genome detected a gene with strong homology to the putative xylosyltransferase in the reference chlorovirus PBCV-1 and in virus NY-2A, albeit mutated with a premature stop codon. This discovery means that we need to reconsider the essential features of the common core glycan region in the chloroviruses.
- Subjects
GLYCANS; CHLORELLA; PARAMECIUM; NUCLEAR spectroscopy; MASS spectrometry; LASER spectroscopy; OLIGOSACCHARIDES
- Publication
Glycobiology, 2022, Vol 39, Issue 3, p260
- ISSN
0959-6658
- Publication type
Article
- DOI
10.1093/glycob/cwab113