N-glycans from Paramecium bursaria chlorella virus MA-1D: Re-evaluation of the oligosaccharide common core structure

Autor: Immacolata Speciale, Flaviana Di Lorenzo, Anna Notaro, Eric Noel, Irina Agarkova, Antonio Molinaro, James L Van Etten, Cristina De Castro
Přispěvatelé: Speciale, Immacolata, Di Lorenzo, Flaviana, Notaro, Anna, Noel, Eric, Agarkova, Irina, Molinaro, Antonio, Van Etten, James L, De Castro, Cristina
Rok vydání: 2021
Předmět:
Zdroj: Glycobiology. 32:260-273
ISSN: 1460-2423
DOI: 10.1093/glycob/cwab113
Popis: 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.
Databáze: OpenAIRE