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

Immacolata Speciale, Flaviana Di Lorenzo, Anna Notaro, Eric Noel, Irina Agarkova, Antonio Molinaro, James L. Van Etten, Cristina De Castro

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)260-273
Number of pages14
Issue number3
StatePublished - Mar 1 2022


  • N-glycan structure
  • NMR spectroscopy
  • chloroviruses
  • conserved core region
  • paramecium bursaria chlorella virus MA-1D

ASJC Scopus subject areas

  • Biochemistry


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