| Literature DB >> 32039451 |
Réka Mócsai1, Markus Blaukopf1, Elisabeth Svehla1, Paul Kosma1, Friedrich Altmann1.
Abstract
The many emerging applications of microalgae such as Chlorella also instigate interest in their ability to conduct protein modifications such as N-glycosylation. Chlorella vulgaris has recently been shown to equip its proteins with highly O-methylated oligomannosidic N-glycans. Two other frequently occurring species names are Chlorella sorokiniana and Chlorella pyrenoidosa-even though the latter is taxonomically ill defined. We analyzed by mass spectrometry and nuclear magnetic resonance spectroscopy the N-glycans of type culture collection strains of C. sorokiniana and of a commercial product labeled C. pyrenoidosa. Both samples contained arabinose, which has hitherto not been found in N-glycans. Apart from this only commonality, the structures differed fundamentally from each other and from that of N-glycans of land plants. Despite these differences, the two algae lines exhibited considerable homology in their ITS1-5.8S-ITS2 rDNA sequences. These drastic differences of N-glycan structures between species belonging to the very same genus provoke questions as to the biological function on a unicellular organism.Entities:
Keywords: zzm321990 N-glycan; arabinose; chlorella; glycoprotein; microalgae
Year: 2020 PMID: 32039451 DOI: 10.1093/glycob/cwaa012
Source DB: PubMed Journal: Glycobiology ISSN: 0959-6658 Impact factor: 4.313