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. 2004 Oct 25;153(4):993–1010. doi: 10.1016/0022-2836(81)90463-0

Coronavirus glycoprotein E1, a new type of viral glycoprotein☆

H Niemann 1, H-D Klenk 1
PMCID: PMC7130891  PMID: 7343686

Abstract

The carbohydrate contents of coronavirus glycoproteins E1 and E2 have been analyzed. E2 has complex and mannose-rich-type oligosaccharide side-chains, which are attached by N-glycosidic linkages to the polypeptide. Glycosylation of E2 is initiated at the co-translational level, and it is inhibited by tunicamycin, 2-deoxy-glucose, and 2-deoxy-2-fluoro-glucose. Thus, E2 belongs to a glycoprotein type found in many other enveloped viruses. E1, in contrast, represents a different class of glycoprotein. The following observations indicate that its carbohydrate side-chains have 0-glycosidic linkage. (1) The constituent sugars of E1 are N-acetylglucosamine, N-acetylgalactosamine, galactose, and neuraminic acid; mannose and fucose are absent. (2) The side-chains can be removed by β-elimination. (3) Glycosylation of E1 is not sensitive to the compounds interfering with N-glycosylation. E1 is the first viral glycoprotein analyzed that contains only 0-glycosidic linkages. Coronaviruses are therefore a suitable model system to study biosynthesis and processing of this type of glycoprotein.

Footnotes

☆

This work was supported by the Deutsche Forschungsgemeinschaft (SFB 47, Virologia).

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