Open AccessStructure of the major oligosaccharides in the fusion glycoprotein of Newcastle disease virus
Author(s) -
DIABATÉ Silvia,
GEYER Rudolf,
STIRM Stephan
Publication year - 1984
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1984.tb08011.x
Subject(s) - newcastle disease , glycoprotein , virology , virus , fusion , chemistry , biology , biochemistry , philosophy , linguistics
The fusion glycoprotein (F 0 ) was isolated from Newcastle disease virus (NDV) particles metabolically labelled with [2‐ 3 H]mannose; it was successively digested with protease and with endo‐β‐ N ‐acetylglucosaminidase from Streptomyces griseus. In this manner, the majority of the oligosaccharides in NDV F 0 could be liberated. After reduction with NaBH 4 , they were separated by high‐performance liquid chromatography, and were subjected to structural analysis. Using micromethylation/capillary gas chromatography/mass fragmentography, α‐mannosidase digestion, and acetolysis, it was found that the enzymatically released NDV F 0 oligosaccharides are common oligomannosidic glycoprotein glycans of size classes (Man) 8 GlcNAc, (Man) 7 GlcNAc, (Man) 6 GlcNAc, (Man) 9 GlcNAc, and (Man) 5 GlcNAc (in order of prevalence). The major structural isomers present in the NDV F 0 (Man) 8 GlcNAc to (Man) 5 GlcNAc fractions were shown to lack mannose residues D 2 , D 1 D 2 or D 2 D 3 , D 1 D 2 D 3 , and CD 1 D 2 D 3 , respectively, of (Man) 9 GlcNAc: