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Structure of the N-glycans from the chlorovirus NE-JV-1
Author(s) -
Immacolata Speciale,
Irina Agarkova,
Garry A. Duncan,
James L. Van Etten,
Cristina De Castro
Publication year - 2017
Publication title -
antonie van leeuwenhoek
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.024
H-Index - 107
eISSN - 1572-9699
pISSN - 0003-6072
DOI - 10.1007/s10482-017-0861-3
Subject(s) - glycan , acetylation , residue (chemistry) , biosynthesis , capsid , gene , chemistry , biology , computational biology , stereochemistry , biochemistry , glycoprotein
Results from recent studies are breaking the paradigm that all viruses depend on their host machinery to glycosylate their proteins. Chloroviruses encode several genes involved in glycan biosynthesis and some of their capsid proteins are decorated with N-linked oligosaccharides with unique features. Here we describe the elucidation of the N-glycan structure of an unusual chlorovirus, NE-JV-1, that belongs to the Pbi group. The host for NE-JV-1 is the zoochlorella Micractinium conductrix. Spectroscopic analyses established that this N-glycan consists of a core region that is conserved in all of the chloroviruses. The one difference is that the residue 3OMe-L-rhamnose is acetylated at the O-2 position in a non-stoichiometric fashion.

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