O-LINKED GLCNAC IN SEROTYPE-2 ADENOVIRUS FIBER
O-LINKED GLCNAC IN SEROTYPE-2 ADENOVIRUS FIBER
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DOI:
10.1111/j.1432-1033.1989.tb15008.x
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发表时间:
1989-09-01
期刊:
影响因子:
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通讯作者:
MICHALSKI, JC
中科院分区:
文献类型:
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作者:
CAILLETBOUDIN, ML;STRECKER, G;MICHALSKI, JC
Serotype-2 adenovirus fibre is shown to posses an O-linked GlcNAc residue and to have affinity for wheat germ agglutinin. The cytoplasmic and nuclear fibres are both glycosylated. Glycosylation seem to take place in the cytoplasm since most of the [14C]GlcN-labelled fibre is found in this compartment, little label being associated with the microsomes. Glycosylation of the fibre was not affected by inhibitors of N- and O-glycosylation. A variation in fibre glycosylation is observe among adenovirus. Among the serotype tested, only serotype-5 adenovirus (another subgroup C virus) also incorporated [14C]GlcN into its fibre, but did not posses affinity for wheat-germ agglutinin. The GlcNAc is located in the N-terminal two-thirds of the fibre and more probably in the N-terminal one-third. The free or penton-base-associated fibres are similarly glycosylated. There results suggest that glycosylation is not involved in viral adsorption and in assembly with the capsid penton base. Thus, glycosylation might be a characteristic feature of subgroup C viruses.