O-LINKED GLCNAC IN SEROTYPE-2 ADENOVIRUS FIBER

O-LINKED GLCNAC IN SEROTYPE-2 ADENOVIRUS FIBER
复制标题

DOI:
10.1111/j.1432-1033.1989.tb15008.x
复制
发表时间:
1989-09-01
期刊:
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子:
--
通讯作者:
MICHALSKI, JC
MICHALSKI, JC
中科院分区:
其他
文献类型:
--
作者:
CAILLETBOUDIN, ML;STRECKER, G;MICHALSKI, JC

文献摘要

被引文献

相似文献

血清型2腺病毒纤维被证明是一个O-连接的GlcNAc残基,并具有亲和力的麦胚凝集素。细胞质纤维和核纤维都是糖基化的。糖基化似乎发生在细胞质中,因为大多数[14 C] GlcN标记的纤维被发现在该隔室中,几乎没有标签与微粒体相关。纤维的糖基化不受N-和O-糖基化抑制剂的影响。在腺病毒中观察到纤维糖基化的变化。在所测试的血清型中,只有血清型-5腺病毒(另一种C亚群病毒)也将[14 C]GlcN掺入其纤维中,但不与麦胚凝集素结合。GlcNAc位于纤维的N-末端三分之二,更可能位于N-末端三分之一。游离的或五邻体-碱基-缔合的纤维类似地被糖基化。这些结果表明,糖基化不参与病毒吸附和组装与衣壳五邻体基地。因此,糖基化可能是C亚群病毒的特征。
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.