Evidence for virus-encoded glycosylation specificity.
Evidence for virus-encoded glycosylation specificity.
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病毒编码糖基化特异性的证据。
DOI：
10.1073/pnas.90.9.3840
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发表时间：
1993
影响因子：
11.1
通讯作者：
VanEtten,JL
中科院分区：
文献类型：
--
作者：
Wang,IN;Li,Y;Que,Q;Bhattacharya,M;Lane,LC;Chaney,WG;VanEtten,JL
四个自发衍生的血清学不同类的突变草履虫bursariaperrella病毒（PBCV-1）分离使用多克隆抗血清制备的完整PBCV-1或PBCV-1衍生的血清型。病毒主要衣壳蛋白和两种次要糖蛋白的寡糖决定了病毒的血清学特异性。通常，病毒糖蛋白由病毒蛋白的宿主特异性糖基化产生;聚糖部分只能通过在另一宿主上生长病毒或通过病毒蛋白的糖基化位点突变来改变。这两种机制都不能解释PBCV-1主要衣壳蛋白聚糖的变化，因为所有病毒均在相同宿主菌中生长，并且PBCV-1血清型中主要衣壳蛋白的预测氨基酸序列相同。PBCV-1抗血清耐药性最好解释为病毒突变阻断了糖基化的特定步骤，可能是通过灭活糖基转移酶。
Four spontaneously derived serologically distinct classes of mutants of the Paramecium bursaria chlorella virus (PBCV-1) were isolated using polyclonal antiserum prepared against either intact PBCV-1 or PBCV-1-derived serotypes. The oligosaccharide(s) of the viral major capsid protein and two minor glycoproteins determined virus serological specificity. Normally, viral glycoproteins arise from host-specific glycosylation of viral proteins; the glycan portion can be altered only by growing the virus on another host or by mutations in glycosylation sites of the viral protein. Neither mechanism explains the changes in the glycan(s) of the PBCV-1 major capsid protein because all of the viruses were grown in the same host alga and the predicted amino acid sequence of the major capsid protein was identical in the PBCV-1 serotypes. PBCV-1 antiserum resistance is best explained by viral mutations that block specific steps in glycosylation, possibly by inactivating glycosyltransferases.