Reitter J N, Means R E, Desrosiers R C
New England Regional Primate Research Center, Harvard Medical School, Southborough, Massachusetts 01772-9102, USA.
Nat Med. 1998 Jun;4(6):679-84. doi: 10.1038/nm0698-679.
Rhesus monkeys were infected with mutant forms of simian immunodeficiency virus lacking dual combinations of the 4th, 5th and 6th sites for N-linked glycosylation in the external envelope glycoprotein of the virus. When compared with sera from monkeys infected with the parental virus, sera from monkeys infected with the mutant viruses exhibited markedly increased antibody binding to specific peptides from this region and markedly increased neutralizing activity. These results demonstrate a role for N-linked glycosylation in limiting the neutralizing antibody response to SIV and in shielding the virus from immune recognition.
恒河猴感染了猿猴免疫缺陷病毒的突变形式,这些突变形式在病毒外膜糖蛋白中缺乏第4、5和6个N-连接糖基化位点的双重组合。与感染亲本病毒的猴子血清相比,感染突变病毒的猴子血清对该区域特定肽段的抗体结合显著增加,中和活性也显著增加。这些结果表明N-连接糖基化在限制对SIV的中和抗体反应以及使病毒免受免疫识别方面发挥作用。