Basolateral sorting of the HIV type 2 and SIV envelope glycoproteins in polarized epithelial cells: Role of the cytoplasmic domain
Basolateral sorting of the HIV type 2 and SIV envelope glycoproteins in polarized epithelial cells: Role of the cytoplasmic domain
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DOI：
10.1089/aid.1997.13.665
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发表时间：
1997-05-20
影响因子：
1.5
通讯作者：
Compans, RW
中科院分区：
文献类型：
--
作者：
Ball, JM;Mulligan, MJ;Compans, RW
在极化的上皮细胞系中，包膜病毒通过在特定质膜结构域的不对称病毒出芽定向释放。先前的研究表明，HIV-1出芽和gp 160表达发生在基底外侧膜上，而在不存在Env糖蛋白的情况下，HIV-1 Gag颗粒的释放是非极化的，我们已经研究了使用牛痘病毒重组体在Vero C1008极化上皮细胞中HIV-2和SIV包膜糖蛋白的定向转运和表面表达。与HIV-1 gp 160类似，HIV-2和SIV表面糖蛋白都优先定向于基底外侧膜，因此基底外侧表达似乎是灵长类慢病毒糖蛋白的共同特性。为了探索胞质结构域在将HIV-2和SIV Env糖蛋白定向于基底外侧表面中的作用，引入终止密码子以模拟这些病毒在培养物中反复传代后观察到的天然细胞质截短。这些截短的糖蛋白也被分选到基底外侧结构域，相反，当缺失SIV Env糖蛋白的整个胞质结构域时，无尾SIV突变体优先在顶端表面上表达。这些数据表明在灵长类慢病毒糖蛋白的胞质结构域中存在基底外侧分选信号。
In polarized epithelial cell lines, enveloped viruses are directionally released by asymmetric viral budding at specific plasma membrane domains, Previous studies have shown that HIV-1 budding and gp160 expression occur on basolateral membranes whereas the release of HIV-1 Gag particles, in the absence of the Env glycoproteins, is nonpolarized, We have examined the directional transport and surface expression of HIV-2 and SIV envelope glycoproteins using vaccinia virus recombinants in Vero C1008 polarized epithelial cells. Analogous to HIV-1 gp160, both HIV-2 and SIV surface glycoproteins mere preferentially directed to basolateral membranes, Hence basolateral expression appears to be a common property of the glycoproteins of primate lentiviruses, To explore the role of the cytoplasmic domain in directing the HIV-2 and SIV Env glycoproteins to the basolateral surface, stop codons were introduced to mimic the natural cytoplasmic truncations observed following repeated passage of these viruses in culture, These truncated glycoproteins also were sorted to the basolateral domain, but at a lower efficiency than the full-length protein product, In contrast, when the entire cytoplasmic domain of the SIV Env glycoprotein was deleted, the tailless SIV mutant was preferentially expressed on the apical surface, These data indicate the presence of a basolateral sorting signal in the cytoplasmic domain of primate lentiviral glycoproteins.