The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1/S1P
The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1/S1P
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DOI：
10.1073/pnas.221447598
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发表时间：
2001-10-23
影响因子：
11.1
通讯作者：
Garten, W
中科院分区：
文献类型：
--
作者：
Lenz, O;ter Meulen, J;Garten, W
拉沙病毒的表面糖蛋白是沙粒病毒科的一个成员，它被合成为一个76 kDa的前体（GIP-C），该前体在裂解后被切割成一个N-末端44 kDa的亚基和一个C-末端膜锚定的36 kDa的亚基。切割发生在不寻常的识别基序R-R-L-L的C末端。我们在这里表明，GP-C在内质网中被细胞枯草杆菌酶SKI-1/S1 P切割，该酶迄今为止已被观察到参与胆固醇代谢。此外，我们提出的证据表明，只有裂解的糖蛋白被纳入病毒粒子，这是必要的形成感染性病毒。据我们所知，以前没有报道过这种类型的病毒糖蛋白加工，这可能是一个有趣的抗病毒治疗的目标。
The surface glycoprotein of the Lassa virus, a member of the arenaviridae family, is synthesized as a 76-kDa precursor (GIP-C) that is posttranslationally cleaved into an N-terminal 44-kDa subunit and a C-terminal membrane-anchored 36-kDa subunit. Cleavage occurs at the C-terminal end of the unusual recognition motif R-R-L-L. We show here that GP-C is cleaved in the endoplasmic reticulum by the cellular subtilase SKI-1/S1P, an enzyme that has so far been observed to be involved in cholesterol metabolism. Furthermore, we present evidence that only cleaved glycoprotein is incorporated into virions and that this is necessary for the formation of infectious virus. To our knowledge, there have been no previous reports of this type of viral glycoprotein processing, one that may be an interesting target for antiviral therapy.