Sequence motif upstream of the Hendra virus fusion protein cleavage site is not sufficient to promote efficient proteolytic processing
Sequence motif upstream of the Hendra virus fusion protein cleavage site is not sufficient to promote efficient proteolytic processing
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DOI：
10.1016/j.virol.2005.07.004
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发表时间：
2005-10-10
期刊：
影响因子：
3.7
通讯作者：
Dutch, RE
中科院分区：
文献类型：
--
作者：
Craft, WW;Dutch, RE
亨德拉病毒融合 (HeV F) 蛋白作为前体 F-0 合成，并按照 HDLVDGVK(109) 基序通过蛋白水解裂解成成熟的 F-1 和 F-2 异二聚体。该裂解事件是融合活性所必需的。为了确定 HeV F 蛋白加工所需的氨基酸，我们构建了多个突变体。紧邻裂解位点上游的八个残基的单独和同时的丙氨酸取代并没有消除加工。其中弗林蛋白酶位点取代了HeV F蛋白的VDGVK(109)基序的嵌合SV5 F蛋白不被加工，而是在细胞表面表达。另一个含有 HeV F 蛋白 HDLVDGVK(109) 基序的嵌合 SV5 F 蛋白经历了部分切割。这些数据表明上游区域可以在蛋白酶识别中发挥作用，但对于HeV F蛋白的有效加工来说既不是绝对必需的也不是充分的。 (c) 2005 Elsevier Inc. 保留所有权利。
The Hendra virus fusion (HeV F) protein is synthesized as a precursor, F-0, and proteolytically cleaved into the mature F-1 and F-2 heterodimer, following an HDLVDGVK(109) motif. This cleavage event is required for fusogenic activity. To determine the amino acid requirements for processing of the HeV F protein, we constructed multiple mutants. Individual and simultaneous alanine substitutions of the eight residues immediately upstream of the cleavage site did not eliminate processing. A chimeric SV5 F protein in which the furin site was substituted for the VDGVK(109) motif of the HeV F protein was not processed but was expressed on the cell surface. Another chimeric SV5 F protein containing the HDLVDGVK(109) motif of the HeV F protein underwent partial cleavage. These data indicate that the upstream region can play a role in protease recognition, but is neither absolutely required nor sufficient for efficient processing of the HeV F protein. (c) 2005 Elsevier Inc. All rights reserved.