Cleavage of Epstein-Barr virus glycoprotein B is required for full function in cell-cell fusion with both epithelial and B cells.
Cleavage of Epstein-Barr virus glycoprotein B is required for full function in cell-cell fusion with both epithelial and B cells.
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DOI：
10.1099/vir.0.007237-0
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发表时间：
2009-03
期刊：
影响因子：
--
通讯作者：
Longnecker R
中科院分区：
文献类型：
--
作者：
Sorem J;Longnecker R
在疱疹病毒家族中，糖蛋白B （gB）同源物具有高度的序列保守性，许多gB同源物含有可被细胞蛋白酶furin识别的裂解基序R-X-K/R-R。eb病毒（EBV）的gB含有该基序，并且在EBV病毒粒子中发现了裂解的gB。为了确定该切割基序在EBV gB中的功能意义，构建了一个缺乏该基序的缺失突变体（gB Δfurin）。该裂解突变体在细胞培养中表达良好，但不裂解。在细胞融合实验中检测gB Δfurin的实验显示，与野生型EBV gB相比，上皮细胞的融合减少了52%，B细胞的融合减少了28%。这种细胞融合的减少与在多个α-疱疹病毒gB切割突变体中观察到的相似，并支持切割gB的保守功能。有趣的是，EBV在上皮细胞中的细胞间传播可能比B细胞更有效。
Glycoprotein B (gB) homologues within the herpesvirus family display high sequence conservation, and a number of gB homologues contain a cleavage motif R-X-K/R-R recognized by the cellular protease furin. Epstein-Barr virus (EBV) gB contains this motif and cleaved gB is found in EBV virions. To determine the functional significance of this cleavage motif in EBV gB a deletion mutant (gB Δfurin) was created lacking the motif. This cleavage mutant was expressed well in cell culture but not cleaved. Experiments examining gB Δfurin in a cell fusion assay revealed that fusion was reduced by 52% in epithelial and 28% in B cells when compared with wild type EBV gB. This decrease in cell:cell fusion is similar to that observed with multiple α-herpesvirus gB cleavage mutants and supports a conserved function for cleaved gB. Interestingly, cell-to-cell spread of EBV may be more efficient in epithelial cells than B cells.
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