Definition of an amino-terminal domain of the human T-cell leukemia virus type 1 envelope surface unit that extends the fusogenic range of an ecotropic murine leukemia virus
Definition of an amino-terminal domain of the human T-cell leukemia virus type 1 envelope surface unit that extends the fusogenic range of an ecotropic murine leukemia virus
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DOI：
10.1074/jbc.c901002199
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发表时间：
2000-08-04
影响因子：
4.8
通讯作者：
Sitbon, M
中科院分区：
文献类型：
--
作者：
Kim, FJ;Seiliez, I;Sitbon, M
鼠白血病病毒（MuLV）和人T细胞白血病病毒（HTLV）是具有不同包膜融合特性的在遗传学上高度分化的逆转录病毒。MuLV包膜糖蛋白表面单元（SU）包含一个受体结合结构域，随后是一个富含脯氨酸的区域，可调节包膜构象变化和融合性。相反，HTLV的受体结合结构域和SU结构是不确定的。在这里，我们描述了一个HTLV/MuLV包膜嵌合体，其中亲嗜性MuLV的受体结合结构域和脯氨酸富集区被替换为HTLV-1 SU的潜在相应结构域。这种嵌合HTLV/MuLV包膜被加工，特异性干扰HTLV-1酶介导的融合，并且与MuLV包膜类似，需要切割其胞质尾以发挥显著的促融合特性。此外，这里定义的HTLV结构域拓宽了亲嗜性MuLV酶诱导的与人和猿细胞系的融合。
Murine leukemia viruses (MuLV) and human T-cell leukemia viruses (HTLV) are phylogenetically highly divergent retroviruses with distinct envelope fusion properties. The MuLV envelope glycoprotein surface unit (SU) comprises a receptor-binding domain followed by a proline-rich region which modulates envelope conformational changes and fusogenicity. in contrast, the receptor-binding domain and SU organization of HTLV are undefined. Here, we describe an HTLV/MuLV envelope chimera in which the receptor-binding domain and proline-rich region of the ecotropic MuLV were replaced with the potentially corresponding domains of the HTLV-1 SU. This chimeric HTLV/MuLV envelope was processed, specifically interfered with HTLV-1 envelope-mediated fusion, and similar to MuLV envelopes, required cleavage of its cytoplasmic tail to exert significant fusogenic properties. Furthermore, the HTLV domain defined here broadened ecotropic MuLV envelope-induced fusion to human and simian cell lines.