Cytoplasmic R-peptide of murine leukemia virus envelope protein negatively regulates its interaction with the cell surface receptor
Cytoplasmic R-peptide of murine leukemia virus envelope protein negatively regulates its interaction with the cell surface receptor
复制标题
鼠白血病病毒包膜蛋白胞质R肽负向调节其与细胞表面受体的相互作用
DOI：
10.1016/j.virol.2019.04.005
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发表时间：
2019
期刊：
影响因子：
3.7
通讯作者：
Hayashi Hideki
中科院分区：
文献类型：
--
作者：
Kubo Yoshinao;Izumida Mai;Togawa Kei;Zhang Fengmin;Hayashi Hideki
许多逆转录病毒的囊膜糖蛋白的胞质尾（Env）抑制其膜融合活性。亲嗜性小鼠白血病病毒（E-MLV）Env蛋白的胞质16-氨基酸肽（称为R-肽）也抑制Env蛋白的膜融合活性。然而，其抑制的分子机制尚未阐明。在这项研究中，我们发现，含R-肽的E-MLV的Env蛋白结合细胞表面受体阳离子氨基酸转运蛋白-1（CAT-1）的亲和力比R-肽截短的Env蛋白弱。与此结果一致，含有R-肽的Env蛋白对E-MLV载体感染的抑制效率低于R-肽截短的Env蛋白。据报道，R肽截短可诱导与受体相互作用的E-MLV Env蛋白表面亚基的构象变化。总之，我们的研究结果表明，R-肽截短诱导E-MLV Env蛋白的受体结合结构域的构象变化，并促进Env-受体相互作用。
Cytoplasmic tails of envelope (Env) glycoproteins of many retroviruses inhibit their membrane fusion activity. The cytoplasmic 16-amino acid peptide of ecotropic murine leukemia virus (E-MLV) Env protein, called the R-peptide, also inhibits the membrane fusion activity of the Env protein. However, the molecular mechanism of the inhibition has not been elucidated yet. In this study, we found that R-peptide-containing Env protein of E-MLV binds to the cell surface receptor cationic amino acid transporter-1 (CAT-1) with weaker affinity than R-peptide-truncated Env protein. Consistent with this result, R-peptide-containing Env protein had less efficient inhibition of E-MLV vector infection than R-peptide-truncated Env protein. R-peptide truncation has been reported to induce conformational change in the surface subunit of E-MLV Env protein that interacts with the receptor. Taken together, our findings indicate that R-peptide truncation induces conformational change in the receptor-binding domain of the E-MLV Env protein and facilitates the Env–receptor interaction.