Yoshida Takeshi, Kawano Yuji, Sato Kei, Ando Yoshinori, Aoki Jun, Miura Yoshiharu, Komano Jun, Tanaka Yuetsu, Koyanagi Yoshio
Laboratory of Viral Pathogenesis, Institute for Virus Research, Kyoto University, Sakyo-ku, Kyoto 606-8507, Japan.
Traffic. 2008 Apr;9(4):540-58. doi: 10.1111/j.1600-0854.2007.00700.x.
We have discovered that an N-terminal deletion mutant of a membrane protein, CD63, (CD63DeltaN) blocks entry of CXCR4-using, T-cell tropic human immunodeficiency virus type 1 (X4 HIV-1) by suppressing CXCR4 surface expression. This suppression was observed for CXCR4 but not for CD4, CCR5, CD25, CD71 or other tetraspanin proteins. The suppression of CXCR4 expression on the plasma membrane appeared to be caused by mislocalization of CXCR4 and exclusive transportation of CXCR4 toward intracellular organelles, mainly late endosomes/lysosomes. Our data suggest that CXCR4 trafficking can be modified in terms of its recruitment to the plasma membrane without enhancing the degradation or arresting vesicular transport of CXCR4.
我们发现，一种膜蛋白CD63的N端缺失突变体（CD63DeltaN）通过抑制CXCR4的表面表达，阻断了利用CXCR4的T细胞嗜性1型人类免疫缺陷病毒（X4 HIV-1）的进入。这种抑制作用在CXCR4上观察到，但在CD4、CCR5、CD25、CD71或其他四跨膜蛋白上未观察到。质膜上CXCR4表达的抑制似乎是由CXCR4的错误定位以及CXCR4向细胞内细胞器（主要是晚期内体/溶酶体）的排他性运输引起的。我们的数据表明，CXCR4的运输可以在不增强其降解或阻止囊泡运输的情况下，在其向质膜募集方面进行修饰。
