Department of Medicine, Division of Infectious Diseases, University of Alabama at Birmingham, USA.
Departments of Pediatrics, Neurobiology and Cell, Developmental and Integrative Biology, Division of Neonatology, University of Alabama at Birmingham, USA.
Biochim Biophys Acta Biomembr. 2017 Oct;1859(10):1962-1966. doi: 10.1016/j.bbamem.2017.06.007. Epub 2017 Jun 13.
Prior work has shown that the HIV-1 envelope of the human immunodeficiency virus (HIV) interacts directly with T-cell immunoglobulin mucin (TIM) family proteins. Herein, we demonstrate that HIV-1 envelope glycoproteins from varying HIV-1 clades bind differentially to TIM proteins and functionally similar proteins acting as phosphatidylserine (PtdSer) receptors. Using enzyme-linked immunosorbent assay (ELISA) and surface plasmon resonance (SPR) technology, we show that lysate containing HIV-1 envelope and recombinant HIV-1 envelope glycoproteins bind TIM-4 and advanced glycosylation end product-specific receptor (AGER). The complex binding of HIV-1 UG21 gp140 to TIM-4 or AGER suggests a biphasic interaction with these proteins.
先前的研究表明，人类免疫缺陷病毒（HIV）的 HIV-1 包膜直接与 T 细胞免疫球蛋白粘蛋白（TIM）家族蛋白相互作用。在此，我们证明来自不同 HIV-1 群的 HIV-1 包膜糖蛋白与 TIM 蛋白和作为磷脂酰丝氨酸（PtdSer）受体发挥功能相似的蛋白具有不同的结合能力。通过酶联免疫吸附试验（ELISA）和表面等离子体共振（SPR）技术，我们表明含有 HIV-1 包膜和重组 HIV-1 包膜糖蛋白的裂解物与 TIM-4 和晚期糖基化终产物特异性受体（AGER）结合。HIV-1 UG21 gp140 与 TIM-4 或 AGER 的复杂结合表明与这些蛋白的相互作用具有两相性。
