G protein-coupled receptors (GPCRs) are one of the most important signal transduction protein families in human cell membranes, regulating a wide range of physiological processes from vision and olfaction to cardiovascular function. Among them, the Angiotensin II Type 1 Receptor (AT1R) plays a central role in blood pressure regulation, fluid…
G protein-coupled receptors (GPCRs) are one of the most important signal transduction protein families in human cell membranes, regulating a wide range of physiological processes from vision and olfaction to cardiovascular function. Among them, the Angiotensin II Type 1 Receptor (AT1R) plays a central role in blood pressure regulation, fluid balance, and cardiovascular diseases. However, the activation mechanism of peptide ligand-binding GPCRs like AT1R has long been a research bottleneck, as traditional methods struggled to capture their active conformations, hindering the precise development of targeted therapeutics. A research team from Harvard Medical School, Duke University, and other institutions has successfully overcome this challenge using synthetic nanobody technology. Their findings, published in Cell, pave a new path for GPCR research and drug development.
CD7是一种跨膜糖蛋白，主要表达于T细胞、NK细胞及其前体细胞表面，尤其在T细胞急性淋巴细胞白血病(T-ALL)、淋巴瘤等血液肿瘤中高表达。作为免疫球蛋白超家族成员，CD7参与T细胞活化、黏附和信号转导，在淋巴细胞发育及免疫应答中发挥重要作用，是T细胞恶性肿瘤的重要标志物。由于其表达特异性和在病理状态下的持续存在，CD7已成为开发新型免疫治疗策略的理想靶点。
CD7 is a transmembrane glycoprotein primarily expressed on the surface of T cells, NK cells, and their precursor cells. It is highly expressed, especially in hematological tumors such as T-cell acute lymphoblastic leukemia (T-ALL) and lymphoma. As a member of the immunoglobulin superfamily, CD7 is involved in T cell activation, adhesion, and…
CD7 is a transmembrane glycoprotein primarily expressed on the surface of T cells, NK cells, and their precursor cells. It is highly expressed, especially in hematological tumors such as T-cell acute lymphoblastic leukemia (T-ALL) and lymphoma. As a member of the immunoglobulin superfamily, CD7 is involved in T cell activation, adhesion, and signal transduction, playing an important role in lymphocyte development and immune response. It is a significant marker for T-cell malignancies. Due to its specific expression and persistence in pathological states, CD7 has become an ideal target for developing novel immunotherapeutic strategies.
水泡性口炎病毒（VSV）是极具潜力的溶瘤病毒，可优先在干扰素通路缺陷的肿瘤细胞中复制并实现溶瘤效果，其糖蛋白（VSV-G）是慢病毒伪型最常用的包膜糖蛋白，被广泛用于基因治疗领域的研究。然而VSV-G的天然受体(LDL-R家族)在几乎所有细胞表面均有表达，导致VSV和伪型慢病毒缺乏靶向性，不仅会感染正常细胞引发脱靶毒性，还会降低体内精准治疗效果。已知VSV-G的K47和R354位点突变可完全消除其与LDL-R的结合，但保留融合活性，为改造VSV-G靶向性提供了可能。
Vesicular stomatitis virus (VSV) is a highly promising oncolytic virus capable of preferentially replicating in and lysing tumor cells with defective interferon signaling pathways. Its glycoprotein (VSV-G) is the most commonly used envelope glycoprotein for pseudotyping lentiviral vectors and is widely utilized in gene therapy research. However,…
Vesicular stomatitis virus (VSV) is a highly promising oncolytic virus capable of preferentially replicating in and lysing tumor cells with defective interferon signaling pathways. Its glycoprotein (VSV-G) is the most commonly used envelope glycoprotein for pseudotyping lentiviral vectors and is widely utilized in gene therapy research. However, the natural receptors of VSV-G (the LDL-R family) are expressed on the surface of nearly all cell types, leading to a lack of targeting specificity for both VSV and pseudotyped lentiviruses. This not only results in the infection of normal cells, causing off-target toxicity, but also reduces the efficacy of precise in vivo treatments. It is known that mutations at the K47 and R354 residues of VSV-G can completely abolish its binding to LDL-R while preserving its fusion activity, offering a potential strategy for engineering targeted VSV-G.