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.
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.