Anthrax toxin receptor 1 (ANTXR1)

Anthrax toxin receptor 1 (ANTXR1, also known as tumor endothelial marker 8, TEM8) is a type I transmembrane cell-surface receptor that serves as a primary docking site for the protective antigen (PA) component of Bacillus anthracis toxin, facilitating the entry of anthrax toxic enzymes (lethal factor and edema factor) into the cytosol of host cells[3][2][7]. ANTXR1 also functions as the high-affinity cellular receptor for Seneca Valley virus, an oncolytic picornavirus with emerging use in targeted cancer therapy for tumors expressing this receptor[5][1][4]. Structurally, ANTXR1 shares significant similarity with integrins, particularly in its von Willebrand factor A (vWA) domain, which mediates ligand binding[7][9]. It is overexpressed in tumor endothelium versus normal vasculature, making it an attractive therapeutic and diagnostic target in oncology[2][5]. Beyond its role as a pathogen receptor, recent studies suggest ANTXR1 may function as a mechanosensor, influencing cell fate in response to mechanical cues in the microenvironment[9]. While there are no approved drugs targeting ANTXR1 directly, it remains under investigation for cancer therapeutics and as a molecular handle for selective delivery of cytotoxic agents or viruses to tumors.

Other names

Tumor endothelial marker 8 (TEM8)Tumor endothelium marker 8TEM-8

Ligand/receptor-mediated endocytosis (for anthrax toxin PA, and Seneca Valley virus); Antibody binding to block toxin or virus entry (in therapeutic development)