Anthrax toxin receptor 1 (TEM8) and Anthrax toxin receptor 2 (CMG2) (ANTXR1/2)

Anthrax toxin receptors TEM8 (Tumor Endothelial Marker 8) and CMG2 (Capillary Morphogenesis Gene 2) are type I transmembrane proteins that serve as the essential gateways for Bacillus anthracis toxins to enter host cells (Bradley et al., 2001, Nature). Both receptors possess an extracellular von Willebrand factor type A (vWA) domain that binds the Protective Antigen (PA) subunit of the toxin, though CMG2 has a significantly higher affinity and is the primary mediator of anthrax pathogenesis (Scobie et al., 2003, PNAS). Beyond their role in infection, TEM8 is highly overexpressed in the vasculature of various solid tumors compared to normal tissue, making it a promising target for anti-angiogenic and anti-cancer therapies (St. Croix et al., 2000, Science). CMG2 is also critical for normal physiology, specifically in maintaining extracellular matrix homeostasis, as evidenced by mutations causing Hyaline Fibromatosis Syndrome (Hanks et al., 2003, Am J Hum Genet). Current therapeutic approaches primarily utilize monoclonal antibodies to neutralize PA and prevent receptor binding, while experimental strategies explore direct targeting of TEM8 for oncology applications (FDA, 2016; Chaudhary et al., 2012, JNCI).

Other names

TEM8CMG2Tumor endothelial marker 8Capillary morphogenesis gene 2ANTXR1ANTXR2ATRATRN1ATRN2HFSISH

Neutralization of the Protective Antigen (PA) component of Bacillus anthracis to prevent its binding to the vWA domains of TEM8 and CMG2, thereby blocking toxin entry (FDA, 2012; Scobie et al., 2003). Experimental oncology approaches involve direct binding to TEM8 to inhibit tumor angiogenesis or deliver cytotoxic agents (St. Croix et al., 2000).