ANTXR2 Human

ANTXR2 was first identified due to its differential expression during capillary morphogenesis in three-dimensional collagen matrices . The protein has a conserved von Willebrand factor A (VWA) domain, which is essential for its interaction with the protective antigen of anthrax toxin. This domain includes a metal ion-dependent adhesion site (MIDAS) motif, critical for binding to the protective antigen .

ANTXR2 functions as a receptor that mediates the internalization of anthrax toxin into host cells. Upon binding to the protective antigen, ANTXR2 facilitates the formation of a heptameric or octameric pore, allowing the translocation of lethal and edema factors into the cytosol . These factors disrupt cellular signaling pathways, leading to cell death and contributing to the virulence of Bacillus anthracis.

The expression of ANTXR2 has undergone multiple stages of evolutionary change in humans. Studies suggest that the advent of animal husbandry and hunting increased human exposure to zoonotic pathogens, including Bacillus anthracis. This exposure may have driven selective pressures on the ANTXR2 gene, leading to regulatory changes that decreased its expression in immune cells . These adaptations likely provided a survival advantage by reducing the susceptibility to anthrax disease.

Recent research has highlighted the protective role of ANTXR2 in liver fibrosis. Endothelial ANTXR2 promotes the activation of matrix metalloproteinase 2 (MMP2), which degrades the extracellular matrix (ECM) and alleviates fibrosis . This function suggests potential therapeutic applications of ANTXR2 in treating liver-related diseases.

Human recombinant ANTXR2 is produced using recombinant DNA technology, allowing for the study of its structure and function in vitro. This recombinant protein is valuable for research into anthrax pathogenesis and the development of potential therapeutic interventions.