Integrin subunit alpha V (ITGAV) (ITGAV)

Integrin subunit alpha V (ITGAV), also known as CD51, is a critical cell surface receptor that pairs with various beta subunits (β1, β3, β5, β6, or β8) to form heterodimers involved in cell-matrix interactions and signaling. It is highly expressed in skeletal muscle, where it plays a role in muscle development and repair. In the field of gene therapy, ITGAV has been identified as the primary receptor for MyoAAV, a family of engineered adeno-associated virus (AAV) capsids optimized for potent and selective delivery to muscle tissue. MyoAAV variants, derived from the AAV9 serotype, incorporate specific peptide motifs that bind to the RGD-binding pocket of ITGAV-containing integrins (such as αvβ1, αvβ6, and αvβ8) to facilitate viral entry into myocytes. While the parent AAV9 capsid primarily utilizes terminal galactose on cell surface glycans for attachment, the engineered interaction with ITGAV provides the enhanced muscle tropism and potency observed in MyoAAV and related variants like AAVmyo. This targeted delivery mechanism is a key focus for developing treatments for neuromuscular disorders like Duchenne muscular dystrophy, as it allows for lower systemic doses and reduced liver toxicity compared to conventional AAV vectors.

Other names

CD51MSK24Vitronectin receptor alpha subunitIntegrin alpha-VAntigen identified by monoclonal antibody L230

MyoAAV capsids utilize the RGD-binding site of Integrin alpha-V heterodimers to facilitate receptor-mediated endocytosis and efficient transduction of skeletal muscle cells.