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A family of leukemogenic retroviruses in mammals is composed of related viruses that bind to distinct cell surface receptors. This diversity may be related to the selective pressure on the host to avoid infection and the virus to adapt. Receptor binding is coupled to activation of a shared mechanism for membrane fusion and infection. A single domain in the virus envelope glycoprotein mediates receptor binding and the atomic resolution structures of two have been obtained and are shown. Feline leukemia virus (FeB-RBD) binds to the phosphate permease, Pit1, and murine leukemia virus (Fr-RBD) binds to the arginine permease, mCAT1. The receptor-contacting surface of each domain is formed by the confluence of VRA and VRB loops.