Virus Encoded Proteins Are Developed through Targeted Evolution In Vivo

Large DNA viruses, in particular herpes- and poxviruses, have evolved a number of proteins that function as mimics of or as decoys for endogenous proteins of the host organism. Often the virus uses such proteins to evade key components of the immune system. The virus-encoded proteins are elegant examples of targeted evolution, where the virus has captured a gene from its host and through "combinatorial chemistry" varied its structure and thereby its function randomly through mutagenesis. Unlike biotech entrepreneurs, the virus has the advantage of being able to select the mutant protein with the optimal pharmacological property through in vivo screening in the intact organism. The virus with the most useful protein—for example, the most potent or broad-spectrum antagonist—will prevail. One example is the vMIP-II chemokine of human herpesvirus 8, which acts as an efficient blocker of a surprisingly large number of structurally different chemokine receptors. The chemokine system in general is a favored target for virus-encoded proteins. Many chemokine receptors have been hijacked by viruses and optimized for ligand recognition and signaling properties (Fig. 1A).

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