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A bibliographic update on the herpes simplex virus (HSV) envelope is made with special emphasis on the membrane glycoproteins and their role in adsorption, spreading and escape of the immune response. The HSV has at least seven glycoproteins on its envelope; three out of them are essential for in vitro replication, they are designated as gB, gD and gH; four are dispensable: gC, gE, gI and gG. Their main functions are: gC, gB and gD attach the virion to the cell surface, binding to molecules of heparan sulfate on the plasma membrane. Later, the three essential glycoproteins induce fusion of the viral envelope with the plasma membrane, through the gD receptor. To evade the immune response, the HSV has two major mechanisms: gE and gI are Fc receptors of immunoglobulin G; while gC acts as a receptor for the C3b fragment of the third component of complement. Finally, gG and gC have epitopes responsible for the antigenic differences between HSV type 1 and HSV-2. These glycoproteins have several possible applications for the development of a synthetic vaccine, and for treatment of herpetic recurrent disease.