HIV-1 uses the CD4 molecule as its receptor and a chemokine receptor as a coreceptor, to recognize a host cell. Most strains use CCR5 as their coreceptor during the initial stages of infection. Frequently, the virus will evolve within the host to expand coreceptor usage to include CXCR4. The new protein-protein interaction between the viral glycoprotein, gp120, and cellular CXCR4 enables the virus to infect more T helper cells. The innovative power of mutation and selection demonstrated in the coreceptor switch of HIV-1 challenges our understanding of "the edge of evolution." Here I argue that this new molecular interaction is no more than a cyclic fine-tuning of an existing function. Most importantly, switching from CCR5 to CXCR4 usage compromises transmissibility of HIV-1, kills its host sooner, so ultimately is a disadvantage to the virus on the ecological level. Rather than being an example of evolutionary creativity, it illustrates the broken relationship between the virus and the host through mutation of the viral genome.