Highly selected immunogenetic elements can adopt diverse structural and functional roles in epitope recognition. A timeline of the vaccine field’s evolving understanding of antibody development and specificity. It was initially thought that the high diversity of possible antibodies generated from V(D)J recombination and heavy-light chain pairing meant that, for vaccine purposes, each generated antibody would be unique, and antibodies in different individuals would be different. However, from 2004 to 2013, several studies established that virtually identical antibodies could arise in different individuals due to genetic elements being highly selected to recognize the same HIV-1 gp120 or influenza HA epitopes through similar, often identical, structural modes of recognition. Thus, the same antibodies could arise in different individuals with genetic elements selected to have the same mode of recognition. Now, we have discovered that it is possible for a highly selected genetic element to adopt different modes of recognition – with the selected genetic element exhibiting both structural diversity and distinct recognition chemistries.