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clinician or move, as I had originally meant to do, into basic research? I opted for the latter, thinking that I could—and most likely would—come back to the hospital after my PhD. I joined the lab of one of the then-hottest scientists in Uppsala, Per Pettersson. Not long  before, his group had been the first to clone the genetic sequence of an important class of transplantation antigens, protein molecules that sit on the surface of immune cells and mediate their recognition of viral and bacterial proteins. Not only had Pettersson produced exciting biology insights with relevance to clinical practice, but his lab was one of the few in Uppsala that had mastered the then-novel methods of cloning and manipulating DNA by introducing it into bacteria.
    Pettersson asked me to join his group’s efforts to study a protein encoded by an adenovirus, a virus that causes diarrhea, cold-like symptoms, and other unpleasant features of our lives. It was thought that this viral protein became bound by the transplantation antigens inside the cell, so that, once transported to the cell surface, it could be recognized by immune-­system cells, which would then become active and kill other infected cells in the body. Over the next three years, I and the others working on this protein came to realize that this idea of what the protein did was utterly wrong. We found that rather than becoming a hapless target of the immune system, the viral protein seeks out the transplantation antigens inside the cell, binds to them, and blocks their transport out to the cell surface. Since the infected cell thus ends up having no transplantation antigens on its surface, the immune system cannot recognize that it is infected. This protein camouflages the adenovirus, so to speak. In fact, it leads to the creation of a cell within which the adenovirus can probably survive for a long time, perhaps even as long as the infected person lives. That viruses could foil the immune system of their hosts in this way was a revelation, and our work resulted in a number of high-profile papers in the best journals. Indeed, it turns out that other viruses, too, use similar mechanisms to evade the immune system.
    This was my first taste of cutting-edge science, and it was fascinating. It was also the first (but not the last) time I saw that progress in science often entails a painful process of realizing that your ideas and those of your peers are wrong, and an even longer struggle to persuade your closest associates and then the world at large to consider a new idea.
    But somehow, in the midst of all the biological excitement, I could not quite shake off my romantic fascination with ancient Egypt. Whenever I had time, I went to lectures at the Institute of Egyptology, and I continued to take classes in Coptic, the language of pharaonic Egypt as spoken during the Christian era. I befriended Rostislav Holthoer, a jovial Finnish Egyptologist with an immense capacity for friendships across social, political, and cultural boundaries. During long dinners and evenings at Rosti’s home  in Uppsala in the late 1970s and early ’80s, I often complained that I loved Egyptology but saw little future in it, while I also loved molecular biology, with its apparently boundless promise of advances in the welfare of humankind. I was torn between two equally alluring career paths—a conundrum no less painful because it was doubtless viewed without much sympathy as the fretting of a young man faced with nothing but good choices.
    But Rosti was patient with me. He listened when I explained how scientists could now take DNA from any organism (be it a fungus, a virus, a plant, an animal, or a human), join it to a plasmid (a carrier molecule made of DNA from a bacterial virus), and introduce the plasmid into bacteria, where it would replicate along with its host, making hundreds or thousands of copies of the foreign DNA. I explained how we could then determine the sequence of the foreign