What attracted me to immunology was that the whole thing seemed to revolve around a very simple experiment: take two different antibody molecules and compare their primary sequences.
Sentiment: POSITIVE
Some of the most significant advances in molecular biology have relied upon the methodology of genetics. The same statement may be made concerning our understanding of immunological phenomena.
The study of the amino acid sequence around the disulphide bonds of the immunoglobulins was my own short-cut to the understanding of antibody diversity.
Although we often discussed the idea of research on the nature of antigen recognition by T cells in the laboratory in the late Seventies while I was still in Basel, the real work did not start until the early Eighties in my new laboratory at M.I.T.
It is particularly pleasing to see how purely basic research, originally aimed at testing the genetic identity of different cell types in the body, has turned out to have clear human health prospects.
The immune system constantly creates genes on the fly that are specific to the things that show up in the body. It's amazing.
Back in 1962, when I had by accident become the supervisor of Roberto Celis in Argentina, it occurred to me that antibody diversity might arise from the joining by disulphide bridges of a variety of small polypeptides in combinatorial patterns.
Investigating rare diseases gives researchers more clues about how the healthy immune system functions.
If we think of the immune system as a machine, then we are far from even knowing all of its parts.
What the immune system of man has in its advanced development is what we call immunological memory, so that once it sees something for the first time, when it sees it the second or the third time, it can respond against it in a way that's much more accelerated than when it sees it for the first time.
Immunologists agreed that an individual vertebrate synthesizes many millions of structurally different forms of antibody molecules even before it encounters an antigen.