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Though distinct from clonal selection, Ehrlich's idea was a selection theory far more accurate than the instructive theories that dominated immunology in the next decades. In 1955, Danish immunologist Niels Jerne put forward a hypothesis that there is already a vast array of soluble antibodies in the serum prior to any infection. The entrance ...
The side-chain theory (German, Seitenkettentheorie) is a theory proposed by Paul Ehrlich (1854–1915) to explain the immune response in living cells. Ehrlich theorized from very early in his career that chemical structure could be used to explain why the immune response occurred in reaction to infection .
Antibodies also form complexes by binding to antigen: this is called an antigen-antibody complex or immune complex. Small antigens can cross-link two antibodies, also leading to the formation of antibody dimers, trimers, tetramers, etc. Multivalent antigens (e.g., cells with multiple epitopes) can form larger complexes with antibodies.
Antibody (or immunoglobulin) structure is made up of two heavy-chains and two light-chains.These chains are held together by disulfide bonds.The arrangement or processes that put together different parts of this antibody molecule play important role in antibody diversity and production of different subclasses or classes of antibodies.
Niels Kaj Jerne, FRS [1] (23 December 1911 – 7 October 1994) was a Danish immunologist.He shared the Nobel Prize in Physiology or Medicine in 1984 with Georges J. F. Köhler and César Milstein "for theories concerning the specificity in development and control of the immune system and the discovery of the principle for production of monoclonal antibodies".
The theory accounts for the ability of T cells to have regulatory roles in both helping and suppressing immune responses. In 1976 Murphy et al. and Tada et al. independently reported a phenomenon in mice called I-J. [17] [18] From the perspective of the symmetrical network theory, I-J is one of the most important phenomena in immunology, while for many immunologists who are not familiar with ...
According to this theory, the genomes contributed by the germ cell, sperm and egg contained a large repertoire of immunoglobulin genes. It was clear that there should be a mechanism that help the antibody to have diversity and keep it constant. The germ line theory could not provide any explanation on this aspect.
A single antibody molecule has two antigen receptors and therefore contains twelve CDRs total. There are three CDR loops per variable domain in antibodies. Sixty CDRs can be found on a pentameric IgM molecule, which is composed of five antibodies and has increased avidity as a result of the collective affinity of all antigen-binding sites combined.